Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Paul C.R. Hopkins"'
Publikováno v:
Journal of Lipid Research, Vol 43, Iss 11, Pp 1881-1889 (2002)
We present a murine model that examines the effects of macrophage-produced apolipoprotein E3 (apoE3) and apoE4 on VLDL and high density lipoprotein (HDL) metabolism. Mice expressing apoE3 on the Apoe−/− background had substantially lower VLDL lev
Externí odkaz:
https://doaj.org/article/95e56aedea884033ad13810c60474a2d
Autor:
Eliezer Masliah, Ina Tesseur, Paul C.R. Hopkins, Qin Xu, Kimberly Scearce-Levie, Lisa Kekonius, Robert W. Mahley, Jo Dee Fish, Walter J. Brecht, Faith M. Harris, Karl H. Weisgraber, Tony Wyss-Coray, Lennart Mucke, Yadong Huang
Publikováno v:
Proceedings of the National Academy of Sciences. 100:10966-10971
Apolipoprotein (apo) E4 increases the risk and accelerates the onset of Alzheimer's disease (AD). However, the underlying mechanisms remain to be determined. We previously found that apoE undergoes proteolytic cleavage in AD brains and in cultured ne
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9dcfa63bba7f6bcf96092c6b30a725a7
https://doi.org/10.1073/pnas.1434398100
https://doi.org/10.1073/pnas.1434398100
Autor:
Pierre Lavigne, Lyne Bissonnette, Erick K. Dufour, Paul C.R. Hopkins, Jean-Bernard Denault, Richard Leduc
Publikováno v:
Journal of Biological Chemistry. 276:38971-38979
A series of mutants incorporating furin recognition sequences within the P6-P1 region of the reactive site loop of alpha(1)-antitrypsin were constructed. Variants containing different combinations of basic residues in the P1, P2, P4, and P6 positions
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e2e86a55539b1b179e9971d749a9e01
https://doi.org/10.1074/jbc.m102959200
https://doi.org/10.1074/jbc.m102959200
Autor:
Bernard Le Bonniec, Paul C.R. Hopkins, Stephen P. Bottomley, James C. Whisstock, Justin P. Ludeman
Publikováno v:
Biophysical Journal. 80:491-497
The x-ray crystal structure of the serpin-proteinase complex is yet to be determined. In this study we have investigated the conformational changes that take place within antitrypsin during complex formation with catalytically inactive (thrombin S195
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72d5e748adc77e5969eb2468196a81f5
https://doi.org/10.1016/s0006-3495(01)76031-6
https://doi.org/10.1016/s0006-3495(01)76031-6
Publikováno v:
Journal of Molecular Evolution. 51:507-515
Protease cascades and their inhibitors are a common feature of many biological regulatory systems, and the various components of such cascades have been subjected to a long and concerted evolution. We present here evidence that in the coagulation cas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14f4e81d6095bda333c745cc1719ed4e
https://doi.org/10.1007/s002390010114
https://doi.org/10.1007/s002390010114
Publikováno v:
Biochemical and Biophysical Research Communications. 251:1-5
A number of disease states are attributable to α 1 -antitrypsin polymerisation within the endoplasmic reticulum of hepatocytes and subsequent plasma deficiency. Two distinct mechanisms describing the process of α 1 -antitrypsin polymerisation have
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a51337f00370c0c6b914fb39f95e373
https://doi.org/10.1006/bbrc.1998.9254
https://doi.org/10.1006/bbrc.1998.9254
Autor:
James C. Whisstock, Mark R. Wardell, Robin W. Carrell, Paul C.R. Hopkins, Wun Shaing W. Chang, Arthur M. Lesk
Publikováno v:
Protein Science. 6:89-98
Serpin polymerization is the underlying cause of several diseases, including thromboembolism, emphysema, liver cirrhosis, and angioedema. Understanding the structure of the polymers and the mechanism of polymerization is necessary to support rational
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e5b83c135211236f86d6decbcef3db34
https://doi.org/10.1002/pro.5560060110
https://doi.org/10.1002/pro.5560060110
Autor:
Stuart R. Stone, Paul C.R. Hopkins
Publikováno v:
Biochemistry. 34:15872-15879
The hinge region of serpins is a conserved sequence of 8 amino acids located 7 residues away from the scissile bond at P8 to P15, on the edge of the protease-binding domain. In the inhibitory serpins the P8 to P12 residues of this motif are usually s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f40fc3594d1119593d9530608530d0e
https://doi.org/10.1021/bi00048a033
https://doi.org/10.1021/bi00048a033
Publikováno v:
Journal of Biological Chemistry. 270:11866-11871
Recombinant alpha 1-antitrypsin with a P1 arginine residue (Arg-alpha 1-antitrypsin) is a rapid inhibitor of both thrombin and activated protein C (APC). A series of mutants were made in an attempt to increase the specificity of this serpin for throm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35da9ffd0ef8e35b46db630fdeb76fd0
https://doi.org/10.1074/jbc.270.20.11866
https://doi.org/10.1074/jbc.270.20.11866
Publikováno v:
Biochemical Journal. 298:507-510
The importance of interactions with residues 15-21 in the core domain of hirudin for the formation of the complex with thrombin has been investigated by site-directed mutagenesis. Contacts made by Leu-15 were found to be particularly important; repla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b7c38d895a56c5be0a10892fc54204c
https://doi.org/10.1042/bj2980507
https://doi.org/10.1042/bj2980507