Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Wei-Jia Ou"'
Publikováno v:
Journal of Biological Chemistry. 270:18051-18059
The type I membrane protein calnexin functions as a molecular chaperone for secretory glycoproteins in the endoplasmic reticulum with ATP and Ca2+ as two of the cofactors involved in substrate binding. Protease protection experiments with intact cani
Autor:
John J.M. Bergeron, Francois Authier, Wei-Jia Ou, Richard A. Rachubinski, Paul A. Walton, Barry I. Posner
Publikováno v:
Proceedings of the National Academy of Sciences. 92:3859-3863
A peroxisomal location for insulin-degrading enzyme (IDE) has been defined by confocal immunofluorescence microscopy of stably transfected CHO cells overexpressing IDE and digitonin-permeabilization studies in normal nontransfected fibroblasts. The f
Autor:
Mahmoud Aminlari, Thomas Asquith, Katherine Sarlo, Jerome M. Bailey, Oanh Tu, Gilbert Issai, Alice Ha, John E. Shively, Alexander W. Bell, Nicole C. Baur, John J. M. Bergeron, Wei -Jia Ou, David Y. Thomas, Katherine Cianflone, Allain Baldo, Maxwell T. Hincke, Richard L. Momparler, Josée Laliberté, David M. P. Thomson, M. Sutherland, Vladimir Besada, Javier Gonzalez, Gabriel Padron, Hilda Garay, Osvaldo Reyes, Toshifumi Takao, Yasutsugu Shimonishi, Rainer Bischoff, Dominique Roecklin, Bernadette Bouchon, Klaus Klarskov, Alain Van Dorsselaer, Patricia G. Brake, Anne Pacitti, Terry Higgins, Panos Stevis, John Malinowski, Sue McElhiney, Janes Huang, Christine Vestal, Scott D. Buckel, Tracy Stevenson, Joseph A. Loo, Martin Caffrey, Jin Wang, Carmichael J. A. Wallace, Ian Clark-Lewis, C. A. Carothers Carraway, J. Huang, Y. Li, S. -H. Juang, A. Gallo, B. J. Mayer, K. L. Carraway, Patrick L. Coleman, Daniel Sarpong, David W. Deerfield, Amanda Holland-Minkley, John D. Hempel, Hugh B. Nicholas, Nancy D. Denslow, Leroy C. Folmar, Craig V. Sullivan, James D. Dixon, Jonathan P. Mark, Christopher P. Elicone, Simin D. Maleknia, Brian F. McGuinness, Fred E. Regnier, Noubar B. Afeyan, Julia M. Dolence, C. Dale Poulter, Tsezi Egorov, Alexander Musolyamov, Yves Popineau, Jens Andersen, Peter Roepstorff, Roberto J. Falkenstein, Mirtha J. Biscoglio de Jiménez Bonino, Clara Peña, D. L. Gauggel, T. N. Asquith, R. J. Isfort, N. S. Miller, D. B. Cody, Michael F. Giblin, Tuck C. Wong, Thomas P. Quinn, Gregory A. Grant, Mark W. Crankshaw, Scott Griffith, Steve Schroeder, Thomas Quinn, F. Guinet, Y. Petillot, J. M. Chapsal, J. Dubayle, F. Greco, O. Barge, E. Forest, C. Valentin, Frederick M Hahn, Jonathan A. Baker, Mitsuru Haniu, William C. Kenney, Michael F. Rohde, James G. Harman, Eun Ju Lee, Joel Glasgow, Sew Fen Lew, Ali O. Belduz, Reed J. Harris, Michael S. Molony, Lene H. Keyt, Shiaw -Lin Wu, David H. Hawke, Jaqueline Tso, Sherrell Early, Chad G. Miller, G. Thomas Hayman, Jan A. Miernyk, Ulf Hellman, Christer Wernstedt, Jorge Góñez, Daniel Hess, Ralph Studer, Peter E. Hunziker, Hisashi Hirano, Yoshihiro Watanabe, Sergei F. Barbashov, Setsuko Komatsu, Andrew M. Hemmings, Masaru Miyagi, Susumu Tsunasawa, Reuben E. Huber, Nathan J. Roth, Michael T. Gaunt, Paul Jenö, Thierry Mini, Suzette Moes, Martin Horst, Kenji Jinnai, Tetsuo Ashizawa, M. Zouhair Atassi, Anders H. Johnsen, Hanne Jensen, Jens F. Rehfeld, Masaharu Kamo, Takao Kawakami, Norifumi Miyatake, Akira Tsugita, JN Keen, PF Zagalsky, JBC Findlay, Regine Kraft, Susanne Kostka, Enno Hartmann, Henry C. Krutzsch, John K. Inman, Claudia Machalinski, Mirtha Biscoglio de Jiménez Bonino, Donald K. McRorie, Gregg R. Dieckmann, Susan Heilman, William F. DeGrado, Vincent L. Pecoraro, James Kenny, Julie Sahakian, Jacqueline Tso, Mary B. Moyer, William A. Burkhart, Tatyana Muranova, Lubov Makova, Hugh Nicholas, John Hempel, Amy Hinich, David Deerfield, Joseph Behrmann, Alex Ropelewski, Lori Nixon, Leonard Maneri, Kerry Nugent, Ken Stoney, John Wieser, Hiroshi Ohguro, Krzysztof Palczewski, Kenneth A. Walsh, Richard S. Johnson, Leonard C Packman, Carl Webster, John Gray, G. Padrón, V. Morera, L. J. González, Y. Támbara, V. Besada, R. Villalonga, G. Chinea, O. Reyes, H. Garay R. Bringas, C. Nazábal, Bruce P. Parkinson, Kent A. Yamada, Anne Randolph, Anthony Pisano, Nicole H. Packer, John W. Redmond, Keith L. Williams, Andrew A. Gooley, Hanne H. Rasmussen, Ejvind Mørtz, Matthias Mann, Julio E. Celis, Lone K. Rasmussen, Esben S. Sørensen, Torben E. Petersen, Jørgen Gliemann, Poul Henning Jensen, Staffan Renlund, Henrik Wadensten, Annika Persson, Per Persson, Agneta Johansson, Per -Olof Edlund, Donald J. Rose, Ragna Sack, Alex Apffel, Chad Miller, Rodney L. Levine, Kazuyasu Sakaguchi, Nicola Zambrano, Marc S. Lewis, Eric T. Baldwin, Bruce A. Shapiro, John W Erickson, James G. Omichinski, G. Marius Clore, Angela M. Gronenborn, Ettore Appella, Werner Schröder, Irmgard Moser, Werner Pansegrau, Erich Lanka, Richard J. Simpson, James Eddes, Hong Ji, Gavin E. Reid, Robert L. Moritz, Peter Højrup, David W. Speicher, David F. Reim, Kaye D. Speicher, B. R. Srinivasa, S. P. Barde, William G. Stirtan, Alyona Sukhanova, Sergey Vorob'ev, Alexander Gabibov, Igor Bronstein, Kenji Tanaka, Kuniko Einaga, Minoru Tsukada, Jonathan F. Tait, Kazuo Fujikawa, Keiji Takamoto, Kazuo Satake, Ilya A. Vakser, V. V. Velikodvorskaia, A. G. Gabibov, A. G. Rabinkov, Tennie Videler, Michael Osborne, Geoffrey Moore, Richard James, Colin Kleanthous, Jane H. Walent, Richard Bessen, Dick Marsh, Ronald L. Niece, Francis H. C. Tsao, Hong Wang, Scot R. Weinberger, Lynn M. Chakel, Ewald M. Wondrak, Alan R. Kimmel, John M. Louis
Publikováno v:
Journal of Protein Chemistry. 13:515-543
Publikováno v:
Journal of Biological Chemistry. 269:7464-7472
The endoplasmic reticulum (ER) not only links the translational machinery to the endomembrane system in eukaryotic cells but also provides a protective environment for the folding of exoplasmic proteins translocated across the ER membrane. Here we de
Publikováno v:
Journal of Biological Chemistry. 267:23789-23796
Signal sequence receptor alpha (SSR alpha) and calnexin are major calcium-binding proteins of the endoplasmic reticulum (ER) which are implicated in chaperone functions. They were identified as major membrane substrates after in vitro phosphorylation
Autor:
D. Rindress, Alexander W. Bell, Ikuo Wada, John J.M. Bergeron, Wei-Jia Ou, David Y. Thomas, D. Dignard, J.J. Doherty nd, Daniel Louvard, Pamela H. Cameron
Publikováno v:
Journal of Biological Chemistry. 266:19599-19610
GTP phosphorylation of rough microsomes in vitro is limited to four integral membrane proteins. Two of these, a phosphoprotein (pp90) and a phosphoglycoprotein (pgp35) were purified as a complex with two nonphosphorylated membrane glycoproteins, gp25
Autor:
Pamela H. Cameron, Wei-Jia Ou, André Zapun, David Y. Thomas, Francesco Parlati, R. Hemming, John J.M. Bergeron
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9781461374572
It has often been speculated that one of the selective forces for the evolution of Nlinked glycosylation is that of productive protein folding. Strong experimental support has now been put forward as a consequence of studies with the endoplasmic reti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::55d69b47089ace4a8553c54fa348f765
https://doi.org/10.1007/978-1-4615-5383-0_11
https://doi.org/10.1007/978-1-4615-5383-0_11
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 93(18)
The HIV-1 envelope glycoprotein gp120 displays inefficient intracellular transport, which is caused by its retention in the endoplasmic reticulum. Coexpression in insect cells (Sf9) of HIV-1 gp120 with calnexin has shown that their interaction was mo
Publikováno v:
Calreticulin ISBN: 9783662062050
The endoplasmic reticulum is the entry point into the secretory pathway for the majority of soluble secreted proteins and membrane proteins (collectively termed secretory proteins). Within the endoplasmic reticulum secretory proteins have their signa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::595f856c358d1d7bfc5e5c74d96e4544
https://doi.org/10.1007/978-3-662-06203-6_4
https://doi.org/10.1007/978-3-662-06203-6_4
Publikováno v:
The EMBO journal. 13(18)
Rat liver parenchyma harbors equal numbers of epidermal growth factor (EGF) and insulin receptors. Following administration of a saturating dose of EGF (10 micrograms/100 g body weight), there was a rapid (t1/2 approximately 1.1 min) internalization