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1,136 results on '"Goldstein, Joseph L."'

152. How to win a Lasker? Take a close look at Bathers and Bulls

Author

Goldstein, Joseph L.

Subjects
Analysis, Services, Achievements and awards, Awards (Prizes) -- Analysis, Scientists -- Achievements and awards -- Services
Abstract

Some of our most influential scientists have spent their spare time moonlighting as amateur philosophers. Famous figures like the physiologist Claude Bernard, the biochemist Hans Krebs, the immunologist Peter Medawar, [...]

Published
2010

153. Ghrelin secretion stimulated by [[beta].sub.1]-adrenergic receptors in cultured ghrelinoma cells and in fasted mice

Author

Zhao, Tong-Jin, Sakata, Ichiro, Li, Robert Lin, Liang, Guosheng, Richardson, James A., Brown, Michael S., Goldstein, Joseph L., and Zigman, Jeffrey M.

Subjects
Ghrelin -- Health aspects, Ghrelin -- Genetic aspects, Blood plasma -- Health aspects, Blood plasma -- Genetic aspects, Fasting -- Health aspects, Science and technology
Abstract

Ghrelin, an octanoylated peptide hormone produced in the stomach, rises dramatically in mouse plasma during chronic severe calorie deprivation, an event that is essential to maintain life. The mechanism for this increase is not understood. Here, we study the control of ghrelin secretion in tissue culture cells derived from mice bearing ghrelinomas induced by a tissue-specific SV40 T-antigen transgene. We found that the ghrelin-secreting cells express high levels of mRNA encoding [[beta].sub.1]-adrenergic receptors. Addition of norepinephrine or epinephrine to the culture medium stimulated ghrelin secretion, and this effect was blocked by atenolol, a selective [[beta].sub.1]-adrenergic antagonist. When WT mice were treated with reserpine to deplete adrenergic neurotransmitters from sympathetic neurons, the fasting-induced increase in plasma ghrelin was blocked. Inhibition was also seen following atenolol administration. We conclude that ghrelin secretion during fasting is induced by adrenergic agents released by sympathetic neurons and acting directly on [[beta].sub.1] receptors on the ghrelin-secreting cells of the stomach. endocrine tumors | PG-1 cells | atenolol | octanoate | SV40-T antigen doi/ 10.1073/pnas.1011116107

Published
2010

154. Lasker Awards and papal portraiture: turning fields upside down

Author

Goldstein, Joseph L.

Subjects
Chronic myeloid leukemia -- Care and treatment, Chronic myeloid leukemia -- Research, Portrait-painters -- Achievements and awards, Portraits -- Achievements and awards, Oncology, Experimental -- Genetic aspects, Cancer -- Research, Cancer -- Genetic aspects
Abstract

Picasso has been quoted as saying "my mother said to me, 'If you are a soldier, you will become a general. If you are a monk, you will become a [...]

Published
2009

160. Protein Sensors for Membrane Sterols

Author

Goldstein, Joseph L., DeBose-Boyd, Russell A., and Brown, Michael S.

Subjects
Sterols, Proteins, Sensors, Biological sciences
Abstract

To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.cell.2005.12.022 Byline: Joseph L. Goldstein (1), Russell A. DeBose-Boyd (1), Michael S. Brown (1) Abstract: Cholesterol is an essential component of animal cell membranes, and its concentration is tightly controlled by a feedback system that operates at transcriptional and posttranscriptional levels. Here, we discuss recent advances that explain how cells employ an ensemble of membrane-embedded proteins to monitor sterol concentrations and adjust sterol synthesis and uptake. Author Affiliation: (1) Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA

Published
2006

161. The SREBP Pathway

Author

Radhakrishnan, Arun, primary, Sun, Li-Ping, additional, Espenshade, Peter J., additional, Goldstein, Joseph L., additional, and Brown, Michael S., additional

Published
2010
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162. Unexpected role for IGF-1 in starvation: Maintenance of blood glucose.

Author

Fei Fang, Goldstein, Joseph L., Xuanming Shi, Guosheng Liang, and Brown, Michael S.

Subjects
*BLOOD sugar, *PEPTIDE hormones, *LOW-calorie diet, *ADIPOSE tissues, *STARVATION
Abstract

Wild-type (WT) mice maintain viable levels of blood glucose even when adipose stores are depleted by 6 d of 60% calorie restriction followed by a 23-h fast (hereafter designated as "starved" mice). Survival depends on ghrelin, an octanoylated peptide hormone. Mice that lack ghrelin suffer lethal hypoglycemia when subjected to the same starvation regimen. Ghrelin is known to stimulate secretion of growth hormone (GH), which in turn stimulates secretion of IGF-1 (insulin-like growth factor-1). In the current study, we found that starved ghrelin-deficient mice had a 90% reduction in plasma IGF-1 when compared with starved WT mice. Injection of IGF-1 in starved ghrelindeficient mice caused a twofold increase in glucose production and raised blood glucose to levels seen in starved WT mice. Increased glucose production was accompanied by increases in plasma glycerol, fatty acids and ketone bodies, and hepatic triglycerides. All of these increases were abolished when the mice were treated with atglistatin, an inhibitor of adipose tissue triglyceride lipase. We conclude that IGF-1 stimulates adipose tissue lipolysis in starved mice and that this lipolysis supplies energy and substrates that restore hepatic gluconeogenesis. This action of IGF-1 in starved mice is in contrast to its known action in inhibiting adipose tissue lipase in fed mice. Surprisingly, the ghrelin-dependent maintenance of plasma IGF-1 in starved mice was not mediated by GH. Direct injection of GH into starved ghrelin-deficient mice failed to increase plasma IGF-1. These data call attention to an unsuspected role of IGF-1 in the adaptation to starvation. [ABSTRACT FROM AUTHOR]

Published
2022
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164. Crucial step in cholesterol homeostasis: sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER

Author

Yang, Tong, Espenshade, Peter J., Wright, Michael E., Yabe, Daisuke, Gong, Yi, Aebersold, Ruedi, Goldstein, Joseph L., and Brown, Michael S.

Subjects
Endoplasmic reticulum -- Physiological aspects, Protein metabolism -- Physiological aspects, Homeostasis -- Physiological aspects, Cholesterol -- Physiological aspects, Biological sciences
Abstract

Research describes an endoplasmic reiculum protein, INSIG-1, which binds to the sterol-sensing domain of SREBP cleavage-activating (SCAP) protein in the presence of sterols. Data show that the role of INSIG-1 in cholesterol homeostasis is indicated by its sterol-dependent endoplasmic reticulum retention of the SCAP protein.

Published
2002

167. SREBP cleavage-activating protein (SCAP) is required for increased lipid synthesis in liver induced by cholesterol deprivation and insulin elevation

Author

Matsuda, Morihiro, Korn, Bobby S., Hammer, Robert E., Moon, Young-Ah, Komuro, Ryutaro, Horton, Jay D., Goldstein, Joseph L., Brown, Michael S., and Shimomura, Iichiro

Subjects
Cytochemistry -- Research, Insulin -- Physiological aspects, Cholesterol -- Physiological aspects, Fatty acids -- Physiological aspects, Liver -- Genetic aspects, Proteolysis -- Physiological aspects, Biological sciences
Abstract

Sterol regulatory element-binding protein (SREBP) cleavage-activating protein (SCAP) has been found to be necessary for increased lipid synthesis in liver brought on by cholesterol deprivation and insulin elevation. The SCAP gene was targeted by flanking exon1 with loxP sites, targets for bacteriophage P1Cre recombinase. Mice homozygous for the loxP-tagged SCAP allele were generated. They carry a transgene encoding Cre under control of the interferon-inducible MX1 promoter. The mice have a major lowering in synthesis of cholesterol and fatty acids. They do not have normal increase in the processes in response to insulin or to cholesterol deprivation.

Published
2001

171. FOREWORD

Author

Brown, Michael S., primary and Goldstein, Joseph L., additional

Published
2007
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172. Regulation of mouse sterol regulatory element-binding protein-1c gene (SREBP-1c) by oxysterol receptors, LXR(alpha) and LXR(beta)

Author

Repa, Joyce J., Liang, Guosheng, Ou, Jiafu, Bashmakov, Yuriy, Lobaccaro, Jean-Marc A., Shimomura, Iichiro, Shan, Bei, Brown, Michael S., Goldstein, Joseph L., and Mangelsdorf, David J.

Subjects
Cytochemistry -- Research, Cholesterol -- Physiological aspects, Fatty acids -- Physiological aspects, Cell nuclei -- Physiological aspects, Genetic transcription -- Regulation, Gene expression -- Research, Sterols -- Genetic aspects, Mice -- Genetic aspects, Liver -- Physiological aspects, Biological sciences
Abstract

The liver X receptors (LXRs), members of the nuclear hormone receptor superfamily bound and activated by oxysterols, are discussed. Regulation of mouse sterol regulatory element-binding protein-1c gene (SREBP-1c) by LXR(alpha) and LXR(beta) has been studied. Findings show a unique regulatory relationship between cholesterol and fatty acid metabolism.

Published
2000

173. Regulated step in cholesterol feedback localized to budding of SCAP from ER membranes

Author

Nohturfft, Axel, Yabe, Daisuke, Goldstein, Joseph L., Brown, Michael S., and Espenshade, Peter J.

Subjects
Cholesterol -- Physiological aspects, Metabolic regulation -- Analysis, Endoplasmic reticulum -- Physiological aspects, Sterols -- Physiological aspects, Biological sciences
Abstract

Results demonstrate that in sterol-treated mammalian cells, the polytopic membrane SREBP Cleaving-Activating-Protein budding is reduced. Data further point out that the budding is from endoplasm reticulum of the sterol treated cells.

Published
2000

174. Regulated Intramembrane Proteolysis

Author

Brown, Michael S., Ye, Jin, Rawson, Robert B., and Goldstein, Joseph L.

Subjects
Proteolysis, Biological sciences
Abstract

To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/S0092-8674(00)80675-3 Byline: Michael S Brown (1), Jin Ye (1), Robert B Rawson (1), Joseph L Goldstein (1) Author Affiliation: (1) Department of Molecular Genetics, University of Texas Southwestern, Medical Center, Dallas, Texas 75390-9046, USA

Published
2000

175. Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans

Author

Brown, Michael S., Ye, Jin, Rawson, Robert B., and Goldstein, Joseph L.

Subjects
Cytochemistry -- Research, Cellular signal transduction -- Physiological aspects, Plasma membranes -- Physiological aspects, Homology (Biology) -- Physiological aspects, Endoplasmic reticulum -- Physiological aspects, Membrane proteins -- Physiological aspects, Proteolysis -- Research, Cellular control mechanisms -- Research, Biological sciences
Abstract

Regulated intramembrane proteolysis (Rip), a control mechanism, is discussed in this review article. The mechanism is conserved from bacteria to humans. Conceptual convergence is now seen in the cell signaling field. Transmembrane proteins can be cleaved within the plane of the membrane of the cell to let out cytosolic fragments. The fragments can go into the nucleus to manage gene transcription. The mechanism is called Rip. Five proteins known or thought to undergo Rip in animal cells are SREBP, APP, Notch, Ire1 and ATF6, and there are two in bacteria.

Published
2000

176. Transport-dependent proteolysis of SREBP: relocation of Site-1 protease from Golgi to ER obviates the need for SREBP transport to Golgi

Author

DeBose-Boyd, Russell A., Brown, Michael S., Li, Wei-Ping, Nohturfft, Axel, Goldstein, Joseph L., and Espenshade, Peter J.

Subjects
Proteolysis -- Physiological aspects, Golgi apparatus -- Physiological aspects, Endoplasmic reticulum -- Physiological aspects, Cholesterol metabolism -- Research, Biological sciences
Abstract

Results demonstrate that active domains of sterol regulatory element binding proteins (SREBPs) complexing with SREBP cleavage-activating protein (SCAP) carries the former from endoplasm reticulum to Golgi and are cleaved by Site-1 protease (S1P). The data suggest that shifting S1P from Golgi to endoplasm reticulum obviates this pathway for SREBP.

Published
1999

177. Leptin reverses insulin resistance and diabetes mellitus in mice with congenital lipodystrophy

Author

Shimomura, Iichiro, Hammer, Robert E., Ikemoto, Shinji, Brown, Michael S., and Goldstein, Joseph L.

Subjects
Insulin resistance -- Research, Leptin -- Physiological aspects, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Insulin resistance in a mouse model that mimics the features of congenital generalized lipodystrophy is the result of a deficiency of leptin. This deficiency is secondary to a failure of adipocyte infusion of physiological amounts of leptin. Leptin deficiency does not lead to insulin resistance in these mice through ingestion of excess calories, as caloric limitation significantly cut body weight without reversing the hyperinsulinaemia or hyperglycaemia. It is suggested that leptin modulates insulin sensitivity and glucose disposal independently of its impact on food intake.

Published
1999

184. Contributors

Author

Abrams, John M., primary, Adelman, John P., additional, Alcorn, Joseph L., additional, Alessi, Dario R., additional, Alexov, Emil, additional, Alford, Simon, additional, Alitalo, Kari, additional, Allison, James P., additional, Almo, Steven C., additional, Alory, Christelle, additional, Al-Shamkhani, Aymen, additional, Amundson, Sally A., additional, Anderson, Carl W., additional, Andersen, Jannik N., additional, Angel, Peter, additional, Appella, Ettore, additional, Arendshorst, William J., additional, Arkinstall, Steve, additional, Audhya, Anjon, additional, Avruch, Joseph, additional, Bader, Gary D., additional, Bagala, Cinzia, additional, Balch, William E., additional, Balsinde, Jesus, additional, Banerjee, Utpal, additional, Barford, David, additional, Bar-Sagi, Dafna, additional, Bartlett, Perry F., additional, Bastiaens, Philippe I.H., additional, Battelli, Chiara, additional, Baudhuin, Linnea M., additional, Beavil, Andrew J., additional, Beavil, Rebecca L., additional, Beavo, Joseph A., additional, Bello-Reuss, Elsa, additional, Bellum, Stephen, additional, Belmonte, Juan Carlos Izpisúa, additional, Bennett, Craig B., additional, Benovic, Jeffrey L., additional, Berridge, Michael J., additional, Beuning, Penny J., additional, Bhandari, Rashna, additional, Bhattacharya, Ananya, additional, Biel, Martin, additional, Bielinski, Vincent A., additional, Bilak, Hana, additional, Birnbaumer, Lutz, additional, Birrell, Geoff, additional, Bishop, Gail A., additional, Blackmer, Trillium, additional, Blackshear, Perry J., additional, Blattner, Christine, additional, Blaustein, Mordecai P., additional, Bokoch, Gary M., additional, Bonewald, Lynda F., additional, Bonomi, Marco, additional, Booden, Michelle A., additional, Boone, Charles, additional, Bootman, Martin D., additional, Bos, Johannes L., additional, Bradbury, Jane M., additional, Bradshaw, Ralph A., additional, Bresnick, Anne R., additional, Brevnova, Lena, additional, Brinkworth, Ross I., additional, Brown, Michael S., additional, Brown, Steven A., additional, Brunet, Anne, additional, Bucki, Robert, additional, Burgoyne, Robert D., additional, Buss, Janice E., additional, Butow, Ronald A., additional, Capdevila, Javier, additional, Carafoli, Ernesto, additional, Carlson, Cathrine R., additional, Carpenter, Graham, additional, Carrillo, Juan J., additional, Casey, Patrick J., additional, Catterall, William A., additional, Cerione, Richard A., additional, Cesareni, Gianni, additional, Chan, Andrew C., additional, Chang, Geoffrey, additional, Chao, Moses V., additional, Charbonneau, Harry, additional, Chen, Philip, additional, Cheng, Alan, additional, Chiu, Chris, additional, Chow, Dar-chone, additional, Chrisman, Ted D., additional, Christensen, Anne Elisabeth, additional, Chung, Jee Y., additional, Churchill, Grant C., additional, Ciechanover, Aaron, additional, Cingolani, Gino, additional, Claeysen, Sylvie, additional, Closset, Jean, additional, Cockcroft, Shamshad, additional, Cohen, Patricia T.W., additional, Cohen, Philip, additional, Colbran, Roger J., additional, Comstock, Clay E.S., additional, Conti, Marco, additional, Corbin, Jackie D., additional, Corda, Daniela, additional, Costagliola, Sabine, additional, Cote, Rick H., additional, Coughlin, Shaun R., additional, Cowart, L. Ashley, additional, Cox, Adrienne D., additional, Cragg, Mark S., additional, Crespo, José L., additional, Crosio, Claudia, additional, Daly, Christopher, additional, Damak, Sami, additional, Dasso, Mary, additional, David, Michael, additional, Davis, Anthony J., additional, Davis, Roger J., additional, Day, Richard N., additional, Degerman, Eva, additional, DeLano, Warren L., additional, Dell'Acqua, Mark L., additional, Délot, Emmanuèle, additional, Demple, Bruce, additional, Dennis, Edward A., additional, Denu, John M., additional, DePaoli-Roach, Anna A., additional, Der, Channing J., additional, de Rooij, Johan, additional, de Sauvage, Frederic, additional, Devreotes, Peter N., additional, Dewaste, Valérie, additional, Dickson, Robert B., additional, Diebold, Becky A., additional, Fiori, Pier Paolo Di, additional, Girolamo, Maria Di, additional, Diplexcito, Julie, additional, Dixon, Jack E., additional, Doms, Robert W., additional, Donoghue, Daniel J., additional, Doolittle, Russell F., additional, Døskeland, Stein Ove, additional, Dostmann, Wolfgang R.G., additional, Dreyer, Matthias K., additional, Du, Guo Guang, additional, Du, Keyong, additional, Duchen, Michael R., additional, Dunphy, William G., additional, Durgan, Joanne, additional, Dustin, Michael L., additional, Edwards, Peter A., additional, Egen, Jackson G., additional, Eiden, Lee E., additional, Elion, Elaine A., additional, Emr, Scott, additional, Engelhardt, Othmar G., additional, Erneux, Christophe, additional, Espenshade, Peter J., additional, Esplin, Edward D., additional, Evers, B. Mark, additional, Eyles, Joanne L., additional, Fame, Sheelagh, additional, Farquhar, Marilyn, additional, Feil, Robert, additional, Feng, Gui-Jie, additional, Fields, Stanley, additional, Fiordalisi, James J., additional, Firtel, Richard A., additional, Fitzgerald, Garret A., additional, Flint, Andrew, additional, Foiani, Marco, additional, Forman, Barry Marc, additional, Fornace, Albert J., additional, Francis, Sharron H., additional, Fritz, Günter, additional, Fruman, David A., additional, Galione, Antony, additional, Gandhi, Chris S., additional, Garbers, David L., additional, Garcia, K. Christopher, additional, Geiger, Benjamin, additional, Gerace, Larry, additional, Gerstner, Andrea, additional, Giaccia, Amato J., additional, Giannattasio, Michele, additional, Giguère, Vincent, additional, Glass, Christopher K., additional, Glennie, Martin J., additional, Glick, Jennifer L., additional, Goldstein, Joseph L., additional, Gopal, Venkatesh, additional, Gorospe, Myriam, additional, Govaerts, Cedric, additional, Graves, Paul R., additional, Gray, Patrick W., additional, Graziani, Irene, additional, Green, Douglas R., additional, Greenberg, Michael E., additional, Greenwald, Iva, additional, Gu, Haihua, additional, Gueven, Nuri, additional, Gutkind, J. Silvio, additional, Haeggström, Jesper Z., additional, Hall, Alan, additional, Hall, Michael N., additional, Haller, Otto, additional, Hamm, Heidi E., additional, Hannun, Yusef A., additional, Hansen, Carl A., additional, Harden, T. Kendall, additional, Hardie, D. Grahame, additional, Hasegawa, Kiminori, additional, Hawkins, Phillip T., additional, Haystead, Timothy A.J., additional, He, Xiao-lin, additional, Heizmann, Claus W., additional, Heldin, Carl-Henrik, additional, Hermiston, Michelle L., additional, Herrlich, Peter, additional, Hewat, Elizabeth A., additional, Hille, Bertil, additional, Hilton, Douglas J., additional, Hinchliffe, K.A., additional, Ho, Steffan N., additional, Ho, Su-Chin, additional, Hochstrasser, Mark, additional, Hofmann, Franz, additional, Hogue, Christopher W., additional, Hol, Wim G.J., additional, Holash, Jocelyn, additional, Holmgren, Robert A., additional, Honig, Barry, additional, Hostager, Bruce S., additional, Hubbard, Stevan R., additional, Huber, Michael, additional, Hunter, Tony, additional, Huttenlocher, Anna, additional, Hymowitz, Sarah G., additional, Ihle, James N., additional, Imler, Jean-Luc, additional, Irvine, R.F., additional, Isacoff, Ehud Y., additional, Iturrioz, Xavier, additional, Iversen, Lars F., additional, Iyengar, Ravi, additional, Jackson, Stephen P., additional, Jan, Lily Yeh, additional, Janiak-Spens, Fabiola, additional, Janmey, Paul A., additional, Jansen, Peter Gildsig, additional, Jarriault, Sophie, additional, Javitch, Jonathan A., additional, Jensen, Elwood V., additional, Jepsen, Kristen, additional, Jones, E. Yvonne, additional, Jones, Katherine A., additional, Jordan, J. Dedrick, additional, Joseph, Jomon, additional, Justement, Louis B., additional, Kafri, Yariv, additional, Kahn, Richard A., additional, Kang, Shin W., additional, Karlin, Arthur, additional, Kast-Woelbern, Heidi R., additional, Kaufman, Randal J., additional, Kazlauskas, Andrius, additional, Keen, James H., additional, Kemler, Rolf, additional, Kemp, Bruce E., additional, Kennedy, Mary B., additional, Kennedy, Matthew A., additional, Kikkawa, Ushio, additional, Kim, Albert H., additional, Kim, Soo-A, additional, Kim, Sung-Hou, additional, Kim, Youngjoo, additional, King-Jones, Kirst, additional, Kintner, Chris, additional, Kivimäe, Saul, additional, Klee, Claude B., additional, Klein, Rüdiger, additional, Kleppisch, Thomas, additional, Kliewer, Steven A., additional, Klinghoffer, Richard A., additional, Knoblich, Juergen A., additional, Kobe, Bostjan, additional, Kochs, George, additional, Kong-Beltran, Monica, additional, König, Rolf, additional, Koong, Albert C., additional, Korc, Murray, additional, Kornitzer, Daniel, additional, Kossiakoff, Anthony A., additional, Kotera, Jun, additional, Kovalenko, M.V., additional, Kozasa, Tohru, additional, Kozlov, Sergei, additional, Kozminski, Keith G., additional, Krugmann, Sonja, additional, Kuriyan, John, additional, Kurokawa, Riki, additional, Kwong, Peter D., additional, Lai, Wi S., additional, Lamar, Elise, additional, Lambert, Millard H., additional, Lambright, David G., additional, Lancet, Doron, additional, Landry, Reiko, additional, Langdon, Wallace Y., additional, Langeberg, Lorene K., additional, Lasko, Paul, additional, Latham, Vaughn, additional, Lavin, Martin F., additional, Lease, Kevin A., additional, Leffler, Hakon, additional, Lemmon, Mark A., additional, Leonard, Ann E., additional, Levitzki, Alexander, additional, Liao, Hong-Jun, additional, Liaw, Lucy, additional, Liberi, Giordano, additional, Lickert, Heiko, additional, Liddington, Robert C., additional, Lincoln, Thomas M., additional, Linder, Jürgen U., additional, Linder, Maurine E., additional, Liu, Hui, additional, Liu, Zhengchang, additional, Lohela, Marja K., additional, Louie, Sarah H., additional, Luttrell, Deirdre K., additional, Luttrell, Louis M., additional, Lyons, Karen M., additional, Macaulay, S. Lance, additional, Maceyka, Michael, additional, Maciag, Thomas, additional, Macian, Fernando, additional, MacKintosh, Carol, additional, MacLennan, David H., additional, Mahmood, Nadir A., additional, Malbon, Craig C., additional, Malik, Sohail, additional, Man, Orna, additional, Manahan, Carol L., additional, Mandinova, Anna, additional, Manganiello, Vincent C., additional, Manley, James L., additional, Mann, Matthias, additional, Manning, Gerald, additional, Manser, Ed, additional, Margeta-Mitrovic, Marta, additional, Margolskee, Robert F., additional, Marinissen, Julia, additional, Mariuzza, Roy A., additional, Marmor, Mina D., additional, Martin, G. Steven, additional, Martin, Karen H., additional, Martinez, Sergio E., additional, Mathews, Michael B., additional, Mayer, Bruce J., additional, Mayer, Mark L., additional, Mazzoni, Maria R., additional, McCormick, Frank, additional, McGowan, Clare H., additional, McKay, Melissa M., additional, McKeehan, Wallace L., additional, McLean, Alison J., additional, Means, Anthony R., additional, Meili, Ruedi, additional, Meng, Jingwei, additional, Merchant, Mark, additional, Mercurio, Frank, additional, Milligan, Graeme, additional, Ming, Guo-Li, additional, Minor, Daniel L., additional, Moghal, Nadeem, additional, Møller, Neils Peter H., additional, Mongillo, Marco, additional, Montminy, Marc, additional, Moon, Randall T., additional, Morimoto, Richard I., additional, Moss, Stephen E., additional, Mott, Helen R., additional, Mouta, Carla, additional, Muda, Marco, additional, Mumby, Marc C., additional, Murphy, Gretchen A., additional, Muzi-Falconi, Marco, additional, Nagaraj, Raghavendra, additional, Nahorski, Stefan R., additional, Nairn, Angus C., additional, Nash, Piers, additional, Neel, Benjamin G., additional, Newton, Alexandra C., additional, Nishizuka, Yasutomi, additional, Noel, Joseph P., additional, Nollen, Ellen A.A., additional, Nooren, Irene M.A., additional, O'Connor, Rodney, additional, Offermanns, Stefan, additional, Olender, Tsviya, additional, Ong, Shao-En, additional, Owen, Darerca, additional, Pagliari, Lisa J., additional, Pao, Lily, additional, Papaconstantinou, John, additional, Pardo, Leonardo, additional, Park, Hay-Oak, additional, Park, Young Chul, additional, Parker, Peter J., additional, Parsons, J. Thomas, additional, Passner, J.M., additional, Pawson, Tony, additional, Pelliccioli, Achille, additional, Perez-Polo, J. Regino, additional, Perrimon, Norbert, additional, Petite, Fabrice G., additional, Petroulakis, Emmanuel, additional, Pfaff, Samuel L., additional, Piehler, Jacob, additional, Pike, Linda J., additional, Pinkoski, Michael J., additional, Pixley, Fiona J., additional, Plevani, Paolo, additional, Poo, Mu-ming, additional, Pozzan, Tullioi, additional, Prescott, Stephen M., additional, Prudovsky, Igor, additional, Putney, James W., additional, Radimerski, Thomas, additional, Radzio-Andzelm, Elzbieta, additional, Ram, Prahlad T., additional, Rameh, Lucia, additional, Ramljak, Danica, additional, Ranscht, Barbara, additional, Rao, Anjana, additional, Raport, Carol J., additional, Reeves, Jacqueline D., additional, Rehman, Holger, additional, Reichman, Trevor W., additional, Reiter, Eric, additional, Resnick, Michael A., additional, Reth, Michael, additional, Rhee, Sue Goo, additional, Richter, Joel D., additional, Rietze, Rodney L., additional, Rini, James M., additional, Ripperger, Jürgen A., additional, Rizo, Josep, additional, Robishaw, Janet D., additional, Roderick, H. Llewelyn, additional, Roeder, Robert G., additional, Rohrschneider, Larry R., additional, Ron, David, additional, Rosenfeld, Michael G., additional, Rosenfeldt, Hans, additional, Rossman, Kent L., additional, Roth, Christopher B., additional, Rudolph, Markus G., additional, Ruppelt, Anja, additional, Saez, Lino, additional, Sakmar, Thomas P., additional, Salvesen, Guy S., additional, Sassone-Corsi, Paolo, additional, Saxe, Charles L., additional, Schäfer, Beat W., additional, Schibler, Ueli, additional, Schindler, Christian W., additional, Schmelzle, Tobias, additional, Schmid, Sandra L., additional, Schmidt, Anja, additional, Schmidt, Eric F., additional, Schreiber, Gideon, additional, Schultz, Joachim E., additional, Schwaller, Beat, additional, Schwamborn, Klaus, additional, Schwartz, Thue, additional, Schwindinger, William F., additional, Scita, Giorgio, additional, Scott, John D., additional, Scott, Shaun, additional, Seebeck, Thomas, additional, Serhan, Charles N., additional, Shabb, John B., additional, Shaw, Andrey S., additional, Shears, Stephen B., additional, Shenolikar, Shirish, additional, Shi, Lei, additional, Shin, Chanseok, additional, Shiozaki, Kazuhiro, additional, Shokat, Kevan M., additional, Shuttleworth, Trevor J., additional, Siderovski, David P., additional, Siegelbaum, Steven A., additional, Silverstein, Adam M., additional, Singer, Robert H., additional, Skinner, Michael K., additional, Slack-Davis, Jill K., additional, Smerdon, Stephen J., additional, Smith, Graeme C.M., additional, Smits, Guillaume, additional, Smolik, Sarah M., additional, Smotrys, Jessica E., additional, Smyth, Emer M., additional, Snyder, Jason T., additional, Sogame, Naoko, additional, Soldi, Raffaella, additional, Sondek, John, additional, Sonenberg, Nahum, additional, Sonneberg, Erica Dutil, additional, Sparrow, Lindsay G., additional, Spiegel, Sarah, additional, Sprang, Stephen R., additional, Srivastava, Deepak, additional, Stanfield, Robyn L., additional, Stanley, E. Richard, additional, Stauber, Deborah J., additional, Stefan, Christopher, additional, Stenson-Holst, Lena, additional, Stephens, Len, additional, Sternberg, Paul W., additional, Sternweis, Paul C., additional, Steward, Ruth, additional, Stickney, John T., additional, Stoker, Andrew W., additional, Strittmatter, Stephen M., additional, Stronach, Beth E., additional, Strong, Roland K., additional, Stroud, Robert M., additional, Südhof, Thomas C., additional, Sunahara, Roger K., additional, Sutton, Brian J., additional, Szabolcs, Sipeki, additional, Tang, Xiao-Bo, additional, Taskén, Kjetil, additional, Tatebe, Hisashi, additional, Tauszig-Delamasure, Servane, additional, Taylor, Colin W., additional, Taylor, Garry L., additional, Taylor, Laura J., additional, Taylor, Susan S., additional, Thomas, George, additional, Thomas, Robert P., additional, Thompson, E. 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Published
2003
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186. The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor

Author

Brown, Michael S. and Goldstein, Joseph L.

Subjects
Cytology -- Genetic aspects, DNA-ligand interactions -- Research, Cholesterol metabolism -- Genetic aspects, Biological sciences
Abstract

Sterol regulatory element binding proteins (SREBP) control transcription of cholesterol synthesis by regulating the transcription of 3-hydroxy-3-methyl- glutaryl coenzyme A (HMGCoA) reductase, an enzyme responsible for controllinglevels of cholesterol in the body, regulates LDL receptor which supplies cholesterol through receptor-mediated endocytosis, and also adjusts transcription of genes encoding enzymes of fatty acid synthesis and uptake. To accomplish transcription, SREBPs should be cleaved from the membrane to enter the nucleus and this process is facilitated by mutant SREBP cleavage activation protein (SCAP).

Published
1997

189. Science Over Politics

Author

Lanza, Robert P., Arrow, Kenneth J., Axelrod, Julius, Baltimore, David, Benacerraf, Baruj, Bloch, Konrad E., Bloembergen, Nicolaas, Brown, Herbert C., Brown, Michael S., Cibelli, Jose B., Cohen, Stanley, Cooper, Leon N., Corey, E. J., Dulbecco, Reneto, Fischer, Edmond H., Fitch, Val L., Friedman, Jerome I., Friedman, Milton, Furchgott, Robert F., Gell-Mann, Murray, Glaser, Donald A., Glashow, Sheldon Lee, Gilbert, Walter, Goldstein, Joseph L., Gould, Stephen Jay, Guillemin, Roger, Hauptman, Herbert A., Herschbach, Dudley, Hoffman, Roald, Hood, Leroy, Hubel, David H., Karle, Jerome, Kelin, Lawrence R., Kohn, Walter, Kornberg, Arthur, Krebs, Edwin G., Lederman, Leon M., Lederberg, Joshua, Lee, David M, Lucas, Robert E., Marcus, Rudolph A., Merrifield, R. Bruce, Miller, Merton H., Modigliani, Franco, Molina, Mario J., Mullis, Kary, Murad, Ferid, Murray, Joseph E., Nathans, Daniel, Nirenberg, Marshall W., North, Douglass C., Olah, George A., Palade, George E., Ramsey, Martin F., Richter, Burton, Roberts, Richard J., Robl, James M., Samuelson, Paul A., Schwartz, Melvin, Sharp, Phillip A., Smalley, Richard E., Smith, Hamilton O., Solow, Robert M., Taube, Henry, Tonegawa, Susumu, Watson, James D., Weinberg, Steven, Weller, Thomas H., West, Michael d., Wieschaus, Eric F., Wiesel, Torsten N., and Wilson, Robert W.

Published
1999

190. Sterol resistance in CHO cells traced to point mutation in SREBP cleavage-activating protein

Author

Hua, Xianxin, Nohturfft, Axel, Goldstein, Joseph L., and Brown, Michael S.

Subjects
Cholesterol metabolism -- Genetic aspects, Sterols -- Genetic aspects, Carrier proteins -- Genetic aspects, Biological sciences
Abstract

Sterol regulatory element binding proteins-1 and -2 (SREBP) are key molecules in the cholesterol feedback system. Cleavage of transcription factors SREBP-1 and -2 causes the release of the NH2-terminal segment into the cytosol via the proteolytic pathway. Studies on Chinese hamster ovary cells with defects in feedback regulation have shown that sterols play an important role in the regulation of the feedback system. The accumulation of sterols turns off the protease which clips SREBP activity.

Published
1996

191. Sterol-regulated release of SREBP-2 from cell membranes requires two sequential cleavages, one within a transmembrane segment

Author

Sakai, Juro, Duncan, Elizabeth A., Rawson, Robert B., Hua, Xianxin, Brown, Michael S., and Goldstein, Joseph L.

Subjects
Membrane proteins -- Research, Sterols -- Physiological aspects, Proteolysis -- Analysis, Biological sciences
Abstract

The mechanism of release of sterol regulatory element binding proteins (SREBPs) from the endoplasmic reticulum membranes is a complex two-stage process. The first step, involving a cleavage near or at the Arg-519 in the lumenal loop, produces an intermediate of SREBP-2 that is membrane-bound. The cleavage is regulated by sterols. The second cleavage which is independent of sterols takes place within the transmembrane region. The second cleavage liberates the NH2-terminal mature form of SREBP-2 which translocates to the nucleus.

Published
1996

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