36 results on '"Bromme, Dieter"'
Search Results
2. Lycopene Improves Bone Quality and Regulates AGE/RAGE/NF-кB Signaling Pathway in High-Fat Diet-Induced Obese Mice
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Xia, Bingke, primary, Zhu, Ruyuan, additional, Zhang, Hao, additional, Chen, Beibei, additional, Liu, Yage, additional, Dai, Xuan, additional, Ye, Zimengwei, additional, Zhao, Dandan, additional, Mo, Fangfang, additional, Gao, Sihua, additional, Wang, Xiang-Dong, additional, Bromme, Dieter, additional, Wang, Lili, additional, Wang, Xinxiang, additional, and Zhang, Dongwei, additional
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- 2022
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3. Identification and activity of a lower eukaryotic serine proteinase inhibitor (Serpin) from Cyanea capillata: analysis of a jellyfish serpin, jellypin
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Cole, Elisabeth B., Cataltepe, Sule, Pak, Stephen C, Mills, David R, Silverman, Gary A., Luke, Cliff J., Miller, David, Rometo, David, Greenberg, Robert M., and Bromme, Dieter
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Serpens (Constellation) -- Research ,Serine -- Research ,Proteases -- Research ,Biological sciences ,Chemistry - Published
- 2004
4. Role of Cathepsin K, L and S in Blood Vessel Remodeling
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O., Andriy, primary and Bromme, Dieter, additional
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- 2011
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5. Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design
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Lecaille, Fabien, Kaleta, Jadwiga, and Bromme, Dieter
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Enzymes -- Research ,Endoplasmic reticulum -- Research ,Cysteine proteinases -- Research ,Chemistry - Abstract
The biochemisry of human and parasite cysteine proteases and recent developments in inhibitor-design and their role in physiology and pathology is focused. Papain-like cysteine proteases are expressed as preproenzymes and are synthesized at the rough endoplasmic reticulum.
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- 2002
6. Inhibition of cathepsin K with lysosomotropic macromolecular inhibitors
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Wang, Dong, Pechar, Michal, Li, Weijie, Kopeckova, Pavla, Bromme, Dieter, and Kopecek, Jindrich
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Biochemistry -- Research ,Chemical inhibitors -- Physiological aspects ,Cathepsins -- Physiological aspects ,Lysosomes -- Physiological aspects ,Macromolecules -- Physiological aspects ,Enzymes -- Physiological aspects ,Biological sciences ,Chemistry - Abstract
Research has been conducted on the cathepsin K, responsible for the bone protein matrix degradation. The effect of the cathepsin K inhibitors on the marcomolecular carriers has been investigated and the results are reported.
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- 2002
7. Selective inhibition of the collagenolytic activity of human cathepsin K by altering its S2 subsite specificity
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Lecaille, Fabien, Choe, Youngchool, Brandt, Wolfgang, Li, Zhenqiang, Craik, Charles S., and Bromme, Dieter
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Biochemistry -- Research ,Cathepsins -- Physiological aspects ,Chemical inhibitors -- Physiological aspects ,Collagen -- Physiological aspects ,Cysteine -- Physiological aspects ,Biological sciences ,Chemistry - Abstract
Research has been conducted on the cathepsins K. The ability of this casepsin to cleave interstitial collagens in their triple helical domains has been investigated via the study of the human casepsin K's S2 pocket engineered into the casepsin L-like subsite and the results are reported.
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- 2002
8. Evidence that serpin architecture intrinsically supports papain-like cysteine protease inhibition: engineering alpha(sub)1-antitrypsin to inhibit cathepsin proteases
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Irving, James A., Pike, Robert N., Dai, Weiwen, Bromme, Dieter, Worrall, D. Margaret, Silverman, Gary A., Coetzer, Theresa H.T., Dennison, Clive, Bottomley, Stephen P., and Whisstock, James C.
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Proteases -- Research ,Trypsin inhibitors -- Analysis ,Structure-activity relationships (Biochemistry) -- Analysis ,Enzyme inhibitors -- Analysis ,Biological sciences ,Chemistry - Abstract
Research reveals that chimeras of the alpha(sub)1-antitrypsin efficiently inhibit papain-like cysteine protease and that the inhibition is a function of the length of the reactive center loop. Data indicate that the inhibition requires insertion of the reactive center loop into the body of the cysteine protease body.
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- 2002
9. The serpin SQN-5 is a dual mechanistic-class inhibitor of serine and cysteine proteinases
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Al-Khunaizi, May, Luke, Cliff J., Askew, Yuko S., Pak, Stephen C., Askew, David J., Cataltepe, Sule, Miller, David, Mills, David R., Tsu, Christopher, Bromme, Dieter, Irving, James A., Whisstock, James C., and Silverman, Gary A.
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Enzyme inhibitors -- Analysis ,Proteolysis -- Analysis ,Enzymes -- Structure-activity relationship ,Mechanical chemistry -- Research ,Biological sciences ,Chemistry - Abstract
The mouse SQN-5 serpin inhibits both chymotrypsin-like serine and the papain-like cysteine proteinases through a reactive site loop-dependent inhibitory mechanism. Data indicate that the human and mouse serpin genes seem to have originated from a common ancestor.
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- 2002
10. TIN-ag-RP, a novel catalytically inactive cathepsin B-related protein with EGF domains, is predominantly expressed in vascular smooth muscle cells
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Wex, Thomas, Lipyansky, Alex, Bromme, Natascha C., Wex, Heike, Guan, Xiu Qin, and Bromme, Dieter
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Kidneys -- Physiological aspects ,Protein biosynthesis -- Physiological aspects ,Vascular smooth muscle -- Physiological aspects ,Cytoskeletal proteins -- Analysis ,Biological sciences ,Chemistry - Abstract
A novel protein resembling cathepsin-B and showing about 46% identity to the human tubulointerstitial nephritis antigen (TIN-ag) is isolated and termed as TIN-ag-related protein. The protein detected in vascular smooth muscle cells of various tissues, excepting uterine cells, is a glycosylated secretory protein possessing epidermal growth factor-like domains.
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- 2001
11. Simple modifications of the serpin reactive site loop convert SCCA2 into a cysteine proteinase inhibitor: a critical role for the P3' proline in facilitating RSL cleavage
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Luke, Cliff, Schick, Charles, Tsu, Christopher, Whisstock, James C., Irving, James A., Bromme, Dieter, Juliano, Luiz, Shi, Guo-Ping, Chapman, Harold A., and Silverman, Gary A.
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Biochemistry -- Research ,Cysteine proteinases -- Research ,Scission (Chemistry) -- Analysis ,Antigens -- Research ,Squamous cell carcinoma -- Causes of ,Biological sciences ,Chemistry - Abstract
Research has been conducted on the members of the serpine family human squamous cell carcinoma antigens (SCCA) 1 and 2. The SCCA1 inhibition mechanism is described.
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- 2000
12. Collagenolytic activity of cathepsin K is specifically modulated by cartilage-resident chondroitin sulfates
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Li, Zhenqiang, Hou, Wu-Shiun, and Bromme, Dieter
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Collagen -- Physiological aspects ,Chondroitin -- Research ,Bone diseases -- Physiological aspects ,Cysteine proteinases -- Research ,Biological sciences ,Chemistry - Abstract
Results show that the collagenolytic activity and stability of cathepsin K is determined specifically by chondroitin -4- sulfate (C-4S) present in cartilage. Data also indicate that the cumulative activity of cathepsin K increased by 200 fold in the presence of C-4S.
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- 2000
13. Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization
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Bromme, Dieter, Li, Zhenqiang, Barnes, Michel, and Mehler, Ernest
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Proteases -- Research ,Cysteine proteinases -- Research ,Biological sciences ,Chemistry - Abstract
Research was conducted to examine the functional expression and enzymatic characterization of the novel protease, human cathepsin V, its differences in the electrostatic potential to cathepsin L, its tissue distribution in immune system-related tissues and its chromosomal localization. Results indicate that cathepsin V may likely have an important role to play in thymic self-antigen presentation and may represent a novel target for the treatment of autoimmune disorders.
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- 1999
14. Cross-class inhibition of the cysteine proteinases cathepsins K, L, and S by the serpin squamous cell carcinoma antigen 1: a kinetic analysis
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Schick, Charles, Pemberton, Philip A., Shi, Guo-Ping, Kamachi, Yoshiro, Cataltepe, Sule, Bartuski, Allison J., Gornsteins, Eric R., Bromme, Dieter, Chapman, Harold A., and Silverman, Gary A.
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Squamous cell carcinoma -- Research ,Proteins -- Research ,Serine -- Research ,Cysteine -- Research ,Biological sciences ,Chemistry - Abstract
A study was conducted to test whether the human squamous cell carcinoma antigen 1 (SCCA1) supports inhibitory activity against serine proteinases and whether it can be a potent cross-class inhibitor of the archetypal lysosomal cysteine proteinases cathepsins K, L and S. Reactions were performed in cathepsin buffer at pH 5.5. Results suggested that SCCA1 may be involved in an inhibitory pathway that regulates an array of lysosomal cysteine proteinases.
- Published
- 1998
15. Imbalance between Cysteine Proteases and Inhibitors in a Baboon Model of Bronchopulmonary Dysplasia
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Altiok, Ozden, Yasumatsu, Ryuji, Bingol-Karakoc, Gulbin, Riese, Richard J., Stahlman, Mildred T., Dwyer, William, Pierce, Richard A., Bromme, Dieter, Weber, Ekkehard, and Cataltepe, Sule
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- 2006
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16. Human bleomycin hydrolase: molecular cloning, sequencing, functional expression, and enzymatic characterization
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Bromme, Dieter, Rossi, Alex B., Smeekens, Steven P., Anderson, David C., and Payan, Donald G.
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Proteases -- Research ,Amino acid sequence -- Analysis ,Drug resistance -- Causes of ,Biological sciences ,Chemistry - Abstract
The open reading frame encoding human bleomycin hydrolase (hBH) consists of 1365 bases and produces a protein with 455 amino acids. The protein is 40% and 89.5% identical to the yeast and rabbit bleomycin hydrolase, respectively. The protein functions as a protease and efficiently degrades bleomycin A2 and B2. Most human organs have low levels of hBH while tumor cell lines have high hBH levels. The high hBH levels are probably responsible for the resistance of tumor cells to bleomycin. The gene produces a 52 kDa protein in Spodoptera frugiperda Sf6 cells that behaves as an aminopeptidase.
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- 1996
17. Contribution to activity of histidine-aromatic, amide-aromatic, and aromatic-aromatic interactions in the extended catalytic site of cysteine proteinases
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Bromme, Dieter, Bonneau, Pierre R., Purisima, Enrico, Lachance, Paule, Hajnik, Sohini, Thomas, David Y., and Storer, Andrew C.
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Cysteine proteinases -- Research ,Tryptophan -- Research ,Biological sciences ,Chemistry - Abstract
Kinetic analysis of mutations of cysteine proteinases residues asparagine 175, tryptophan 177 and tryptophan 181 was conducted using cathepsin S, a naturally occurring variant at position 181 to show the side chain contributions of the residues in catalysis and integration of thiolate-imidazolium ion-pair forms. Asn 175 contributes to ion-pair stability by maintaining a catalysis-inducing conformation. Trp 177 side chains aid in the formation of the S'1 subsite. Trp 177-Trp 181 side chains interaction does not yield any significant effect on ion-pair stability.
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- 1996
18. Cathepsin K Is the Principal Protease in Giant Cell Tumor of Bone
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Lindeman, Jan H.N., Hanemaaijer, Roeland, Mulder, Adri, Dijkstra, P.D. Sander, Szuhai, Károly, Bromme, Dieter, Verheijen, Jan H., and Hogendoorn, Pancras C.W.
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- 2004
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19. Role for Cathepsin F in Invariant Chain Processing and Major Histocompatibility Complex Class II Peptide Loading by Macrophages
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Shi, Guo-Ping, Bryant, Rebecca A.R., Riese, Richard, Verhelst, Steven, Driessen, Christoph, Li, Zhenqiang, Bromme, Dieter, Ploegh, Hidde L., and Chapman, Harold A.
- Published
- 2000
20. Characterization of novel cathepsin K mutations in the pro and mature polypeptide regions causing pycnodysostosis
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Hou, Wu-Shiun, Bromme, Dieter, Zhao, Yingming, Mehler, Ernest, Dushey, Craig, Weinstein, Harel, Miranda, Clara Sa, Fraga, Claudia, Greig, Fenella, Carey, John, Rimoin, David L., Desnick, Robert J., and Gelb, Bruce D.
- Published
- 1999
21. [48] N,O-Diacyl hydroxamates as selective and irreversible inhibitors of cysteine proteinases
- Author
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Bromme, Dieter, primary and Demuth, Hans-Ulrich, additional
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- 1994
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22. Diabetes Perturbs Bone Microarchitecture and Bone Strength through Regulation of Sema3A/IGF-1/β-Catenin in Rats
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Ma, Rufeng, primary, Wang, Lili, additional, Zhao, Baosheng, additional, Liu, Chenyue, additional, Liu, Haixia, additional, Zhu, Ruyuan, additional, Chen, Beibei, additional, Li, Lin, additional, Zhao, Dandan, additional, Mo, Fangfang, additional, Li, Yu, additional, Niu, Jianzhao, additional, Jiang, Guangjian, additional, Fu, Min, additional, Bromme, Dieter, additional, Gao, Sihua, additional, and Zhang, Dongwei, additional
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- 2017
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23. The propeptide of cruzipain--a potent selective inhibitor of the trypanosomal enzymes cruzipain and brucipain, and of the human enzyme cathepsin F
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Reis, Flavia C. G., Costa, Tatiana F. R., Sulea, Traian, Mezzetti, Alessandra, Scharfstein, Julio, Bromme, Dieter, Menard, Robert, and Lima, Ana Paula C. A.
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parasitic diseases ,enzymes ,HPC ,Cysteine proteinase inhibitors ,pharmaceutical ,protease ,cathepsins ,enzyme precursors ,protein ,cysteine ,recombinant proteins ,proteins - Abstract
Papain-like cysteine proteases of pathogenic protozoa play important roles in parasite growth, differentiation and host cell invasion. The main cysteine proteases of Trypanosoma cruzi (cruzipain) and of Trypanosoma brucei (brucipain) are validated targets for the development of new chemotherapies. These proteases are synthesized as precursors and activated upon removal of the N-terminal prodomain. Here we report potent and selective inhibition of cruzipain and brucipain by the recombinant full-length prodomain of cruzipain. The propeptide did not inhibit human cathepsins S, K or B or papain at the tested concentrations, and moderately inhibited human cathepsin V. Human cathepsin F was very efficiently inhibited (K(i) of 32 pm), an interesting finding indicating that cruzipain propeptide is able to discriminate cathepsin F from other cathepsin L-like enzymes. Comparative structural modeling and analysis identified the interaction between the beta1p-alpha3p loop of the propeptide and the propeptide-binding loop of mature enzymes as a plausible cause of the observed inhibitory selectivity.
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- 2007
24. Mutations in fibrillin‐1 leading to classical and neonatal Marfan syndrome cause differential protease susceptibilities and protein function
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Hubmacher, Dirk, primary, Kirschner, Ryan, additional, Iyengar, Garud, additional, Bromme, Dieter, additional, Bartels, Rainer, additional, and Reinhardt, Dieter P., additional
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- 2010
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25. Free Cholesterol Accumulation in Macrophage Membranes Activates Toll-Like Receptors and p38 Mitogen-Activated Protein Kinase and Induces Cathepsin K
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Sun, Yu, primary, Ishibashi, Minako, additional, Seimon, Tracie, additional, Lee, Mingsum, additional, Sharma, Sudarshana M., additional, Fitzgerald, Katherine A., additional, Samokhin, Andriy O., additional, Wang, Yibin, additional, Sayers, Scott, additional, Aikawa, Masanori, additional, Jerome, W. Gray, additional, Ostrowski, Michael C., additional, Bromme, Dieter, additional, Libby, Peter, additional, Tabas, Ira A., additional, Welch, Carrie L., additional, and Tall, Alan R., additional
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- 2009
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26. Spontaneous Atherothrombosis and Medial Degradation in Apoe −/− , Npc1 −/− Mice
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Welch, Carrie L., primary, Sun, Yu, additional, Arey, Brian J., additional, Lemaitre, Vincent, additional, Sharma, Naresh, additional, Ishibashi, Minako, additional, Sayers, Scott, additional, Li, Rong, additional, Gorelik, Anna, additional, Pleskac, Nick, additional, Collins-Fletcher, Kadesha, additional, Yasuda, Yoshiyuki, additional, Bromme, Dieter, additional, D’Armiento, Jeanine M., additional, Ogletree, Martin L., additional, and Tall, Alan R., additional
- Published
- 2007
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27. Osteoclastic Bone Degradation and the Role of Different Cysteine Proteinases and Matrix Metalloproteinases: Differences Between Calvaria and Long Bone
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Everts, Vincent, primary, Korper, Wolf, additional, Hoeben, Kees A, additional, Jansen, Ineke DC, additional, Bromme, Dieter, additional, Cleutjens, Kitty BJM, additional, Heeneman, Sylvia, additional, Peters, Christoph, additional, Reinheckel, Thomas, additional, Saftig, Paul, additional, and Beertsen, Wouter, additional
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- 2006
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28. Thiol-Dependent Cathepsins: Pathophysiological Implications and Recent Advances in Inhibitor Design
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Bromme, Dieter, primary and Kaleta, Jadwiga, additional
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- 2002
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29. Structural requirements for the collagenase and elastase activity of cathepsin K and its selective inhibition by an exosite inhibitor.
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Sharma, Vidhu, Panwar, Preety, O'Donoghue, Anthony J., Cui, Haoran, Guido, Rafael V. C., Cralk, Charles S., and Bromme, Dieter
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COLLAGENASES ,ELASTASES ,CATHEPSINS ,TARGETED drug delivery ,BINDING sites ,ENZYME inhibitors - Abstract
Human cathepsin K (CatK) is a major drug target for the treatment of osteoporosis. Although its collagenase activity is unique, CatK also exerts a potent elastolytic activity that is shared with human cathepsins V and S. Other members of the cysteine cathepsin family, which are structurally similar, do not exhibit significant collagen and elastin degrading activities. This raises the question of the presence of specific structural elements, exosites, that are required for these activities. CatK has two exosites that control its collagenolytic and elastolytic activity. Modifications of exosites 1 and 2 block the elastase activity of CatK, whereas only exosite-1 alterations prevent collagenolysis. Neither exosite affects the catalytic activity, protease stability, subsite specificity of CatK or the degradation of other biological substrates by this protease. A low-molecular-mass inhibitor that docks into exosite-1 inhibits the elastase and collagenase activity of CatK without interfering with the degradation of other protein substrates. The identification of CatK exosites opens up the prospect of designing highly potent inhibitors that selectively inhibit the degradation of therapeutically relevant substrates by this multifunctional protease. [ABSTRACT FROM AUTHOR]
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- 2015
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30. Pycnodysostosis: Expression and Biochemical Characterization of Missense Mutations in the Cathepsin K Gene • 718
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Hou, Wu-Shiun, primary, Bromme, Dieter, additional, Mehler, Ernest, additional, Weinstein, Harel, additional, Desnick, Robert J, additional, and Gelb, Bruce D, additional
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- 1998
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31. Contributors
- Author
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Abbott, Catherine Anne, Abraham, Carmela R., Adachi, Hideki, Adachi, Osao, Adam, Zach, Adams, Michael W.W., Adang, Michael J., Adham, Ibrahim, M., Aducci, Patrizia, Agard, David A., Agranovsky, Alexey A., Akamatsu, Tetsuya, Akiyama, Yoshinori, Albrechtsen, Reidar, Alejo, Ali, Amberg, Sean M., Amerik, Alexander Y., Amparyup, Piti, Andrade, Felipe, Andrés, Germán, Andrews, Daniel M., Andrews, Robert K., Antalis, Toni M., Anthony, Colin S., Aoki, Naoya, Apte, Suneel S., Arima, Kazunari, Arlaud, Gérard, Arni, Raghuvir Krishnaswamy, Arnoux, Pascal, Aronson, Nathan N., Jr., Arthur, Michel, Asano, Yasuhisa, Ascenzi, Paolo, Assakura, Marina T., Auld, David S., Ávila, Veridiana de Melo Rodrigues, Avilés, Francesc X., Awad, William M., Jr., Bachhawat, Anand K., Bai, Shan, Baird, Teaster T., Jr., Bajaj, S. Paul, Baker, Susan C., Banbula, Agnieszka, Barrett, Alan J., Barrowman, Jemima, Bartlett, John D., Bartsch, Jörg W., Baschuk, Nikola, Baskova, Isolda P., Batra, Jyotsna, Bauer, Karl, Baumann, Ulrich, Baumeister, Wolfgang, Bauvois, Cédric, Bayés, Alex, Beauvais, Anne, Becker-Pauly, Christoph, Begley, Tadhg P., Békés, Miklós, Belas, Robert, Beleford, Daniah, Beppu, Teruhiko, Bergmann, Ernst M., Bernard, Bruno A., Bernard, Dominique, Berndt, Michael C., Berruti, Giovanna, Berry, Colin, Bertenshaw, Greg P., Betzel, Christian, Bhaskarla, Chetana, Bhosale, Manoj, Bierbaum, Gabriele, Bjarnason Jón, B., Blaber, Michael, Blackman, Michael J., Blinkovsky, Alexander, Boeke, Jef D., Bogyo, Matthew, Bohn, Stefan, Boileau, Guy, Boland, Mike, Bolken, Tové C., Bond, Judith S., Bondeson, Jan, Bordallo, Javier, Borelli, Claudia, Botelho, Tiago O., Bott, Richard R., Bourne, David G., Bovenschen, Niels, Bradshaw, Ralph A., Breddam, Klaus, Brew, Keith, Brindley, Paul J., Brinkman, Diane L., Britton, Collette, Broadbent, Jeff R., Broadhurst, Anne, Brómme, Dieter, Broom, Murray, Brown, Jeremy S., Brown, Mark A., Bruchhaus, Iris, Burleigh, Barbara A., Burns, Kristin E., Burrows, James F., Butler, Michael J., Buttle, David J., Byrd, Chelsea M., Byun, Tony, Cadel, Sandrine, Caffrey, Conor R., Cal, Santiago, Caldentey, Javier, Candela, Thomas, Capasso, Clemente, Capriogilio, Daniel R., Carginale, Vincenzo, Carmona, Adriana Karaoglanovic, Carruthers, Vern B., Castellino, Francis J., Catanese, Joseph J., Caterson, Bruce, Caughey, George H., Cawley, Naimh X., Cawston, Tim E., Cazzulo, Juan José, Chai, Jijie, Chai, Karl X., Chaim, Olga Meiri, Chang, L.S., Chao, Julie, Chapot-Chartier, Marie-Pierre, Charli, Jean-Louis, Charlier, Paulette, Chave, Karen J., Chen, Jian-Min, Chen, Jinq-May, Chen, Li-Mei, Chen, Ya-Wen, Chen, Yu-Yen, Chevrier, Bernard, Chich, Jean-François, Chien, Jeremy, Chimalapati, Suneeta, Cho, Ki Joon, Choi, Kwan Yong, Chuang, Woei-Jer, Chung, Chin Ha, Chung, Ivy Yeuk Wah, Clamagirand, Christine, Clark, Ian M., Clarke, Adrian K., Clarke, Nicola E., Clarke, Steven Gerard, Clauziat, Philippe, Clements, Judith A., Coffinier, Catherine, Cohen, Paul, Colige, Alain, Collignon, Anne, Colloms, Sean D., Conzelmann, Andreas, Coombs, Graham H., Cooney, Jakki C., Cooper, Jonathan B., Cooper, Max D., Copeland, Nikki A., Cottrell, Graeme S., Coyle, Joseph T., Craik, Charles S., Creemers, John W.M., Cretu, Daniela, Croce, Jenifer, Cross, Keith J., Cueva, Rosario, Cui, Sheng, Cunha, Luis, Cutting, Simon, d’Enfert, Christophe, D’Orchymont, Hugues, Dahlbäck, Björn, Dai, Shujia, Dalbey, Ross E., Dalton, John P., Dando, Pam M., Daniel, R.M., Danilov, Sergei M., Davies, Donna E., De Araujo, Heloisa S., De los Santos, Teresa, de Luca, Viviana, De Meester, Ingrid, de Oliveira, Ana Karina, de Oliveira, Eduardo Brandt, De Oliveira, Pedro Lagerblad, de Vos, Sarah, Declercq, Jeroen, Declercq, Wim, Deghmane, Ala-Eddine, Dekker, Niek, Del Prete, Sonia, Del Rosal, Marina, Delmas, Bernard, DeLotto, Robert, Demidyuk, Ilya V., Denison, Mark R., Deussing, Jan M., Devi, Lakshmi A., Diamandis, Eleftherios P., Diaz, Isabel, Díaz-Perales, Araceli, Dijkstra, Bauke W., Ding, Yan, Dixon, Jack E., Dodt, Johannes, Dokland, Terje, Dolenc, Iztok, Dong, Ningzheng, Dong, Tran Cat, Dong, Ying, Dongre, Mitesh, Donovan, Mark, Dore, Timothy M., Dorstyn, Loretta, Dou, Hong, Dou, Zhicheng, Dougall, Annette M., Drag, Marcin, Dudley, Edward G., Dunn, Ben M., Dupuy, Bruno, Duque-Magalhāes, Maria Conceicāo, Durá, M. Asunción, Eeckhout, Yves, Eijsink, Vincent, Eisen, Arthur Z., Eissa, Azza, Eklund, Sandra, Eletr, Ziad M., Ellis, Vincent, Engel, Wolfgang, Erdös, Ervin G., Escalante, Teresa, Estell, David A., Etscheid, Michael, Evans, Herbert J., Everett, Roger D., Faesen, Alex C., Fahrenholz, Falk, Fanjul-Fernández, Miriam, Farady, Christopher J., Feller, Georges, Feng, Hong, Fenster, Kurt M., Férec, Claude, Ferrari, Silvia, Fingleton, Barbara, Fisher, Jed F., Fives-Taylor, Paula M., Fong, Loren G., Forneris, F., Forster, Brian M., Forster, Friedrich, Foster, Simon J., Foulon, Thierry, Foundling, Stephen I., Fox, Jay William, Franzetti, Bruno, Frasch, Alejandra P., Freeze, Hudson H., Frère, Jean-Marie, Frey, Teryl K., Fricke, Beate, Fricker, Lloyd D., Fridman, Rafael, Froelich, Christopher J., Fröhlich, Camilla, Fu, Hsueh-Liang, Fuhrmann, Cynthia N., Fujimura, Satoshi, Fujiwara, Hiroshi, Fukushima, Jun, Fukuyama, Keiichi, Fuller, Robert S., Fusek, Martin, Gaboriaud, Christine, Gache, Christian, Gakh, Oleksandr, Gal, Peter, Gao, Junjun, García-Sastre, Adolfo, Gardiner, Donald L., Gatehouse, John A., Gaucher, G.M., Gauthier, Francis, Ghuysen, Jean-Marie, Gibson, Wade, Gillies, Jennifer, Glaser, Elzbieta, Glaser, Fabian, Glickman, Michael H., Goettig, Peter, Goffin, Colette, Gohda, Eiichi, Goldberg, Alfred L., Goldberg, Daniel E., Goldberg, Gregory I., Goldfarb, Nathan E., Gomis-Rüth, F. Xavier, Gopal, B., Gorbalenya, Alexander E., Gordon, Stuart G., Gorrell, Mark D., Götz, Friedrich, Goulas, Theodoros, Gouzy-Darmon, Cécile, Govind, K., Gráf, Lászlo, Granados, Robert R., Gräwert, Melissa Ann, Gray, Douglas A., Graycar, Thomas P., Green, Jonathan A., Gremski, Luiza Helena, Groll, Michael, Gromova, Tania Yu, Gros, P., Grubman, Marvin J., Grunden, Amy M., Gudmundsdóttir, Ágústa, Guinand, Micheline, Gully, Djamel, Gustchina, Alla, Gutiérrez, José María, Ha, Byung Hak, Haeggström, Jesper Z., Hageman, James H., Haiko, Johanna, Hailfinger, Stephan, Haitchi, Hans Michael, Han, Ji Seon, Hanquez, Chantal, Harada, Minoru, Hara-Nishimura, Ikuko, Harboe, Marianne, Härd, Torleif, Harris, David A., Hassiepen, Ulrich, Hata, Shoji, Hattori, Akira, He, Rong-Qiao, Heck, Albert J.R., Hendricks, Dirk F., Henrich, Bernhard, Henriet, Patrick, Hernández-Arana, Andrés, Herrera-Camacho, Irma, Heussipp, Gerhard, Hibino, Toshihiko, Hicks, P.M., Hillman, Bradley I., Hiraoka, B. Yukihiro, Hiratake, Jun, Hizukuri, Yohei, Ho, Heng-Chien, Hoa, Ngo Thi, Hochstrasser, Mark, Hodge, Kathryn M., Hofmann, Theo, Hohn, Thomas, Hoidal, John R., Höltje, Joachim-Volker, Homma, Koichi J., Honek, John F., Hook, Vivian Y.H., Hooper, John D., Hooper, Nigel M., Hosoi, Kazuo, Howe, Christopher J., Hruby, Dennis E., Hseih, James J.-D., Hsu, Chun-Chieh, Huang, Tony T., Huang, Tur-Fu, Huet, Yoann, Hughes, Clare, Hugonnet, Jean-Emmanuel, Huston, Adrienne L., Ibrahim-Granet, Oumaïma, Ichishima, Eiji, Ikehara, Yukio, Inagami, Tadashi, Ingram, Jessica, Isaac, R.E., Isaya, Grazia, Isaza, Clara E., Ishii, Shin-ichi, Isnard, Amandine, Ito, Kiyoshi, Ito, Koreaki, Itoh, Yoshifumi, Iturrioz, Xavier, Iwanaga, Sadaaki, Jack, Ralph W., Jackson, Mel C., James, Michael N.G., Janata, Jiří, Janoir, Claire, Janska, Hanna, Jarrell, Ken F., Jaskolski, Mariusz, Jaswal, Sheila S., Jean, Ying Y., Jenne, Dieter E., Jeon, Young Joo, Jiang, Ping, Johnson, John E., Johnson, Michael D., Johnston, James A., Jones, Amanda, Jones, Elizabeth W., Joudiou, Carine, Juliano, Luiz, Jung, Hea-Jin, Jupp, Ray, Kagawa, Todd F., Kalbacher, Hubert, Kamata, Yayoi, Kaminogawa, Shuichi, Kamio, Yoshiyuki, Kaneda, Makoto, Kang, Sung Gyun, Kang, Sung Hwan, Kania, Mary, Kantyka, Tomasz, Kanzawa, Nobuyuki, Karim, Abdulkarim Y., Kasumi, Takafumi, Kataoka, Hiroaki, Kaur, Hardeep, Kawabata, Shun-Ichiro, Kawaguchi, Mari, Kay, John, Kaynar, Murat, Keiler, Kenneth C., Kelly, R.M., Kenton, Nathaniel T., Kerr, Michael A., Kersse, Kristof, Kervinen, Jukka, Kessler, Benedikt M., Kessler, Efrat, Khoronen, Timo K., Kidd, Simon, Kikkert, Marjolein, Kilian, Mogens, Kim, Do-Hyung, Kim, Doyoun, Kim, Eunice EunKyeong, Kim, In Seop, Kim, Jung-Gun, Kim, Kyeong Kyu, Kim, Kyung Hyun, Kimber, Matthew S., Kimura, Yukio, Kirschke, Heidrun, Kiso, Yoshiaki, Kleanthous, Colin, Klein, Jürgen R., Klemba, Michael, Kmiec, Beata, Kobayashi, Hideyuki, Kodama, Hiroyuki, Koelsch, Gerald, Kok, Jan, Kolattukody, P.E., Kolb, Fabrice A., Kolmar, Harald, Komori, Yumiko, Konvalinka, Jan, Korkmaz, Brice, Kostrov, Sergey V., Kräusslich, Hans-Georg, Krczal, Gabi, Kress, Lawrence F., Kristjánsson, Magnüs Már, Kučera, Tomáš, Kukday, Sayali S., Kumagai, Hidehiko, Kumar, Sharad, Kumarasiri, Malika, Kumazaki, Takashi, Kümmerer, Beate M., Kuno, Kouji, Kurkinen, Markku, Kutejová, Eva, Kveiborg, Marie, Kwarciak, Agnieszka, Laakkonen, Liisa, Labrou, Nikolaos E., Laing, Gavin D., Lamppa, Gayle, Langer, Thomas, Laursen, Richard A., Lawrenson, Richard A., Layne, Matthew D., Le Bonniec, Bernard F., Leal, María C., Lechan, Ronald M., Lee, David H., Lee, Irene, Lee, Jae, Lee, Kye Joon, Lee, Soohee, Lei, Xiaobo, Leis, Jonathan, LeMosy, Ellen K., Lepage, Thierry, Leppla, Stephen H., Lesner, Adam, Lessard, Ivan A.D., Lhomond, Guy, Li, Huilin, Li, Shu-Ming, Li, Weiguo, Liao, Ta-Hsiu, Liddington, Robert C., Lieber, Toby, Lijnen, H.R., Lima, Christopher D., Lin, Chen-Yong, Lin, Gang, Lin, Ming T., Lin, Xinli, Lin, Yee-Shin, Lindsay, L.L., Lipscomb, William N., Little, John W., Liu, Ching-Chuan, Liu, Chuan-ju, Lively, Mark O., Livnat-Levanon, Nurit, Ljungdahl, Per O., Llorens-Cortes, Catherine, Lobel, Peter, Loh, Y. Peng, Lohi, Jouko, Lomonossoff, G.P., Looze, Yvan, López-Otin, Carlos, Lopez-Quezada, Landys, Loukas, Alex, Lu, Long-Sheng, Lundwall, Áke, Luo, Liu-Ying, Lupas, Andrei, Luthe, Dawn S., Lynch, Nicholas J., Lyons, Peter J., MacKay, Vivian L., Macleod, Jesica M. Levingston, Magdolen, Viktor, Mainardi, Jean-Luc, Mäkinen, Kauko K., Mallari, Jeremy P., Manandhar, Surya P., Mandelbaum, Fajga R., Manicone, Anne M., Mansfeld, Johanna, Marcotrigiano, Joseph, Mares, Michael, Marfany, Gemma, Markland, Francis S., Jr., Marokházi, Judith, Marquis, Hélène, Marr, Robert A., Martegani, Enzo, Martin, Erik W., Martinez, Manuel, Martins, L. Miguel, Maruyama, Masato, Maruyama, Masugi, Maruyama, Sususmu, Masaki, Takeharu, Massoumi, Ramin, Mathew, Rency T., Matrisian, Lynn M., Matsuda, Yoshihiro, Matsushita, Osamu, Matuschek, Marco, Matušková, Anna, Matúz, Krisztina, Mauch, Cornelia, Maurizi, Michael R., Mayr, Lorenz M., McCafferty, Dewey G., McDonald, J. Ken, McKerrow, James H., McMillan, David, Mecham, Robert P., Mehta, Darshini P., Meisinger, Chris, Mellors, Alan, Melton, Roger G., Melvin, Jeffrey A., Ménard, Robert, Menéndez-Arias, Luis, Menezes, Milene C., Mesecar, Andrew, Mesnage, Stéphane, Meyer, Diane H., Meyers, Gregor, Michaelis, Susan, Michalska, Karolina, Mielicki, Wojciech P., Mierau, Igor, Mikoulinskaia, Galina V., Miller, Charles G., Miller, Lydia K., Mills, John, Mills, Kenneth V., Min, Jinrong, Mistou, Michel-Yves, Misumi, Yoshio, Miyoshi, Shin-ichi, Mizutani, Shigehiko, Mobashery, Shahriar, Mochizuki, Satsuki, Mock, William L., Möhrlen, Frank, Moiré, Nathalie, Monahan, Paul E., Moncada-Pazos, Angela, Monnet, Véronique, Monod, Michel, Montecucco, Cesare, Morelli, Laura, Mori, Sumiko, Morita, Takashi, Morrissey, James H., Morse, Richard J., Mort, John S., Mortensen, Uffe H., Morty, Rory E., Moss, Joel, Motoshima, Hidemasa, Mottram, Jeremy C., Moura-da-Silva, Ana M., Mudgett, Mary Beth, Mundt, Egbert, Murakami, Kazuo, Murakami, Mario Tyago, MurakamiMurofoshi, Kimiko, Murao, Sawao, Murphy, Gillian, Murthy, M.R.N., Muta, Tatsushi, Myburgh, Elmarie, Mzhavia, Nino, Nabi, A.H.M. Nurun, Nagase, Hideaki, Nagle, Michael W., Nägler, Dorit K., Naik, Rajesh R., Nair, Divya B., Nakai, Toshiki, Nakajima, Yoshitaka, Nakamura, Yukio, Nakatogawa, Hitoshi, Nakayama, Toru, Nalivaeva, Natalia N., Nandi, Dipankar, Nascimento-Silva, Maria Clara Leal, Nasmyth, Kim, Nathan, Carl F., Navarro-García, Fernando, Naves, Dayane Lorena, Nedialkova, Danny D., Neuman, Keir C., Nguyen, Jeffrey-Tri, Nguyen, Ky-Anh, Niemirowicz, Gabriela T., Nikai, Toshiaki, Nishi, Eiichiro, Nishii, Wataru, Nishiyama, Makoto, Nishiyama, Yasuhiro, Noda, Masatoshi, Nomura, Seiji, Norioka, Shigemi, Nsangou, Desire M.M., O’Brien, Amornrat, O’Connor, Michael B., Oda, Kohei, Odinokova, Irina V., Oetjen, Joyce, Ogura, Teru, Ohman, Dennis E, Ohsumi, Yoshinori, Ojha, Mukti, Okabe, Akinobu, Okada, Yasunori, Okamoto, Keinosuke, Okuda, Kenji, Okumura, Nobuaki, Okuno, Takashi, Oleson, Kjeld, Oliveira de Giuseppe, Priscila, Olivier, Martin, Ono, Yasuko, Oroszlan, Stephen, Ota, Nobuyuki, Ovadia, Michael, O-Wang, Jiyang, Oxvig, Claus, Packer, Jeremy C.L., Padilla-López, Sergio, Paetzel, Mark, Page, Michael J., Page-McCaw, Andrea, Paine, Mark J.I., Park, Byoung Chul, Park, Eunyong, Park, John E., Park, Pyong Woo, Park, Sung Goo, Parkin, Kirk L., Parks, William C, Paschoalin, Thaysa, Pastore, Annalisa, Patananan, Alexander Nikolich, Paul, Sudhir, Paulson, Henry L., Pawel-Rammingen, Ulrich von, Pearce, David A., Pearson, Mark S., Pei, Duanqing, Pejler, Gunnar, Pemberton, Alan D., Peng, Jianhao, Pernier, Julien, Peters, Jan-Michael, Pfirrmann, Thorsten, Pham, Viet-Laï, Pichová, Iva, Pickering, Darren, Piesse, Christophe, Pignol, David, Pike, Robert N., Pinck, Lothaire, Pirkle, Hubert, Pitot, Henry C., Plaut, Andrew G., Ploegh, Hidde, Polgár, László, Porter, Corrine, Postina, Rolf, Potempa, Jan, Poulsen, Knud, Power, Scott D., Pratt, Rex. F., Prehna, Gerd, Prévost, Gilles, Pshezhetsky, Alexey V., Qasim, Mohammad A., Qian, Feng, Qiu, Jiazhou, Radisky, Evette S., Rader, Stephen D., Raman, Kavita, Ramsay, Andrew J., Rancourt, Derrick E., Ranjit, Najju, Rao, Narayanam V., Ratia, Kiira, Rawlings, Neil D., Rawson, Robert B., Reddy, Vijay, Redman, Colvin M., Regonesi, Maria Elena, Reichert, Andreas S., Reichl, Antonia P., Remaut, Han, Remington, S. James, Renatus, Martin, Reverter, David, Reynolds, Eric C., Rholam, Mohamed, Rice, Charles M., Ridky, Todd W., Riezman, Howard, Rijken, D.C., Rio, Marie-Christine, Ritchie, Alison, Robert-Baudouy, Janine, Robinson, Mark W., Robinson, Michael, Rodriguez-Romero, Adela, Rodriques, Renata Santos, Rogers, John C., Rojas, Camilo, Romesberg, Floyd E., Roper, David J., Rosas-Murrieta, Nora, Rose, A.M., Rosenthal, Philip J., Rosing, J., Rossetto, Ornella, Rossi, Véronique, Roth, Richard A., Rottensteiner, Hanspeter, Rowan, Andrew D., Rozanov, Mikhail, Rucavado, Alexandra, Ruecker, Andrea, Rul, Françoise, Rümenapf, Till, Russo, Ilaria, Ryan, Martin D., Sacco, Elena, Sadler, J. Evan, Saenger, W., Sahl, Hans-Georg, Sajid, Mohammed, Sakaguchi, Masayoshi, Sakiyama, Fumio, Salas, Maria L., Salgado, Maria Cristina O., Salvesen, Guy S., Sánchez, Edith, Sanchez, Eladio F., Sang, Qing-Xiang Amy, Sankaran, Krishnan, Sarkar, Susanta K., Sarras, Michael P., Jr., Sasagawa, Yoshikiyo, Satohiko, Araki, Sauvage, Eric, Saveanu, Loredana, Savithri, H.S., Sawada, Hitoshi, Sawers, R. Gary, Scarisbrick, Isobel A., Schaller, Andreas, Scheer, Justin M., Scheiflinger, Friedrich, Schiene-Fischer, Cordelia, Schlomann, Uwe, Schlösser, Manfred, Schmaier, Alvin H., Schmidt, Walter K., Schneemann, Anette, Schnellmann, Rick G., Scholze, Henning, Schomburg, Lutz, Schwaeble, Wilhelm J., Scott, Christopher J., Scudiero, Rosaria, Sehara-Fujisawa, Atsuko, Seidah, Nabil G., Seiki, Motoharu, Sekiguchi, Junichi, Senff-Ribeiro, Andrea, Seong, Ihn Sik, Serpe, Mihaela, Serrano, Solange M.T., Setlow, Peter, Shahian, Tina, Shanks, M., Shao, Feng, Shapiro, Steven D., Sharma, Navneet, Shaw, Lindsey N., Shen, Aimee, Shen, Lei, Sherwood, Roger F., Shi, Yun-Bo, Shimoi, Hitoshi, Shimura, Yoichiro, Shirras, A.D., Shridhar, Viji, Shukla, Jinal K., Siigur, Ene, Siigur, Jüri, Silmon de Monerri, Natalie C., Sim, Robert B., Simmer, James P., Simmons, William H., Singh, Jaspreet, Singleton, Alison, Sirakova, Tatiana D., Sixma, Titia K., Skern, Tim, Skidgel, Randal A., Slack, Jeffrey, Sleat, David E., Slusher, Barbara S., Smith, Janet L., Smith, Matthew A., Smyth, Mark J., Snijder, Erik J., Sobhanifar, Solmaz, Söderhaäll, Kenneth, Sohar, Istvan, Sonderegger, Peter, Sorgine, Marcos Henrique Ferreira, Sorimachi, Hiroyuki, Soukhodolets, Karen E., Souza, Tatiana de Arruda Campos Brasil de, Sperka, Tamás, Sriskandan, Shiranee, St. Geme, Joseph W., III, St. Leger, Raymond J., Staib, Peter, Steele, James L., Stefansson, Bjarki, Steinkühler, Christian, Stenberg, Leisa M., Stenflo, Johan, Stennicke, Henning R., Stepanov, Valentin M., Stepnaya, Olga A., Steven, Frank, Stevens, Richard L., Stevenson, Kenneth J., St-Louis, Mathieu, Stobart, Christopher C., Stöcker, Walter, Storer, Andrew C., Sträter, Norbert, Strauss, Ellen G., Strauss, James H., Stříšovský, Kvido, Strynadka, Natalie C.J., Sturrock, Edward D., Su, Dan, Su, Xiao-Dong, Suárez-Rendueles, Paz, Sulea, Traian, Sundararajan, Venkatesh, Suno, Ryoji, Suzuki, Carolyn K., Suzuki, Fumiaki, Suzuki, Hideyuki, Suzuki, Nobuhiro, Swenson, Stephen, Szabady, Rose L., Szecsi, Pal Bela, Szilágyi, Lászlo, Taha, Muhamed-Kheir, Takahashi, Eizo, Takahashi, Kenji, Takai, Toshiro, Takeda, Atsushi, Takeda, Soichi, Tame, Jeremy J.R.H., Tamura, Tomohiro, Tan, Fulong, Tanaka, Keiji, Tanase, Carmen, Tang, Jordan, Tanizaki, Martha M., Tannich, Egbert, Tans, Guido, Tarentino, Anthony L., Tassanakajon, Anchalee, Tatsumi, Hiroki, Tautz, Norbert, Taylor, Erin Bassford, Teixeira, Pedro Filipe, Telugu, Bhanu Prakash V.L., Templin, Markus F., Terada, Shigeyuki, Tetsuya, Uchikoba, Thacker, C., Thaker, Maulik, Thiel, Heinz-Jürgen, Thielens, Nicole, Thierry, Gonzales, Thivierge, Karine, Thomas, Mark D., Thome, Margot, Thorsness, Mary K., Thorsness, Peter E., Tigue, Natalie J., Todi, Sokol V., Tomkinson, Birgitta, Tonello, Fiorella, Tong, Liang, Toogood, H.S., Tortora, Paolo, Tözsèr, József, Travassos, Luiz Rodolpho, Travis, James, Trevisan-Silva, Dilza, Trinchella, Francesca, Trivedi, Neil N., Troy, Carol M., Tschesche, Harald, Tseng, Yu-Lun, Tsujimoto, Masafumi, Tu, Anthony T., Tumelty, Kathleen E., Turk, Boris, Turk, Dusan, Turk, Vito, Turner, Anthony J., Uchikoba, Tetsuya, Ueno, Takayuki, Ugalde, Alejandro P., Uitto, Veli-Jukka, Urban, Sinisa, Valdenaire, Olivier, Valli, Adrian, Van Beeumen, Jozef, Van den Burg, Bertus, Van der Hoorn, Renier A.L., van Dijl, Jan Maarten, Van Endert, Peter, Van Raam, Bram J., Van Wart, Harold E., Vanden Berghe, Tom, Vandenabeele, Peter, Vanoni, Margo, Veiga, Silvio Sanches, Velander, William H., Velasco, Gloria, Vendrell, Josep, Venekei, I. István, Vetvicka, Vaclav, Vögtle, F.-Nora, Vollmer, Waldemar, Wada, Kei, Wagner, Fred W., Wai, Sun Nyunt, Wai, Timothy, Wainwright, Shane, Walker, Kenneth W., Walker, Stephen J., Wallach, Jean, Walling, Linda L., Walsh, Peter N., Wang, Hai-Yan, Wang, Hengbin, Wang, Jianwei, Wang, Peng, Wang, Ping, Wassenegger, Michael, Watanabe, Kunihiko, Webb, Helen, Weber, Joseph M., Weber, Niklas, Webster, Daniel R., Wei, Shuo, Welch, Rodney A., Wells, James A., Wenzel, Herbert, Wertz, Ingrid E., Wewer, Ulla W., Whyteside, Alison R., Wilk, Sherwin, Wilkin, Jean-Marc, Wilmes, Claudia, Winther, Jakob R., Wishart, David S., Wlodawer, Alexander, Woessner, J. Fred, Wolfe, Michael S., Wong, Wilson, Woodgate, Roger, Wright, Gerry, Wu, Jiunn-Jong, Wu, Qingyu, Wysocka, Magdalena, Xu, Chao, Xu, Zhenghong, Yahori, Kinnosuke, Yamada, Shoji, Yamaguchi, Nozomi, Yamaguchi, Shinji, Yamakawa, Yoshio, Yamamoto, Hiroki, Yana, Ikao, Yang, Maozhou, Yang, Na, Yao, Chenjuan, Yao, Tingting, Yasuda, Noriko, Yasuhara, Toshimasa, Yasumasu, Shigeki, Yeh, Edward T.H., Yiallouros, Irene, Yin, Jiang, Yonezawa, Hiroo, Yoo, Soon Ji, Yoshimoto, Tadashi, Young, Michael W., Young, Stephen G., Zaidi, Nousheen, Zavalova, Ludmila L., Zavodszky, Peter, Zhang, Aidong, Zhang, Xianming, Zhang, Yi-Zheng, Zheng, Dominick, Zhong, Guangming, Zhong, Rong, Zhou, Yuan, Zhou, Zhaohui Sunny, Zick, Michael, Zigrino, Paola, and Zimin, Andrei A.
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- 2013
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32. Vinyl Sulfones as Mechanism-Based Cysteine Protease Inhibitors
- Author
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Palmer, James T., primary, Rasnick, David, additional, Klaus, Jeffrey L., additional, and Bromme, Dieter, additional
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- 1995
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33. Free Cholesterol Accumulation in Macrophage Membranes Activates Toll-Like Receptors and p38 Mitogen-Activated Protein Kinase and Induces Cathepsin K.
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Yu Sun, Ishibashi, Minako, Seimon, Tracie, Mingsum Lee, Sharma, Sudarshana M., Fitzgerald, Katherine A., Samokhin, Andriy O., Yibin Wang, Sayers, Scott, Aikawa, Masanori, Jerome, W. Gray, Ostrowski, Michael C., Bromme, Dieter, Libby, Peter, Tabas, Ira A., Welch, Carrie L., and Tall, Alan R.
- Subjects
CHOLESTEROL ,BLOOD cholesterol ,MACROPHAGES ,ANTIGEN presenting cells ,PROTEIN kinases - Abstract
The article presents a study that examines the accumulation of free cholesterol in macrophage membranes. Result of the study shows that macrophages from knockout mice showed important role for Toll-like receptor (TLR) 4 and TLR3 after late endosomal loading. The study suggests that free cholesterol enrichment of either plasma and endosomal membrane in macrophages leads to activation of various TLRs and prolonged p38 nitrogen-activated protein kinase as well as the induction of Cathepsin K(Ctsk).
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- 2009
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34. Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate.
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Li, Zhenqiang, Hou, Wu-Shiun, Escalante-Torres, Carlos R, Gelb, Bruce D, and Bromme, Dieter
- Abstract
Bone resorption in balance with bone formation is vital for the maintenance of the skeleton and is mediated by osteoclasts. Cathepsin K is the predominant protease in osteoclasts that degrades the bulk of the major bone forming organic component, type I collagen. Although the potent collagenase activity of cathepsin K is well known, its mechanism of action remains elusive. Here, we report a cathepsin K-specific complex with chondroitin sulfate, which is essential for the collagenolytic activity of the enzyme. The complex is an oligomer consisting of five cathepsin K and five chondroitin sulfate molecules. Only the complex exhibits potent triple helical collagen-degrading activity, whereas monomeric cathepsin K has no collagenase activity. The primary substrate specificity of cathepsin K is not altered by complex formation, suggesting that the protease-chondroitin sulfate complex primarily facilitates the destabilization and/or the specific binding of the triple helical collagen structure. Inhibition of complex formation leads to the loss of collagenolytic activity but does not impair the proteolytic activity of cathepsin K toward noncollagenous substrates. The physiological relevance of cathepsin K complexes is supported by the findings that (i) the content of chondroitin sulfate present in bone and accessible to cathepsin K activity is sufficient for complex formation and (ii) Y212C, a cathepsin K mutant that causes pycnodysostosis (a bone sclerosing disorder) and that has no collagenase activity but remains potent as a gelatinase, is unable to form complexes. These findings reveal a novel mechanism of bone collagen degradation and suggest that targeting cathepsin K complex formation would be an effective and specific treatment for diseases with excessive bone resorption such as osteoporosis.
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- 2002
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35. Cathepsin V is involved in the degradation of invariant chain in human thymus and is overexpressed in myasthenia gravis.
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Tolosa, Eva, Weijie Li, Yasuda, Yoshiyuki, Wienhold, Wolfgang, Denzin, Lisa K., Lautwein, Alfred, Driessen, Christoph, Schnorrer, Petra, Weber, Ekkhard, Stevanovic, Stefan, Kurek, Raffael, Melms, Arthur, and Bromme, Dieter
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- *
CYSTEINE proteinases , *PROTEOLYTIC enzymes , *EPITHELIAL cells , *MAJOR histocompatibility complex , *CELLS , *EPITHELIUM - Abstract
Presents a study which reported that Cathepsin (Cat) V is the dominant cysteine protease in cortical human thymic epithelial cells. Comparison of Cat V expression between thymi from patients with myasthenia gravis and healthy controls; Proteolytic events required by MHC class II antigen presentation; Cat inhibitors that can block the degradation of invariant chain.
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- 2003
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36. Spontaneous atherothrombosis and medial degradation in Apoe-/-, Npc1-/- mice.
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Welch CL, Sun Y, Arey BJ, Lemaitre V, Sharma N, Ishibashi M, Sayers S, Li R, Gorelik A, Pleskac N, Collins-Fletcher K, Yasuda Y, Bromme D, D'Armiento JM, Ogletree ML, and Tall AR
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- Animals, Apolipoproteins E physiology, Atherosclerosis metabolism, Cholesterol genetics, Cholesterol metabolism, Genetic Predisposition to Disease, Intracellular Signaling Peptides and Proteins, Mice, Mice, Inbred BALB C, Mice, Inbred C57BL, Mice, Knockout, Mice, Mutant Strains, Mutation, Niemann-Pick C1 Protein, Proteins physiology, Thrombosis enzymology, Tunica Media metabolism, Apolipoproteins E deficiency, Apolipoproteins E genetics, Atherosclerosis genetics, Atherosclerosis pathology, Proteins genetics, Thrombosis genetics, Thrombosis pathology, Tunica Media pathology
- Abstract
Background: The formation of an occluding thrombus on a ruptured or eroded atherosclerotic plaque is the hallmark event leading to acute coronary syndromes, myocardial infarction, and sudden death in humans. However, other species are highly resistant to plaque complications, and the specific processes predisposing to plaque destabilization and thrombosis are poorly understood., Methods and Results: Mice carrying a null mutation of a gene regulating intracellular cholesterol transport (the Niemann-Pick C1 [Npc1] gene) were crossed with apolipoprotein E (Apoe) knockout mice to examine the effect of Npc1 on atherosclerotic lesion formation. Double-mutant mice showed greater lesion area compared with Apoe-/- littermates. Remarkably, the double mutants also developed large, protruding thrombi associated with the plaques and prominent medial degradation with inflammatory cell infiltration into the adventitia. Genetic studies suggested that the BALB background was permissive for plaque complications compared with C57BL/6J, and a BALB susceptibility locus was mapped by linkage analysis to chromosome 6. Examination of clotting parameters in double-knockout mice revealed that native clotting times were shortened and thrombin-antithrombin complex and soluble CD40 ligand levels were elevated compared with wild-type controls. In addition, cathepsin K was induced in Npc1-/- macrophages, and cathepsin K immunostaining and elastase activity were increased in proximal aortas of double-mutant mice compared with controls., Conclusions: A defect in intracellular cholesterol trafficking caused by the Npc1 null mutation predisposes to increased lesion formation, atherothrombosis, and medial degradation. Plaque complications may require a procoagulant state and an increased protease activity, leading to plaque destabilization.
- Published
- 2007
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