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1. Body Mass Index Impact on the Long-Term Outcome after Kidney Transplantation in Japanese Patients

Author

Morita, K., Iwami, D., Takada, Y., Higuchi, H., Sasaki, H., Shinohara, N., Morita, K., Iwami, D., Takada, Y., Higuchi, H., Sasaki, H., and Shinohara, N.

Abstract

Objective: While high BMI has negative impact on patients with acute or chronic kidney disease, low BMI is related to mal-nutrition and poor survival in patients on dialysis. On the other hand, pretransplant medical policy recommends recipients to improve their overweight status in order to prevent postoperative surgical complications. We investigated how pretransplant BMI influence postoperative course in Japanese end-stage renal disease patients. Patients and methods: We reviewed 219 patients who underwent kidney transplantation between 1986 and 2014 at our institution. Pediatric recipients (age<20) were excluded. We divided the recipients into 4 groups by BMI (under 18.5, 18.5-21.9, 22.0-24.9, over 25.0). Postoperative complications (wound related and infectious adverse events), allograft rejection, and allograft survival were investigated among the BMI groups. Results: Post-transplant infectious disease was more frequent (5 in 27 cases: 18.5%) in over 25.0 group than any of other BMI groups (0 to 2.1%, p=0.006). Ten year allograft survival rate of over 25.0 group was inferior to that of under 18.5 group (p=0.037). Meanwhile, BMI over 25.0 did not impair graft survival compared to other factors (age, preemptive transplantation, ABO blood type incompatibility and mycophenolate mofetile utilization) in Cox proportional hazards analysis. Conclusion: Overweight (BMI>25.0) in Japanese kidney recipients might affect post-transplant infectious disease occurrence; however, it is not a deteriorating factor for long-term allograft survival., We appreciate the support provided by Kota Ono, MPH. (Translational research and clinical trial center, Hokkaido University Hospital, Japan), who provided expert assistance with statistical analysis. His contribution was involved in the study design, patient enrollment, data collection, analysis, interpretation or preparation of the manuscript. (Kota Ono, Hokkaido University, Department of Biostatistics, Graduate School of Medicine (Hokkaido University Hospital, Clinical Research and Medical Innovation Center, Biostatistics Division))

Published
2017

2. Body Mass Index Impact on the Long-Term Outcome after Kidney Transplantation in Japanese Patients

Author

Morita, K., Iwami, D., Takada, Y., Higuchi, H., Sasaki, H., Shinohara, N., Morita, K., Iwami, D., Takada, Y., Higuchi, H., Sasaki, H., and Shinohara, N.

Abstract

Objective: While high BMI has negative impact on patients with acute or chronic kidney disease, low BMI is related to mal-nutrition and poor survival in patients on dialysis. On the other hand, pretransplant medical policy recommends recipients to improve their overweight status in order to prevent postoperative surgical complications. We investigated how pretransplant BMI influence postoperative course in Japanese end-stage renal disease patients. Patients and methods: We reviewed 219 patients who underwent kidney transplantation between 1986 and 2014 at our institution. Pediatric recipients (age<20) were excluded. We divided the recipients into 4 groups by BMI (under 18.5, 18.5-21.9, 22.0-24.9, over 25.0). Postoperative complications (wound related and infectious adverse events), allograft rejection, and allograft survival were investigated among the BMI groups. Results: Post-transplant infectious disease was more frequent (5 in 27 cases: 18.5%) in over 25.0 group than any of other BMI groups (0 to 2.1%, p=0.006). Ten year allograft survival rate of over 25.0 group was inferior to that of under 18.5 group (p=0.037). Meanwhile, BMI over 25.0 did not impair graft survival compared to other factors (age, preemptive transplantation, ABO blood type incompatibility and mycophenolate mofetile utilization) in Cox proportional hazards analysis. Conclusion: Overweight (BMI>25.0) in Japanese kidney recipients might affect post-transplant infectious disease occurrence; however, it is not a deteriorating factor for long-term allograft survival., We appreciate the support provided by Kota Ono, MPH. (Translational research and clinical trial center, Hokkaido University Hospital, Japan), who provided expert assistance with statistical analysis. His contribution was involved in the study design, patient enrollment, data collection, analysis, interpretation or preparation of the manuscript. (Kota Ono, Hokkaido University, Department of Biostatistics, Graduate School of Medicine (Hokkaido University Hospital, Clinical Research and Medical Innovation Center, Biostatistics Division))

Published
2017

3. Body Mass Index Impact on the Long-Term Outcome after Kidney Transplantation in Japanese Patients

Author

Morita, K., Iwami, D., Takada, Y., Higuchi, H., Sasaki, H., Shinohara, N., Morita, K., Iwami, D., Takada, Y., Higuchi, H., Sasaki, H., and Shinohara, N.

Abstract

Objective: While high BMI has negative impact on patients with acute or chronic kidney disease, low BMI is related to mal-nutrition and poor survival in patients on dialysis. On the other hand, pretransplant medical policy recommends recipients to improve their overweight status in order to prevent postoperative surgical complications. We investigated how pretransplant BMI influence postoperative course in Japanese end-stage renal disease patients. Patients and methods: We reviewed 219 patients who underwent kidney transplantation between 1986 and 2014 at our institution. Pediatric recipients (age<20) were excluded. We divided the recipients into 4 groups by BMI (under 18.5, 18.5-21.9, 22.0-24.9, over 25.0). Postoperative complications (wound related and infectious adverse events), allograft rejection, and allograft survival were investigated among the BMI groups. Results: Post-transplant infectious disease was more frequent (5 in 27 cases: 18.5%) in over 25.0 group than any of other BMI groups (0 to 2.1%, p=0.006). Ten year allograft survival rate of over 25.0 group was inferior to that of under 18.5 group (p=0.037). Meanwhile, BMI over 25.0 did not impair graft survival compared to other factors (age, preemptive transplantation, ABO blood type incompatibility and mycophenolate mofetile utilization) in Cox proportional hazards analysis. Conclusion: Overweight (BMI>25.0) in Japanese kidney recipients might affect post-transplant infectious disease occurrence; however, it is not a deteriorating factor for long-term allograft survival., We appreciate the support provided by Kota Ono, MPH. (Translational research and clinical trial center, Hokkaido University Hospital, Japan), who provided expert assistance with statistical analysis. His contribution was involved in the study design, patient enrollment, data collection, analysis, interpretation or preparation of the manuscript. (Kota Ono, Hokkaido University, Department of Biostatistics, Graduate School of Medicine (Hokkaido University Hospital, Clinical Research and Medical Innovation Center, Biostatistics Division))

Published
2017

4. A point mutation of integrin beta 1 subunit blocks binding of alpha 5 beta 1 to fibronectin and invasin but not recruitment to adhesion plaques.

Author

Takada, Y, Takada, Y, Ylänne, J, Mandelman, D, Puzon, W, Ginsberg, MH, Takada, Y, Takada, Y, Ylänne, J, Mandelman, D, Puzon, W, and Ginsberg, MH

Abstract

A point mutation in a highly conserved region of the beta 1 subunit, Asp130 to Ala (D130A) substitution, abrogates the Arg-Gly-Asp (RGD)-dependent binding of alpha 5 beta 1 to fibronectin (FN) without disrupting gross structure or heterodimer assembly. The D130A mutation also interferes with binding to invasin, a ligand that lacks RGD sequence. In spite of the lack of detectable FN binding by alpha 5 beta 1(D130A), it was recruited to adhesion plaques formed on FN by endogenous hamster receptors. Thus, intact ligand binding function is not required for recruitment of alpha 5 beta 1 to adhesion plaques. Overexpression of beta 1(D130A) partially interfered with endogenous alpha 5 beta 1 function, thus defining a dominant negative beta 1 integrin mutation.

Published
1992

5. A point mutation of integrin beta 1 subunit blocks binding of alpha 5 beta 1 to fibronectin and invasin but not recruitment to adhesion plaques.

Author

Takada, Y, Takada, Y, Ylänne, J, Mandelman, D, Puzon, W, Ginsberg, MH, Takada, Y, Takada, Y, Ylänne, J, Mandelman, D, Puzon, W, and Ginsberg, MH

Abstract

A point mutation in a highly conserved region of the beta 1 subunit, Asp130 to Ala (D130A) substitution, abrogates the Arg-Gly-Asp (RGD)-dependent binding of alpha 5 beta 1 to fibronectin (FN) without disrupting gross structure or heterodimer assembly. The D130A mutation also interferes with binding to invasin, a ligand that lacks RGD sequence. In spite of the lack of detectable FN binding by alpha 5 beta 1(D130A), it was recruited to adhesion plaques formed on FN by endogenous hamster receptors. Thus, intact ligand binding function is not required for recruitment of alpha 5 beta 1 to adhesion plaques. Overexpression of beta 1(D130A) partially interfered with endogenous alpha 5 beta 1 function, thus defining a dominant negative beta 1 integrin mutation.

Published
1992

6. Performance of a Remotely Located Muon Radiography System to Identify the Inner Structure of a Nuclear Plant

Author

Fujii, H., Hara, K., Hashimoto, S., Ito, F., Kakuno, H., Kim, S. H., Kochiyama, M., Nagamine, K., Suzuki, A., Takada, Y., Takahashi, Y., Takasaki, F., Yamashita, S., Fujii, H., Hara, K., Hashimoto, S., Ito, F., Kakuno, H., Kim, S. H., Kochiyama, M., Nagamine, K., Suzuki, A., Takada, Y., Takahashi, Y., Takasaki, F., and Yamashita, S.

Abstract

The performance of a muon radiography system designed to image the inner structure of a nuclear plant located at a distance of 64 m was evaluated. We concluded absence of the fuel in the pressure vessel during the measurement period and succeeded in profiling the fuel material placed in the storage pool. The obtained data also demonstrated the sensitivity of the system to water level changes in the reactor well and the dryer-separator pool. It is expected that the system could reconstruct a 2 m cubic fuel object easily. By operating multiple systems, typically four identical systems, viewing the reactor from different directions simultaneously, detection of a 1 m cubic object should also be achievable within a few month period., Comment: * hara@hep.px.tsukuba.ac.jp; accepted for publication in Progress of Theoretical and Experimental Physics

Published
2013
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7. Graft loss and poor outcomes after living-donor liver transplantation owing to arterioportal shunts caused by liver needle biopsies.

Author

10359789, 80378645, 40252449, Hori, T, Ueda, M, Oike, F, Ogura, Y, Ogawa, K, Nguyen, J H, Yonekawa, Y, Takada, Y, Egawa, H, Yoshizawa, A, Sibulesky, L, Balci, D, Chen, F, Baine, A-M T, Uemoto, S, 10359789, 80378645, 40252449, Hori, T, Ueda, M, Oike, F, Ogura, Y, Ogawa, K, Nguyen, J H, Yonekawa, Y, Takada, Y, Egawa, H, Yoshizawa, A, Sibulesky, L, Balci, D, Chen, F, Baine, A-M T, and Uemoto, S

Abstract

BACKGROUND: Arterioportal shunts (APS) are well-known critical complications after liver transplantation (OLT). The aims of this study were to assess the frequency and causes of APS after OLT and to analyze APS patients with poor outcomes. PATIENTS: We evaluated 1415 OLT recipients retrospectively investigating APS cases. RESULTS: APS were detected in at least 9 patients (0.6%). All patients with APS had a history of posttransplant invasive procedures; percutaneous transhepatic cholangio drainage (n = 6) or needle biopsy (LNB; n = 3). Two patients with poor outcomes showed proximal APS caused by LNBs. The other 7 patients with distal APSs, showed stable conditions. Imaging findings in the 2 proximal APS patients revealed drastic changes in graft hemodynamics. Although they finally underwent re-OLT, their outcomes were poor, owing to fatal complications associated with advanced collaterals. CONCLUSION: We concluded that even careful LNBs can cause APS at unexpected points. Earlier, more aggressive treatments are required, especially for proximal APS patients.

Published
2010

8. System provided with an assistance-controller for assisting an operator of the system, control-operation assisting device, control-operation assisting method, driving-operation assisting device, and driving-operation assisting method

Author

Mulder, M. (author), Abbink, D. (author), Van Paassen, R. (author), Van der Helm, F. (author), Boer, E.R. (author), Takada, Y. (author), Mulder, M. (author), Abbink, D. (author), Van Paassen, R. (author), Van der Helm, F. (author), Boer, E.R. (author), and Takada, Y. (author)

Abstract

A target-travel-path generating circuit calculates a target travel path along which the controlled object can travel in the future from the current controlled object position, an ideal-control-signal calculating circuit calculates a control profile S to travel along the target travel path P, and a difference calculating circuit calculates a difference d between the ideal control magnitude S and a current control magnitude S. An operation system assistance controller controls the operation system based on the magnitude of the calculated difference d to assist the control operation of the operator, the control-operation-state of the operator, the environment-state, and the required operation-precision. Accordingly, it is possible to provide the operator with control operation assistance that is a function of the magnitude of the difference d from an ideal control state, the control-operation-state of the operator, the environment-state, and the required operation-precision, and thus, a control-operation assistance control can be outputted that is suitable for the conditions that characterize the state of the operator, the environment, and the controlled object., Biomechanical Engineering, Mechanical, Maritime and Materials Engineering

Published
2010

9. System provided with an assistance-controller for assisting an operator of the system, control-operation assisting device, control-operation assisting method, driving-operation assisting device, and driving-operation assisting method

Author

Mulder, M. (author), Abbink, D. (author), Van Paassen, R. (author), Van der Helm, F. (author), Boer, E.R. (author), Takada, Y. (author), Mulder, M. (author), Abbink, D. (author), Van Paassen, R. (author), Van der Helm, F. (author), Boer, E.R. (author), and Takada, Y. (author)

Abstract

A target-travel-path generating circuit calculates a target travel path along which the controlled object can travel in the future from the current controlled object position, an ideal-control-signal calculating circuit calculates a control profile S to travel along the target travel path P, and a difference calculating circuit calculates a difference d between the ideal control magnitude S and a current control magnitude S. An operation system assistance controller controls the operation system based on the magnitude of the calculated difference d to assist the control operation of the operator, the control-operation-state of the operator, the environment-state, and the required operation-precision. Accordingly, it is possible to provide the operator with control operation assistance that is a function of the magnitude of the difference d from an ideal control state, the control-operation-state of the operator, the environment-state, and the required operation-precision, and thus, a control-operation assistance control can be outputted that is suitable for the conditions that characterize the state of the operator, the environment, and the controlled object., Biomechanical Engineering, Mechanical, Maritime and Materials Engineering

Published
2010

16. Determination of zinc in aluminium metal by sequential metal vapor elution analysis with radio - frequency induction heating method

Author

Department of Chemistry for Materials, Faculty of Engineering, Mie University, Environmental Preservation Center, Mie University, Takada, Y, Kaneco, S, Katsumata, H, Suzuki, T, Ohta, Department of Chemistry for Materials, Faculty of Engineering, Mie University, Environmental Preservation Center, Mie University, Takada, Y, Kaneco, S, Katsumata, H, Suzuki, T, and Ohta

Abstract

ポスター発表梗概, In recent years, a separation system with a high temperature column (> 990 K), sequential metal vapor elution analysis (SMVEA) has been reported for the separation and analysis of trace metal elements. The advantages of SMVEA are (a) direct separation of metal vapors, (b) rapid analysis without a prior chemical treatment, (c) simplicity, (d) elimination of spectral and chemical interferences occurring in conventional atomic spectrometry such as atomic absorption spectrometry (AAS) and inductively coupled plasma optical emission spectrometry (ICP-OES) and (e) possibility as a powerful accessory of analytical instruments containing mass spectrometry. However, in spite of these attractions, little information on the SMVEA has been reported owing to the technical difficulty of instrumentation. Aluminium in metal contains some trace impurity metals, including zinc, which can affect its quality and numerous papers concerning the determination of zinc in aluminium metal by atomic absorption spectrometry or inductively coupled plasma optical emission spectrometry have been reported. In these methods, however, there are some problems such as poor sensitivity and optical and chemical interferences. In order to eliminate the interferences from aluminum matrix, liquid-liquid extraction, coprecipitation or an ion-exchange method to separate zinc from the matrix has been used. In the present work, the determination of zinc in aluminium metal by sequential metal vapor elution analysis with radio-frequency induction heating method was investigated. The results were in good agreement with the certified value.

Published
2007

21. A critical role of TRPM2 in neuronal cell death hy hydrogen peroxide

Author

60177516, 60362456, 10303843, 80212265, Kaneko, S, Kawakami, S, Hara, Y, Wakamori, M, Itoh, E, Minami, T, Takada, Y, Kume, T, Katsuki, H, Mori, Y, Akaike, A, 60177516, 60362456, 10303843, 80212265, Kaneko, S, Kawakami, S, Hara, Y, Wakamori, M, Itoh, E, Minami, T, Takada, Y, Kume, T, Katsuki, H, Mori, Y, and Akaike, A

Published
2006

23. Time-dependent density-functional theory for the stopping power of an interacting electron gas for slow ions

Author

Universidad del País Vasco, Eusko Jaurlaritza, Ministerio de Ciencia y Tecnología (España), National Research Foundation of Korea, Nazarov, V. U., Pitarke, José María, Kim, C. S., Takada, Y., Universidad del País Vasco, Eusko Jaurlaritza, Ministerio de Ciencia y Tecnología (España), National Research Foundation of Korea, Nazarov, V. U., Pitarke, José María, Kim, C. S., and Takada, Y.

Abstract

Based on the time-dependent density-functional theory, we have derived a rigorous formula for the stopping power of an interacting electron gas for ions in the limit of low projectile velocities. If dynamical correlation between electrons is not taken into account, this formula recovers the corresponding stopping power of noninteracting electrons in an effective Kohn-Sham potential. The correlation effect, specifically the excitonic one in electron-hole pair excitations, however, is found to considerably enhance the stopping power for intermediately charged ions, bringing our theory into good agreement with experiment.

Published
2005

24. Critical cysteine residues for regulation of integrin alpha IIb beta 3 are clustered in the epidermal growth factor domains of the beta 3 subunit

Author

Kamata, T, Kamata, T, Ambo, H, Puzon-McLaughlin, W, Tieu, K K, Handa, M, Ikeda, Y, Takada, Y, Kamata, T, Kamata, T, Ambo, H, Puzon-McLaughlin, W, Tieu, K K, Handa, M, Ikeda, Y, and Takada, Y

Abstract

Chemical or enzymic reduction/oxidation of integrin cysteine residues (e.g. by reducing agents and protein disulphide isomerase) may be a mechanism for regulating integrin function. It has also been proposed that unique cysteine residues in the integrin 3 subunit are involved in the regulation of alphaIIbeta3. In the present study, we studied systematically the role of disulphide bonds in 3 on the ligand-binding function of alphaIIbbeta3 by mutating individual cysteine residues of beta3 to serine. We found that the disulphide bonds that are critical for alphaIIbbeta3 regulation are clustered within the EGF (epidermal growth factor) domains. Interestingly, disrupting only a single disulphide bond in the EGF domains was enough to activate alphaIIbeta3 fully. In contrast, only two (of 13) disulphide bonds tested outside the EGF domains activated aIIbbeta3. These results suggest that the disulphide bonds in the EGF domains should be intact to keep alphaIIbbeta3 in an inactive state, and that there is no unique cysteine residue in the EGF domain critical for regulating the receptor. The cysteine residues in the EGF domains are potential targets for chemical or enzymic reduction.

Published
2004

25. Critical cysteine residues for regulation of integrin alpha IIb beta 3 are clustered in the epidermal growth factor domains of the beta 3 subunit

Author

Kamata, T, Kamata, T, Ambo, H, Puzon-McLaughlin, W, Tieu, K K, Handa, M, Ikeda, Y, Takada, Y, Kamata, T, Kamata, T, Ambo, H, Puzon-McLaughlin, W, Tieu, K K, Handa, M, Ikeda, Y, and Takada, Y

Abstract

Chemical or enzymic reduction/oxidation of integrin cysteine residues (e.g. by reducing agents and protein disulphide isomerase) may be a mechanism for regulating integrin function. It has also been proposed that unique cysteine residues in the integrin 3 subunit are involved in the regulation of alphaIIbeta3. In the present study, we studied systematically the role of disulphide bonds in 3 on the ligand-binding function of alphaIIbbeta3 by mutating individual cysteine residues of beta3 to serine. We found that the disulphide bonds that are critical for alphaIIbbeta3 regulation are clustered within the EGF (epidermal growth factor) domains. Interestingly, disrupting only a single disulphide bond in the EGF domains was enough to activate alphaIIbeta3 fully. In contrast, only two (of 13) disulphide bonds tested outside the EGF domains activated aIIbbeta3. These results suggest that the disulphide bonds in the EGF domains should be intact to keep alphaIIbbeta3 in an inactive state, and that there is no unique cysteine residue in the EGF domain critical for regulating the receptor. The cysteine residues in the EGF domains are potential targets for chemical or enzymic reduction.

Published
2004

28. Measurement of the Running of Effective QED Coupling at Large Momentum Transfer in the Spacelike Region

Author

Odaka, S., Abe, K., Amako, K., Arai, Y., Asano, Y., Chiba, M., Chiba, Y., Daigo, M., Fukawa, M., Fukushima, Y., Haba, J., Hamasaki, H., Hemmi, Y., Higuchi, M., Hirose, T., Homma, Y., Ishihara, N., Iwata, Y., Kanzaki, J., Kikuchi, R., Kondo, T., Korhonen, T. T., Kurashige, H., Matsuda, E. K., Matsui, T., Miyake, K., Mori, S., Nagashima, Y., Nakagawa, Y., Nakamura, T., Nakano, I., Ogawa, K., Ohama, T., Ohsugi, T., Ohyama, H., Okabe, K., Okamoto, A., Ono, A., Pennanen, J., Sakamoto, H., Sakuda, M., Sato, M., Sato, N., Shioden, M., Shirai, J., Sumiyoshi, T., Takada, Y., Takasaki, F., Takita, M., Tamura, N., Tobimatsu, K., Tsuboyama, T., Uehara, S., Unno, Y., Watanabe, T., Watase, Y., Yabuki, F., Yamada, Y., Yamagata, T., Yonezawa, Y., Yoshida, H., Odaka, S., Abe, K., Amako, K., Arai, Y., Asano, Y., Chiba, M., Chiba, Y., Daigo, M., Fukawa, M., Fukushima, Y., Haba, J., Hamasaki, H., Hemmi, Y., Higuchi, M., Hirose, T., Homma, Y., Ishihara, N., Iwata, Y., Kanzaki, J., Kikuchi, R., Kondo, T., Korhonen, T. T., Kurashige, H., Matsuda, E. K., Matsui, T., Miyake, K., Mori, S., Nagashima, Y., Nakagawa, Y., Nakamura, T., Nakano, I., Ogawa, K., Ohama, T., Ohsugi, T., Ohyama, H., Okabe, K., Okamoto, A., Ono, A., Pennanen, J., Sakamoto, H., Sakuda, M., Sato, M., Sato, N., Shioden, M., Shirai, J., Sumiyoshi, T., Takada, Y., Takasaki, F., Takita, M., Tamura, N., Tobimatsu, K., Tsuboyama, T., Uehara, S., Unno, Y., Watanabe, T., Watase, Y., Yabuki, F., Yamada, Y., Yamagata, T., Yonezawa, Y., and Yoshida, H.

Published
1998

29. Heparin and heparan sulfate enhancement of the inhibitory activity of plasminogen activator inhibitor type 1 toward urokinase type plasminogen activator.

Author

Urano, T, Serizawa, K, Takada, Y, Ny, Tor, Takada, A, Urano, T, Serizawa, K, Takada, Y, Ny, Tor, and Takada, A

Abstract

To study effects of glycosaminoglycan on the interaction between two chain urokinase type plasminogen activator (tcu-PA) (EC 3.4.21.31) and plasminogen activator inhibitor type 1 (PAI-1) the second order rate constant (k1) between high molecular weight tcu-PA and active recombinant prokaryotic PAI-1 (rpPAI-1) was determined employing a continuous method using chromogenic substrate S-2444 either in the presence or absence of various kinds of glycosaminoglycans. k1 was (5.9 +/- 1.6).10(6)/mol per s in the absence of effector molecule, and following addition of heparin (1.0 U/ml) k1 was enhanced to (3.22 +/- 0.73).10(7). A significant enhancement of k1 was also obtained by heparan sulfate (1.87 +/- 0.25).10(7). Dermatan sulfate or chondroitin sulfate did not show a significant effect on k1 although a slight decrease was obtained by mono-dextran sulfate (4.2 +/- 1.2).10(6). The intrinsic fluorescence of rpPAI-1 was shown to be slightly increased following addition of heparin (1.49 +/- 0.22%, n = 6), suggesting that heparin may enhance the inhibitory activity of PAI-1 toward tcu-PA both by a template mechanism and by a modification of PAI-1 structure.

Published
1994

30. Distinct functions of integrin alpha and beta subunit cytoplasmic domains in cell spreading and formation of focal adhesions.

Author

Ylänne, J, Ylänne, J, Chen, Y, O'Toole, TE, Loftus, JC, Takada, Y, Ginsberg, MH, Ylänne, J, Ylänne, J, Chen, Y, O'Toole, TE, Loftus, JC, Takada, Y, and Ginsberg, MH

Abstract

Integrin-mediated cell adhesion often results in cell spreading and the formation of focal adhesions. We exploited the capacity of recombinant human alpha IIb beta 3 integrin to endow heterologous cells with the ability to adhere and spread on fibrinogen to study the role of integrin cytoplasmic domains in initiation of cell spreading and focal adhesions. The same constructs were also used to analyze the role of the cytoplasmic domains in maintenance of the fidelity of the integrin repertoire at focal adhesions. Truncation mutants of the cytoplasmic domain of alpha IIb did not interfere with the ability of alpha IIb beta 3 to initiate cell spreading and form focal adhesions. Nevertheless, deletion of the alpha IIb cytoplasmic domain allowed indiscriminate recruitment of alpha IIb beta 3 to focal adhesions formed by other integrins. Truncation of the beta 3 subunit cytoplasmic domain abolished cell spreading mediated by alpha IIb beta 3 and also abrogated recruitment of alpha IIb beta 3 to focal adhesions. This truncation also dramatically impaired the ability of alpha IIb beta 3 to mediate the contraction of fibrin gels. In contrast, the beta 3 subunit cytoplasmic truncation did not reduce the fibrinogen binding affinity of alpha IIb beta 3. Thus, the integrin beta 3 subunit cytoplasmic domain is necessary and sufficient for initiation of cell spreading and focal adhesion formation. Further, the beta 3 cytoplasmic domain is required for the transmission of intracellular contractile forces to fibrin gels. The alpha subunit cytoplasmic domain maintains the fidelity of recruitment of the integrins to focal adhesions and thus regulates their repertoire of integrins.

Published
1993

31. Distinct functions of integrin alpha and beta subunit cytoplasmic domains in cell spreading and formation of focal adhesions.

Author

Ylänne, J, Ylänne, J, Chen, Y, O'Toole, TE, Loftus, JC, Takada, Y, Ginsberg, MH, Ylänne, J, Ylänne, J, Chen, Y, O'Toole, TE, Loftus, JC, Takada, Y, and Ginsberg, MH

Abstract

Integrin-mediated cell adhesion often results in cell spreading and the formation of focal adhesions. We exploited the capacity of recombinant human alpha IIb beta 3 integrin to endow heterologous cells with the ability to adhere and spread on fibrinogen to study the role of integrin cytoplasmic domains in initiation of cell spreading and focal adhesions. The same constructs were also used to analyze the role of the cytoplasmic domains in maintenance of the fidelity of the integrin repertoire at focal adhesions. Truncation mutants of the cytoplasmic domain of alpha IIb did not interfere with the ability of alpha IIb beta 3 to initiate cell spreading and form focal adhesions. Nevertheless, deletion of the alpha IIb cytoplasmic domain allowed indiscriminate recruitment of alpha IIb beta 3 to focal adhesions formed by other integrins. Truncation of the beta 3 subunit cytoplasmic domain abolished cell spreading mediated by alpha IIb beta 3 and also abrogated recruitment of alpha IIb beta 3 to focal adhesions. This truncation also dramatically impaired the ability of alpha IIb beta 3 to mediate the contraction of fibrin gels. In contrast, the beta 3 subunit cytoplasmic truncation did not reduce the fibrinogen binding affinity of alpha IIb beta 3. Thus, the integrin beta 3 subunit cytoplasmic domain is necessary and sufficient for initiation of cell spreading and focal adhesion formation. Further, the beta 3 cytoplasmic domain is required for the transmission of intracellular contractile forces to fibrin gels. The alpha subunit cytoplasmic domain maintains the fidelity of recruitment of the integrins to focal adhesions and thus regulates their repertoire of integrins.

Published
1993

32. In-situ, chemical impedance measurement in the anodic dissolution reaction of pure copper.

Author

Takada Y., Fuwa A., Takada Y., and Fuwa A.

Abstract

The measurements were done with a pure copper anode and one attached with a porous filter; attention was focused on the Warburg impedance, which appears at lower frequencies and represents the diffusion contribution of cupric ions through a boundary layer. The Warburg impedance is larger with the anode with the porous filter that the one without a filter. It is suggested that this impedance may adequately indicate the in-situ properties of the slimes in the copper electrolytic refining process., The measurements were done with a pure copper anode and one attached with a porous filter; attention was focused on the Warburg impedance, which appears at lower frequencies and represents the diffusion contribution of cupric ions through a boundary layer. The Warburg impedance is larger with the anode with the porous filter that the one without a filter. It is suggested that this impedance may adequately indicate the in-situ properties of the slimes in the copper electrolytic refining process.

34. Letter of Intent by the Solenoidal Detector Collaboration to construct and operate a detector at the Superconducting Super Collider

Author

SDC Collaboration, Trilling, GH, Berger, EL, Blair, RE, Dawson, JW, Ekenberg, TL, Derrick, M, Fields, TH, Guarino, V, Hagstrom, RT, Hill, NF, Job, P, Kirk, TBW, May, EN, Nasiatka, J, Nodulman, LJ, Price, LE, Proudfoot, J, Spinka, HM, Talaga, RL, Trost, HJ, Underwood, DG, Wagner, RG, Wicklund, AB, Wu, MM, Johns, KA, Cui, Hua-chuan, Gao, Wen-xiu, Huang, De-qiang, Li, Wei-guo, Mao, Hui-shun, Ni, Hui-ling, Qi, Na-ding, Wang, Tai-jie, Yan, Wu-guang, Ye, Ming-han, Zhao, Wei-ren, Zheng, Liu-sheng, Zhou, Yue-hua, Ming, He Yu, Xi, Lai Chu, Tao, Liu Hong, Qiu, Liu Song, Qiao, Lou Bing, Xiang, Yang Ji, De, Yao Shu, Ju, Zhang Re, Behrends, S, Bensinger, JR, Blocker, C, Kesten, P, Kirsch, L, Povinec, P, Strmen, P, Foster, B, Heath, GP, Cutts, D, Gao, GS, Partridge, R, Alexa, A, Horoi, M, Pantea, D, Pentia, M, Petrascu, C, Weinstein, AJ, Gunion, JF, Pellett, D, Mani, S, Lankford, A, Arisaka, K, Bengtsson, HU, Buchanan, C, Chrisman, D, Cline, D, Hauser, J, Muller, T, Park, J, Roberts, D, Slater, W, Ellison, J, Wimpenny, SJ, Sivertz, M, Thomas, D, DeWitt, J, Dorfan, D, Heusch, C, Hubbard, B, Hutchinson, D, Litke, AL, Lockman, WS, Nilsson, W, O'Shaughnessy, K, Pitzl, D, Rowe, W, Sadrozinski, H, Seiden, A, Spencer, E, Armitage, J, Dixit, MS, Estabrooks, P, Godfrey, S, Losty, M, Mes, H, Oakham, G, O'Neille, M, Kawai, H, Campagneri, C, Contreras, M, Eno, S, Frisch, H, Gross-Pilcher, C, Miller, M, Rosenberg, L, Sanders, H, Shochet, M, Sullivan, G, Baranko, GJ, Cheung, HWK, Cumalat, JP, Erdos, E, Ford, WT, Nauenberg, U, Rankin, P, Schultz, G, Smith, JG, Astakhov, VI, Batyunya, BV, Bischoff, A, Budagov, YA, Chuenko, AM, Dokshin, AI, Finger, M, Gerasimov, SB, Golovatyuk, VM, Gotra, Yu N, Gusar, Yu S, Guzik, Z, Khubua, DI, Ilyin, Yu V, Kashigin, SV, Kharzheev, YN, Kolpakov, IF, Kovalenko, AD, Levchanovsky, FV, Lomakin, YF, Malakhov, AI, Matyushevsky, EA, Omelyanenko, AA, Pakhmutov, Yu S, Panebratsev, YA, Puzynin, IV, Semenov, AA, Senner, AE, Shabunov, AV, Sidorov, VT, Sinaev, AN, Sisakian, AN, Smirnov, V, Spassov, T, Tsyganov, EN, Tyapkin, IA, Vasilev, LA, Velev, GV, Vinogradov, VB, Vodopyanov, AS, Vrba, V, Zanevsky, Yu V, Zhuravlev, NI, Zimin, NI, Zinchenko, AI, Goshaw, AT, Oh, SH, Phillips, TJ, Robertson, WJ, Simpkins, JD, Walker, WD, Amatuni, AC, Vartapetian, GA, Areti, VH, Atac, M, Barsotti, E, Bartoszek, L, Baumbaugh, AE, Beretvas, A, Bernstein, R, Binkley, M, Bross, AD, Clark, AG, Cooper, JW, Denby, BH, Denisenko, KG, Denisenko, NL, Droege, T, Eartly, DP, Elias, JE, Fast, RW, Finley, D, Foster, GW, Freeman, J, Gaines, I, Gourlay, SA, Green, DR, Grimson, J, Grozis, C, Hahn, SR, Harris, RM, Hoff, J, Huth, J, Hylen, J, Kephart, RD, Kilmer, J, Krebs, HJ, Kuzminski, J, Lee, A, Limon, PJ, Martin, PS, Mukerjee, A, Nash, T, Newman-Holmes, C, Para, A, Patrick, J, Plunkett, R, Schmidt, EE, Segler, SL, Stanek, RP, Srefanik, A, Stredde, HJ, Tkaczyk, S, Vidal, R, Wagner, RL, Wands, RH, Yarema, R, Yeh, GP, Yoh, J, Zimmerman, T, Field, R, Harmon, J, Walker, J, Corden, M, Hagopian, V, Johnson, K, Wahl, H, Kawaguchi, M, Yoshida, H, Dvornik, AM, Maksimenko, NB, Brandenburg, G, Feldman, G, Franklin, M, Geer, S, Konigsberg, J, Oliver, J, Sadowski, E, Schlabach, P, Wilson, R, Kenney, C, Parker, S, Chiba, Y, Ohsugi, T, Asai, M, Shioden, M, Goldberg, H, Margulies, S, Solomon, J, Downing, R, Errede, S, Gautier, A, Haney, M, Holloway, L, Karliner, I, Liss, A, O'Halloran, T, Thaler, J, Sheldon, P, Simaitis, V, Wiss, J, Blockus, D, Brabson, B, Dzierba, A, Foster, R, Hanson, G, Lou, X, Luehring, F, Martin, B, Ogren, H, Rust, D, Wente, E, Hauptman, J, Bagger, JA, Barnett, BA, Blumenfeld, BJ, Fisher, PH, Matthews, JAJ, Abe, F, Amako, K, Arai, Y, Doi, Y, Fujii, H, Fukui, Y, Haruyama, T, Ikeda, H, Inaba, S, Inagaki, T, Iwasaki, H, Kabe, S, Kanematsu, N, Kanzaki, J, Kondo, T, Maki, A, Manabe, A, Mishina, M, Noumachi, M, Odaka, S, Ogawa, K, Ohska, TK, Sakai, Y, Sakamoto, H, Sasaki, O, Shinkawa, T, Takaiwa, Y, Terada, S, Tsuboyama, T, Tsukada, K, Ujiie, N, Unno, Y, Watase, Y, Yamamoto, A, Yasu, Y, Krivan, F, Seman, M, Spalek, J, Kikuchi, R, Miyake, K, Abrams, GS, Barbaro-Galtieri, A, Barnett, RM, Cahn, RN, Corradi, CA, Eberhard, PH, Einsweiler, K, Edwards, WR, Ely, R, Gilchriese, MGD, Groom, DE, Haber, C, Hearty, C, Hinchliffe, I, Hoff, M, Jared, R, Kadel, RW, Kadyk, JA, Kleinfelder, S, Levi, ME, Lim, A, Loken, SC, Madden, N, Minamihara, YY, Milgrome, O, Millaud, J, Moore, TL, Nygren, DR, Palounek, APT, Pope, WL, Pripstein, M, Rasson, J, Shapiro, M, Shuman, D, Spieler, HG, Stone, R, Strovink, M, Thur, W, Weidenbach, RC, Wenzel, WA, Ziock, H, Bailey, J, Beck, GA, Dainton, JB, Gabathuler, E, Maxfield, SJ, Smith, G, Baden, AR, Ball, AH, Chang, CY, Fong, DG, Goodman, JA, Hadley, NJ, Jawahery, A, Kellogg, RG, Kunori, S, Skuja, A, Zorn, GT, Ragan, K, Stairs, DG, Amidei, D, Ball, RC, Campbell, M, Chapman, J, De, K, Derwent, P, Gustafson, HR, Hashim, K, Hong, S, Jones, LW, Kim, SB, Longo, MJ, Mann, J, Marcin, MR, Neal, HA, Nitz, D, Roe, BP, Snow, G, Thun, R, Wu, D, Zhang, S, Border, P, Courant, H, Gray, R, Heller, K, Kubota, Y, Marshak, M, Peterson, E, Poling, R, Ruddick, K, Kulchitsky, JA, Moroz, LG, Moore, D, Summers, D, Nakamura, T, Nakamura, M, Niwa, K, Miyano, K, Miyata, H, Bishop, J, Biswas, N, Cason, N, Godfrey, J, Kenney, VP, Piekarz, J, Ruchti, R, Shephard, W, Alley, G, Alsmiller, RG, Alsmiller, FS, Fu, CY, Glover, CW, Mahall, J, Ryan, T, Vandergriff, D, Byslma, B, Durkin, LS, Ling, TY, Park, SK, Romanowski, TA, Tamura, N, Okusawa, T, Takahashi, T, Teramoto, Y, Yoshida, T, Nagashima, Y, Sugimoto, S, Bibby, J, Cashmore, R, Harnew, N, Nickerson, R, Williams, W, Gladney, L, Hollebeek, RJ, Newcomer, M, Van Berg, R, Williams, HH, Armstrong, TA, Hartman, KW, Hasan, A, Heppelmann, SF, Lewis, RA, Minor, ED, Oh, BY, Smith, GA, Toothacker, WS, Whitmore, J, Zhang, Y, Amendolia, R, Bedeschi, F, Bellettini, G, Galeotti, S, Grassman, H, Mangano, ML, Menzione, A, Pauletta, G, Passuello, D, Punzi, G, Ristori, L, Engels, EE, Humanic, T, Shepard, PF, Barnes, VE, Garfinkel, AF, Koltick, DS, Laasanen, AT, McIlwain, R, Miller, DH, Shibata, E, Shipsey, IP, Adams, D, Ahmad, S, Bonner, B, Corcoran, M, Miettinen, H, Mutchler, G, Roberts, J, Skeens, J, Bodek, A, Kanda, S, Lobkowicz, F, Sill, A, Slattery, P, Thorndike, EH, Appolinari, G, Giokaris, N, Goulianos, K, Melese, P, Rusack, R, Vacchi, A, White, S, Devlin, T, Watts, T, Edwards, M, Gee, N, Grayer, G, Bonamy, P, Ernwein, J, Hubbard, R, Le Du, P, Pansart, J -P, Rondeaux, F, Murakami, A, Kobayashi, S, Masuda, K, Tsenov, RV, Iordanov, AB, Bintinger, D, Coupal, D, Fry, A, Johnstad, H, Siegrist, J, Turcotte, M, Aliev, Sh, Kan, S, Khaneles, A, Pak, A, Surin, E, Yuldashev, B, Alimov, M, Gulamov, K, Kaprior, V, Myalkovsky, V, Turdaliev, K, Yuldashev, A, Amaglobeli, NS, Chiladze, BG, Hubua, DI, Salukvadze, RG, Grunhaus, J, Heifetz, R, Levy, A, Barasch, E, Bowcock, TJV, Huson, FR, McIntyre, PM, White, J T, Cantrell, CD, Chaney, RC, Fenyves, EJ, Hammack, H, Orgeron, J, Lowery, WB, Johnson, NP, Higuchi, M, Hoshi, Y, Abe, K, Hasegawa, K, Yuta, H, Kato, S, Nishikawa, K, Homma, S, Miyachi, T, Kaneyuki, K, Tanimori, T, Watanabe, Y, Chiba, M, Hamatsu, R, Hirose, T, Emura, T, Takahashi, K, Bailey, DC, Luste, GJ, Martin, JF, Orr, RS, Prentice, JD, Sinervo, P, Yoon, TS, Fujiwara, I, Funayama, Y, Hara, K, Iinuma, T, Kaneko, T, Kim, S, Kondo, K, Miyashita, S, Morita, Y, Nakano, I, Takano, M, Takikawa, K, Yasuoka, K, Asano, Y, Mori, S, Takada, Y, Kafka, T, Mann, WA, Milburn, RH, Napier, A, Sliwa, K, Lu, B, Mo, LW, Nunamaker, TA, Piilonen, LE, Daigo, M, Davisson, RJ, Liang, G, Lubatti, HJ, Wilkes, RJ, Zhao, T, Bellinger, J, Carlsmith, D, Cherwinka, J, Erwin, A, Feyzi, F, Foudas, C, Lackey, J, Loveless, R, Ott, G, Reeder, DD, Smith, W, Wendt, C, Wu, SL, Frisken, WR, Hasell, D, Koniuk, R, Courtney, W, Fisher, S, Elam, A, Poole, E, Caprio, C, Kapcio, P, Buddle, B, Gerace, T, Arens, JF, Jernigan, JG, Atlas, G, Barkan, Ol, Collins, T, Kramer, G, Pfeiffer, C, Wheeler, B, Wolfe, D, Worley, S, Anderson, EJ, Petroff, MD, Brown, J, Dittert, L, McGinley, W, Nunez, A, Riddle, M, Klokow, D, VanderHave, L, Shapiro, SL, Burke, MA, Einolf, C W, Hackworth, DT, Marschik, D, Scherbarth, DW, Swensrud, RL, Toms, JM, SDC Collaboration, Trilling, GH, Berger, EL, Blair, RE, Dawson, JW, Ekenberg, TL, Derrick, M, Fields, TH, Guarino, V, Hagstrom, RT, Hill, NF, Job, P, Kirk, TBW, May, EN, Nasiatka, J, Nodulman, LJ, Price, LE, Proudfoot, J, Spinka, HM, Talaga, RL, Trost, HJ, Underwood, DG, Wagner, RG, Wicklund, AB, Wu, MM, Johns, KA, Cui, Hua-chuan, Gao, Wen-xiu, Huang, De-qiang, Li, Wei-guo, Mao, Hui-shun, Ni, Hui-ling, Qi, Na-ding, Wang, Tai-jie, Yan, Wu-guang, Ye, Ming-han, Zhao, Wei-ren, Zheng, Liu-sheng, Zhou, Yue-hua, Ming, He Yu, Xi, Lai Chu, Tao, Liu Hong, Qiu, Liu Song, Qiao, Lou Bing, Xiang, Yang Ji, De, Yao Shu, Ju, Zhang Re, Behrends, S, Bensinger, JR, Blocker, C, Kesten, P, Kirsch, L, Povinec, P, Strmen, P, Foster, B, Heath, GP, Cutts, D, Gao, GS, Partridge, R, Alexa, A, Horoi, M, Pantea, D, Pentia, M, Petrascu, C, Weinstein, AJ, Gunion, JF, Pellett, D, Mani, S, Lankford, A, Arisaka, K, Bengtsson, HU, Buchanan, C, Chrisman, D, Cline, D, Hauser, J, Muller, T, Park, J, Roberts, D, Slater, W, Ellison, J, Wimpenny, SJ, Sivertz, M, Thomas, D, DeWitt, J, Dorfan, D, Heusch, C, Hubbard, B, Hutchinson, D, Litke, AL, Lockman, WS, Nilsson, W, O'Shaughnessy, K, Pitzl, D, Rowe, W, Sadrozinski, H, Seiden, A, Spencer, E, Armitage, J, Dixit, MS, Estabrooks, P, Godfrey, S, Losty, M, Mes, H, Oakham, G, O'Neille, M, Kawai, H, Campagneri, C, Contreras, M, Eno, S, Frisch, H, Gross-Pilcher, C, Miller, M, Rosenberg, L, Sanders, H, Shochet, M, Sullivan, G, Baranko, GJ, Cheung, HWK, Cumalat, JP, Erdos, E, Ford, WT, Nauenberg, U, Rankin, P, Schultz, G, Smith, JG, Astakhov, VI, Batyunya, BV, Bischoff, A, Budagov, YA, Chuenko, AM, Dokshin, AI, Finger, M, Gerasimov, SB, Golovatyuk, VM, Gotra, Yu N, Gusar, Yu S, Guzik, Z, Khubua, DI, Ilyin, Yu V, Kashigin, SV, Kharzheev, YN, Kolpakov, IF, Kovalenko, AD, Levchanovsky, FV, Lomakin, YF, Malakhov, AI, Matyushevsky, EA, Omelyanenko, AA, Pakhmutov, Yu S, Panebratsev, YA, Puzynin, IV, Semenov, AA, Senner, AE, Shabunov, AV, Sidorov, VT, Sinaev, AN, Sisakian, AN, Smirnov, V, Spassov, T, Tsyganov, EN, Tyapkin, IA, Vasilev, LA, Velev, GV, Vinogradov, VB, Vodopyanov, AS, Vrba, V, Zanevsky, Yu V, Zhuravlev, NI, Zimin, NI, Zinchenko, AI, Goshaw, AT, Oh, SH, Phillips, TJ, Robertson, WJ, Simpkins, JD, Walker, WD, Amatuni, AC, Vartapetian, GA, Areti, VH, Atac, M, Barsotti, E, Bartoszek, L, Baumbaugh, AE, Beretvas, A, Bernstein, R, Binkley, M, Bross, AD, Clark, AG, Cooper, JW, Denby, BH, Denisenko, KG, Denisenko, NL, Droege, T, Eartly, DP, Elias, JE, Fast, RW, Finley, D, Foster, GW, Freeman, J, Gaines, I, Gourlay, SA, Green, DR, Grimson, J, Grozis, C, Hahn, SR, Harris, RM, Hoff, J, Huth, J, Hylen, J, Kephart, RD, Kilmer, J, Krebs, HJ, Kuzminski, J, Lee, A, Limon, PJ, Martin, PS, Mukerjee, A, Nash, T, Newman-Holmes, C, Para, A, Patrick, J, Plunkett, R, Schmidt, EE, Segler, SL, Stanek, RP, Srefanik, A, Stredde, HJ, Tkaczyk, S, Vidal, R, Wagner, RL, Wands, RH, Yarema, R, Yeh, GP, Yoh, J, Zimmerman, T, Field, R, Harmon, J, Walker, J, Corden, M, Hagopian, V, Johnson, K, Wahl, H, Kawaguchi, M, Yoshida, H, Dvornik, AM, Maksimenko, NB, Brandenburg, G, Feldman, G, Franklin, M, Geer, S, Konigsberg, J, Oliver, J, Sadowski, E, Schlabach, P, Wilson, R, Kenney, C, Parker, S, Chiba, Y, Ohsugi, T, Asai, M, Shioden, M, Goldberg, H, Margulies, S, Solomon, J, Downing, R, Errede, S, Gautier, A, Haney, M, Holloway, L, Karliner, I, Liss, A, O'Halloran, T, Thaler, J, Sheldon, P, Simaitis, V, Wiss, J, Blockus, D, Brabson, B, Dzierba, A, Foster, R, Hanson, G, Lou, X, Luehring, F, Martin, B, Ogren, H, Rust, D, Wente, E, Hauptman, J, Bagger, JA, Barnett, BA, Blumenfeld, BJ, Fisher, PH, Matthews, JAJ, Abe, F, Amako, K, Arai, Y, Doi, Y, Fujii, H, Fukui, Y, Haruyama, T, Ikeda, H, Inaba, S, Inagaki, T, Iwasaki, H, Kabe, S, Kanematsu, N, Kanzaki, J, Kondo, T, Maki, A, Manabe, A, Mishina, M, Noumachi, M, Odaka, S, Ogawa, K, Ohska, TK, Sakai, Y, Sakamoto, H, Sasaki, O, Shinkawa, T, Takaiwa, Y, Terada, S, Tsuboyama, T, Tsukada, K, Ujiie, N, Unno, Y, Watase, Y, Yamamoto, A, Yasu, Y, Krivan, F, Seman, M, Spalek, J, Kikuchi, R, Miyake, K, Abrams, GS, Barbaro-Galtieri, A, Barnett, RM, Cahn, RN, Corradi, CA, Eberhard, PH, Einsweiler, K, Edwards, WR, Ely, R, Gilchriese, MGD, Groom, DE, Haber, C, Hearty, C, Hinchliffe, I, Hoff, M, Jared, R, Kadel, RW, Kadyk, JA, Kleinfelder, S, Levi, ME, Lim, A, Loken, SC, Madden, N, Minamihara, YY, Milgrome, O, Millaud, J, Moore, TL, Nygren, DR, Palounek, APT, Pope, WL, Pripstein, M, Rasson, J, Shapiro, M, Shuman, D, Spieler, HG, Stone, R, Strovink, M, Thur, W, Weidenbach, RC, Wenzel, WA, Ziock, H, Bailey, J, Beck, GA, Dainton, JB, Gabathuler, E, Maxfield, SJ, Smith, G, Baden, AR, Ball, AH, Chang, CY, Fong, DG, Goodman, JA, Hadley, NJ, Jawahery, A, Kellogg, RG, Kunori, S, Skuja, A, Zorn, GT, Ragan, K, Stairs, DG, Amidei, D, Ball, RC, Campbell, M, Chapman, J, De, K, Derwent, P, Gustafson, HR, Hashim, K, Hong, S, Jones, LW, Kim, SB, Longo, MJ, Mann, J, Marcin, MR, Neal, HA, Nitz, D, Roe, BP, Snow, G, Thun, R, Wu, D, Zhang, S, Border, P, Courant, H, Gray, R, Heller, K, Kubota, Y, Marshak, M, Peterson, E, Poling, R, Ruddick, K, Kulchitsky, JA, Moroz, LG, Moore, D, Summers, D, Nakamura, T, Nakamura, M, Niwa, K, Miyano, K, Miyata, H, Bishop, J, Biswas, N, Cason, N, Godfrey, J, Kenney, VP, Piekarz, J, Ruchti, R, Shephard, W, Alley, G, Alsmiller, RG, Alsmiller, FS, Fu, CY, Glover, CW, Mahall, J, Ryan, T, Vandergriff, D, Byslma, B, Durkin, LS, Ling, TY, Park, SK, Romanowski, TA, Tamura, N, Okusawa, T, Takahashi, T, Teramoto, Y, Yoshida, T, Nagashima, Y, Sugimoto, S, Bibby, J, Cashmore, R, Harnew, N, Nickerson, R, Williams, W, Gladney, L, Hollebeek, RJ, Newcomer, M, Van Berg, R, Williams, HH, Armstrong, TA, Hartman, KW, Hasan, A, Heppelmann, SF, Lewis, RA, Minor, ED, Oh, BY, Smith, GA, Toothacker, WS, Whitmore, J, Zhang, Y, Amendolia, R, Bedeschi, F, Bellettini, G, Galeotti, S, Grassman, H, Mangano, ML, Menzione, A, Pauletta, G, Passuello, D, Punzi, G, Ristori, L, Engels, EE, Humanic, T, Shepard, PF, Barnes, VE, Garfinkel, AF, Koltick, DS, Laasanen, AT, McIlwain, R, Miller, DH, Shibata, E, Shipsey, IP, Adams, D, Ahmad, S, Bonner, B, Corcoran, M, Miettinen, H, Mutchler, G, Roberts, J, Skeens, J, Bodek, A, Kanda, S, Lobkowicz, F, Sill, A, Slattery, P, Thorndike, EH, Appolinari, G, Giokaris, N, Goulianos, K, Melese, P, Rusack, R, Vacchi, A, White, S, Devlin, T, Watts, T, Edwards, M, Gee, N, Grayer, G, Bonamy, P, Ernwein, J, Hubbard, R, Le Du, P, Pansart, J -P, Rondeaux, F, Murakami, A, Kobayashi, S, Masuda, K, Tsenov, RV, Iordanov, AB, Bintinger, D, Coupal, D, Fry, A, Johnstad, H, Siegrist, J, Turcotte, M, Aliev, Sh, Kan, S, Khaneles, A, Pak, A, Surin, E, Yuldashev, B, Alimov, M, Gulamov, K, Kaprior, V, Myalkovsky, V, Turdaliev, K, Yuldashev, A, Amaglobeli, NS, Chiladze, BG, Hubua, DI, Salukvadze, RG, Grunhaus, J, Heifetz, R, Levy, A, Barasch, E, Bowcock, TJV, Huson, FR, McIntyre, PM, White, J T, Cantrell, CD, Chaney, RC, Fenyves, EJ, Hammack, H, Orgeron, J, Lowery, WB, Johnson, NP, Higuchi, M, Hoshi, Y, Abe, K, Hasegawa, K, Yuta, H, Kato, S, Nishikawa, K, Homma, S, Miyachi, T, Kaneyuki, K, Tanimori, T, Watanabe, Y, Chiba, M, Hamatsu, R, Hirose, T, Emura, T, Takahashi, K, Bailey, DC, Luste, GJ, Martin, JF, Orr, RS, Prentice, JD, Sinervo, P, Yoon, TS, Fujiwara, I, Funayama, Y, Hara, K, Iinuma, T, Kaneko, T, Kim, S, Kondo, K, Miyashita, S, Morita, Y, Nakano, I, Takano, M, Takikawa, K, Yasuoka, K, Asano, Y, Mori, S, Takada, Y, Kafka, T, Mann, WA, Milburn, RH, Napier, A, Sliwa, K, Lu, B, Mo, LW, Nunamaker, TA, Piilonen, LE, Daigo, M, Davisson, RJ, Liang, G, Lubatti, HJ, Wilkes, RJ, Zhao, T, Bellinger, J, Carlsmith, D, Cherwinka, J, Erwin, A, Feyzi, F, Foudas, C, Lackey, J, Loveless, R, Ott, G, Reeder, DD, Smith, W, Wendt, C, Wu, SL, Frisken, WR, Hasell, D, Koniuk, R, Courtney, W, Fisher, S, Elam, A, Poole, E, Caprio, C, Kapcio, P, Buddle, B, Gerace, T, Arens, JF, Jernigan, JG, Atlas, G, Barkan, Ol, Collins, T, Kramer, G, Pfeiffer, C, Wheeler, B, Wolfe, D, Worley, S, Anderson, EJ, Petroff, MD, Brown, J, Dittert, L, McGinley, W, Nunez, A, Riddle, M, Klokow, D, VanderHave, L, Shapiro, SL, Burke, MA, Einolf, C W, Hackworth, DT, Marschik, D, Scherbarth, DW, Swensrud, RL, and Toms, JM

35. Expression of interest by the Solenoidal Detector Collaboration to construct and operate a detector at the Superconducting Super Collider

Author

SDC Collaboration, Trilling, GH, Berger, EL, Blair, RE, Dawson, JW, Derrick, M, Fields, TH, Hagstrom, RT, Hill, NF, Job, P, Kirk, TB, May, EN, Nodulman, LJ, Price, LE, Proudfoot, J, Spinka, HM, Talaga, RL, Trost, HJ, Underwood, DG, Wagner, RG, Wicklund, A B, Johns, KA, Behrends, S, Bensinger, JR, Blocker, C, Kesten, P, Kirsch, L, Povinec, P, Strmen, P, Foster, B, Heath, GP, Cutts, D, Partridge, R, Pellett, D, Arisaka, K, Chrisman, D, Cline, D, Park, J, Roberts, D, Slater, W, Yamamoto, H, Ellison, J, Wimpenny, SJ, Sivertz, M, Thomas, D, Dorfan, D, Heusch, C, Hubbard, B, Litke, AL, Lockman, WS, Pitzl, D, Sadrozinski, H, Seiden, A, Kawai, H, Campagneri, C, Eno, S, Frisch, H, Gross-Pilcher, C, Miller, M, Rosenberg, L, Shochet, M, Sullivan, G, Baranko, GJ, Carr, J, Cheung, HWK, Cumalat, JP, Ford, WT, Nauenberg, U, Rankin, P, Smith, JG, Astakhov, VI, Batyunya, BV, Bischoff, A, Budagov, YA, Denisenko, KG, Denisenko, NL, Gerasimov, SB, Golovatyuk, VM, Guzik, Z, Khubua, DI, Kadyrov, R, Kharzjeev, YN, Kolpakov, IF, Kovalenko, AD, Levchanovsky, FV, Lomakin, YF, Malakhov, AI, Omelyanenko, AA, Panebratsev, YA, Puzynin, IV, Semenov, AA, Senner, AE, Sidorov, VT, Sinaev, AN, Sisakian, AN, Smirnov, V, Spassof, T, Tsyganov, EN, Tyapkin, IA, Velev, GV, Vinogradov, VB, Vodopyanov, AS, Brba, V, Zanevsky, Yu V, Zhuravlev, NI, Zimin, NI, Zinchenko, AI, Fortney, LR, Goshaw, AT, Kowald, W, Oh, SH, Robertson, WJ, Walker, WD, Amatuni, AC, Vartapetian, GA, Amidei, D, Atac, M, Baumbaugh, AE, Beretvas, A, Bernstein, R, Binkley, M, Bross, AD, Clark, AG, Cooper, JW, Eartly, DP, Elias, JE, Fast, R W, Finley, D, Foster, G W, Freeman, J, Gaines, I, Gourlay, SA, Green, DR, Hahn, SR, Harris, RM, Hauser, J, Huth, J, Kephart, RD, Kuzminski, J, Martin, PS, Mishina, M, Mukerjee, A, Nash, T, Newman-Holmes, C, Para, A, Patrick, J, Plunkett, R, Schmidt, EE, Segler, SL, Tkaczyk, S, Vidal, R, Wagner, RL, Yeh, GP, Yoh, J, Field, R, Harmon, J, Walker, J, Corden, M, Hagopian, V, Johnson, K, Wahl, H, Kawaguchi, M, Yoshida, H, Dvornik, AM, Maksimenko, NB, Brandenburg, G, Feldman, G, Franklin, M, Geer, S, Konigsberg, J, Oliver, J, Phillips, T, Wilson, R, Kenney, C, Parker, S, Chiba, Y, Ohsugi, T, Asai, M, Shioden, M, Goldberg, H, Margulies, S, Solomon, J, Downing, R, Errede, S, Gautier, A, Haney, M, Holloway, L, Karliner, I, Liss, A, O'Halloran, T, Thaler, J, Sheldon, P, Simaitis, V, Wiss, J, Blockus, D, Brabson, B, Dzierba, A, Hanson, G, Lou, X, Ogren, H, Rust, D, Hauptman, J, Bagger, JA, Barnett, BA, Blumenfeld, BJ, Fisher, PH, Matthews, JAJ, Abe, F, Amako, K, Arai, Y, Doi, Y, Fujii, H, Fukui, Y, Haruyama, T, Ikeda, H, Ikeda, M, Inaba, S, Inagaki, T, Iwasaki, H, Kabe, S, Kanzaki, J, Kim, SK, Kondo, T, Maki, A, Manabe, A, Noumachi, M, Odaka, S, Ogawa, K, Sakai, Y, Sakamoto, H, Shinkawa, T, Takaiwa, Y, Terada, S, Tsuboyama, T, Tsukada, K, Ujiie, N, Unno, Y, Watase, Y, Yamamoto, A, Yasu, Y, Krivan, F, Seman, M, Spalek, J, Kikuchi, R, Miyake, K, Abrams, GS, Barbaro-Galtieri, A, Barnett, RM, Cahn, RN, Eberhard, PH, Einsweiler, K, Ely, R, Gilchriese, MGD, Groom, DE, Haber, C, Hearty, C, Hinchliffe, I, Kadel, RW, Kadyk, JA, Levi, ME, Limon, PJ, Loken, SC, Nygren, DR, Palounek, APT, Pripstein, M, Shapiro, M, Siegrist, JL, Spieler, HG, Strovink, M, Wang, EM, Wenzel, WA, Bailey, J, Beck, GA, Dainton, JB, Gabathuler, E, Maxfield, SJ, Baden, AR, Ball, AH, Chang, CY, Fong, DG, Goodman, JA, Hadley, NJ, Jawahery, A, Kellogg, RG, Kunori, S, Skuja, A, Zorn, GT, Ball, RC, Campbell, M, Chapman, J, Gustafson, HR, Hong, S, Jones, LW, Longo, MJ, Marcin, MR, Neal, HA, Nitz, D, Roe, BP, Snow, G, Thun, R, Border, P, Courant, H, Heller, K, Kubota, Y, Marshak, M, Peterson, E, Poling, R, Ruddick, K, Kulchitsky, JA, Moroz, LG, Moore, D, Summers, D, Nakamura, T, Nakamura, M, Niwa, K, Miyano, K, Miyata, H, Bishop, J, Biswas, N, Cason, N, Godfrey, J, Kenney, VP, Piekarz, J, Ruchti, R, Shephard, W, Alley, G, Alsmiller, RG, Alsmiller, FS, Fu, CY, Glover, CW, Vandergriff, D, Byslma, B, Durkin, LS, Ling, TY, Park, SK, Romanowski, TA, Tamura, N, Okusawa, T, Takahashi, T, Teramoto, Y, Yoshida, T, Nagashima, Y, Sugimoto, S, Cashmore, R, Harnew, N, Nickerson, R, Weidberg, A, Williams, W, Gladney, L, Hollebeek, RJ, Newcomer, M, Ragan, KJ, Sinervo, PK, Williams, HH, Armstrong, TA, Hartman, KW, Hasan, A, Heppelmann, SF, Lewis, RA, Minor, ED, Oh, BY, Smith, GA, Toothacker, WS, Whitmore, J, Amendolia, R, Bedeschi, F, Bellettini, G, Galeotti, S, Grassman, H, Mangano, ML, Menzione, A, Pauletta, G, Passuello, D, Punzi, G, Ristori, L, Engels, EE, Humanic, T, Mani, S, Shepard, PF, Barnes, VE, Garfinkel, AF, Koltick, DS, Laasanen, AT, McIlwain, R, Miller, DH, Shibata, E, Shipsey, IP, Adams, D, Ahmad, S, Bonner, B, Corcoran, M, Miettinen, H, Mutchler, G, Roberts, J, Skeens, J, Bodek, A, Lobkowicz, F, Sill, A, Slattery, P, Thorndike, EH, Giodaris, N, Goulianos, K, Melese, P, Rusack, R, White, S, Devlin, T, Watts, T, Gee, N, Harvey, JA, Murakami, A, Kobayashi, S, Masuda, K, Tsenov, RV, Iordanov, AB, Lankford, A, Bintinger, D, Johnstad, H, Aliev, Sh, Alimov, M, Gulamov, K, Kan, S, Kaprior, V, Khaneles, A, Myalkovsky, V, Pak, A, Surlin, E, Turdaliev, K, Yuldashev, A, Yuldashev, B, Amaglobeli, NS, Chiladze, BG, Hubua, DI, Salukvadze, RG, McIntyre, PM, Bowcock, TJV, Huson, FR, White, J T, Chaney, RC, Fenyves, EJ, Hammack, H, Orgeron, J, Lowery, WB, Johnson, NP, Higuchi, M, Hoshi, Y, Abe, K, Hasegawa, K, Yuta, H, Kato, S, Nishikawa, K, Homma, S, Miyachi, T, Watanabe, Y, Tanimori, T, Chiba, M, Hamatsu, R, Hirose, T, Kitamura, S, Emura, T, Takahashi, K, Funayama, Y, Hara, K, Kanda, S, Kaneko, T, Kim, S, Kondo, K, Mimashi, T, Miyashita, S, Morita, Y, Nakano, I, Sakurabata, H, Takikawa, K, Yasuoka, K, Asano, Y, Mori, S, Takada, Y, Kafka, T, Mann, WA, Milburn, RH, Napier, A, Sliwa, K, Lu, B, Mo, LW, Piilonen, LE, Daigo, M, Davisson, RJ, Liang, G, Lubatti, HJ, Wilkes, RJ, Zhao, T, Bellinger, J, Carlsmith, D, Erwin, A, Foudas, C, Handler, R, Loveless, R, Ott, G, Reeder, DD, Smith, W, Wendt, C, Wu, SL, SDC Collaboration, Trilling, GH, Berger, EL, Blair, RE, Dawson, JW, Derrick, M, Fields, TH, Hagstrom, RT, Hill, NF, Job, P, Kirk, TB, May, EN, Nodulman, LJ, Price, LE, Proudfoot, J, Spinka, HM, Talaga, RL, Trost, HJ, Underwood, DG, Wagner, RG, Wicklund, A B, Johns, KA, Behrends, S, Bensinger, JR, Blocker, C, Kesten, P, Kirsch, L, Povinec, P, Strmen, P, Foster, B, Heath, GP, Cutts, D, Partridge, R, Pellett, D, Arisaka, K, Chrisman, D, Cline, D, Park, J, Roberts, D, Slater, W, Yamamoto, H, Ellison, J, Wimpenny, SJ, Sivertz, M, Thomas, D, Dorfan, D, Heusch, C, Hubbard, B, Litke, AL, Lockman, WS, Pitzl, D, Sadrozinski, H, Seiden, A, Kawai, H, Campagneri, C, Eno, S, Frisch, H, Gross-Pilcher, C, Miller, M, Rosenberg, L, Shochet, M, Sullivan, G, Baranko, GJ, Carr, J, Cheung, HWK, Cumalat, JP, Ford, WT, Nauenberg, U, Rankin, P, Smith, JG, Astakhov, VI, Batyunya, BV, Bischoff, A, Budagov, YA, Denisenko, KG, Denisenko, NL, Gerasimov, SB, Golovatyuk, VM, Guzik, Z, Khubua, DI, Kadyrov, R, Kharzjeev, YN, Kolpakov, IF, Kovalenko, AD, Levchanovsky, FV, Lomakin, YF, Malakhov, AI, Omelyanenko, AA, Panebratsev, YA, Puzynin, IV, Semenov, AA, Senner, AE, Sidorov, VT, Sinaev, AN, Sisakian, AN, Smirnov, V, Spassof, T, Tsyganov, EN, Tyapkin, IA, Velev, GV, Vinogradov, VB, Vodopyanov, AS, Brba, V, Zanevsky, Yu V, Zhuravlev, NI, Zimin, NI, Zinchenko, AI, Fortney, LR, Goshaw, AT, Kowald, W, Oh, SH, Robertson, WJ, Walker, WD, Amatuni, AC, Vartapetian, GA, Amidei, D, Atac, M, Baumbaugh, AE, Beretvas, A, Bernstein, R, Binkley, M, Bross, AD, Clark, AG, Cooper, JW, Eartly, DP, Elias, JE, Fast, R W, Finley, D, Foster, G W, Freeman, J, Gaines, I, Gourlay, SA, Green, DR, Hahn, SR, Harris, RM, Hauser, J, Huth, J, Kephart, RD, Kuzminski, J, Martin, PS, Mishina, M, Mukerjee, A, Nash, T, Newman-Holmes, C, Para, A, Patrick, J, Plunkett, R, Schmidt, EE, Segler, SL, Tkaczyk, S, Vidal, R, Wagner, RL, Yeh, GP, Yoh, J, Field, R, Harmon, J, Walker, J, Corden, M, Hagopian, V, Johnson, K, Wahl, H, Kawaguchi, M, Yoshida, H, Dvornik, AM, Maksimenko, NB, Brandenburg, G, Feldman, G, Franklin, M, Geer, S, Konigsberg, J, Oliver, J, Phillips, T, Wilson, R, Kenney, C, Parker, S, Chiba, Y, Ohsugi, T, Asai, M, Shioden, M, Goldberg, H, Margulies, S, Solomon, J, Downing, R, Errede, S, Gautier, A, Haney, M, Holloway, L, Karliner, I, Liss, A, O'Halloran, T, Thaler, J, Sheldon, P, Simaitis, V, Wiss, J, Blockus, D, Brabson, B, Dzierba, A, Hanson, G, Lou, X, Ogren, H, Rust, D, Hauptman, J, Bagger, JA, Barnett, BA, Blumenfeld, BJ, Fisher, PH, Matthews, JAJ, Abe, F, Amako, K, Arai, Y, Doi, Y, Fujii, H, Fukui, Y, Haruyama, T, Ikeda, H, Ikeda, M, Inaba, S, Inagaki, T, Iwasaki, H, Kabe, S, Kanzaki, J, Kim, SK, Kondo, T, Maki, A, Manabe, A, Noumachi, M, Odaka, S, Ogawa, K, Sakai, Y, Sakamoto, H, Shinkawa, T, Takaiwa, Y, Terada, S, Tsuboyama, T, Tsukada, K, Ujiie, N, Unno, Y, Watase, Y, Yamamoto, A, Yasu, Y, Krivan, F, Seman, M, Spalek, J, Kikuchi, R, Miyake, K, Abrams, GS, Barbaro-Galtieri, A, Barnett, RM, Cahn, RN, Eberhard, PH, Einsweiler, K, Ely, R, Gilchriese, MGD, Groom, DE, Haber, C, Hearty, C, Hinchliffe, I, Kadel, RW, Kadyk, JA, Levi, ME, Limon, PJ, Loken, SC, Nygren, DR, Palounek, APT, Pripstein, M, Shapiro, M, Siegrist, JL, Spieler, HG, Strovink, M, Wang, EM, Wenzel, WA, Bailey, J, Beck, GA, Dainton, JB, Gabathuler, E, Maxfield, SJ, Baden, AR, Ball, AH, Chang, CY, Fong, DG, Goodman, JA, Hadley, NJ, Jawahery, A, Kellogg, RG, Kunori, S, Skuja, A, Zorn, GT, Ball, RC, Campbell, M, Chapman, J, Gustafson, HR, Hong, S, Jones, LW, Longo, MJ, Marcin, MR, Neal, HA, Nitz, D, Roe, BP, Snow, G, Thun, R, Border, P, Courant, H, Heller, K, Kubota, Y, Marshak, M, Peterson, E, Poling, R, Ruddick, K, Kulchitsky, JA, Moroz, LG, Moore, D, Summers, D, Nakamura, T, Nakamura, M, Niwa, K, Miyano, K, Miyata, H, Bishop, J, Biswas, N, Cason, N, Godfrey, J, Kenney, VP, Piekarz, J, Ruchti, R, Shephard, W, Alley, G, Alsmiller, RG, Alsmiller, FS, Fu, CY, Glover, CW, Vandergriff, D, Byslma, B, Durkin, LS, Ling, TY, Park, SK, Romanowski, TA, Tamura, N, Okusawa, T, Takahashi, T, Teramoto, Y, Yoshida, T, Nagashima, Y, Sugimoto, S, Cashmore, R, Harnew, N, Nickerson, R, Weidberg, A, Williams, W, Gladney, L, Hollebeek, RJ, Newcomer, M, Ragan, KJ, Sinervo, PK, Williams, HH, Armstrong, TA, Hartman, KW, Hasan, A, Heppelmann, SF, Lewis, RA, Minor, ED, Oh, BY, Smith, GA, Toothacker, WS, Whitmore, J, Amendolia, R, Bedeschi, F, Bellettini, G, Galeotti, S, Grassman, H, Mangano, ML, Menzione, A, Pauletta, G, Passuello, D, Punzi, G, Ristori, L, Engels, EE, Humanic, T, Mani, S, Shepard, PF, Barnes, VE, Garfinkel, AF, Koltick, DS, Laasanen, AT, McIlwain, R, Miller, DH, Shibata, E, Shipsey, IP, Adams, D, Ahmad, S, Bonner, B, Corcoran, M, Miettinen, H, Mutchler, G, Roberts, J, Skeens, J, Bodek, A, Lobkowicz, F, Sill, A, Slattery, P, Thorndike, EH, Giodaris, N, Goulianos, K, Melese, P, Rusack, R, White, S, Devlin, T, Watts, T, Gee, N, Harvey, JA, Murakami, A, Kobayashi, S, Masuda, K, Tsenov, RV, Iordanov, AB, Lankford, A, Bintinger, D, Johnstad, H, Aliev, Sh, Alimov, M, Gulamov, K, Kan, S, Kaprior, V, Khaneles, A, Myalkovsky, V, Pak, A, Surlin, E, Turdaliev, K, Yuldashev, A, Yuldashev, B, Amaglobeli, NS, Chiladze, BG, Hubua, DI, Salukvadze, RG, McIntyre, PM, Bowcock, TJV, Huson, FR, White, J T, Chaney, RC, Fenyves, EJ, Hammack, H, Orgeron, J, Lowery, WB, Johnson, NP, Higuchi, M, Hoshi, Y, Abe, K, Hasegawa, K, Yuta, H, Kato, S, Nishikawa, K, Homma, S, Miyachi, T, Watanabe, Y, Tanimori, T, Chiba, M, Hamatsu, R, Hirose, T, Kitamura, S, Emura, T, Takahashi, K, Funayama, Y, Hara, K, Kanda, S, Kaneko, T, Kim, S, Kondo, K, Mimashi, T, Miyashita, S, Morita, Y, Nakano, I, Sakurabata, H, Takikawa, K, Yasuoka, K, Asano, Y, Mori, S, Takada, Y, Kafka, T, Mann, WA, Milburn, RH, Napier, A, Sliwa, K, Lu, B, Mo, LW, Piilonen, LE, Daigo, M, Davisson, RJ, Liang, G, Lubatti, HJ, Wilkes, RJ, Zhao, T, Bellinger, J, Carlsmith, D, Erwin, A, Foudas, C, Handler, R, Loveless, R, Ott, G, Reeder, DD, Smith, W, Wendt, C, and Wu, SL

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