Zobrazeno 1 - 10
of 89
pro vyhledávání: '"James D. Lear"'
Autor:
Amanda E Siglin, Shangjin Sun, Jeffrey K Moore, Sarah Tan, Martin Poenie, James D Lear, Tatyana Polenova, John A Cooper, John C Williams
Publikováno v:
PLoS ONE, Vol 8, Iss 4, p e59453 (2013)
Cytoplasmic dynein and dynactin participate in retrograde transport of organelles, checkpoint signaling and cell division. The principal subunits that mediate this interaction are the dynein intermediate chain (IC) and the dynactin p150(Glued); howev
Externí odkaz:
https://doaj.org/article/68e8f2115ad140cfaefc02fb6de3eb24
Publikováno v:
Journal of periodontology. 67
Actinobacillus actinomycetemcomitans has been implicated as a causative organism in early-onset periodontitis. The mechanisms by which A. actinomycetemcomitans is pathogenic are not known, but the organism produces several potential virulence factors
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb0925718c88c99942df94f5811a6323
https://pubmed.ncbi.nlm.nih.gov/29539844
https://pubmed.ncbi.nlm.nih.gov/29539844
Autor:
Patricia A. Keenan, James D. Lear, J. Kent Blasie, Jeffery G. Saven, William F. DeGrado, Hongling Zou, Vikas Nanda, H. Christopher Fry, Frank V. Cochran, Michael J. Therien, Karen A. McAllister, Alessandro Senes, Gretchen M. Bender
Publikováno v:
Journal of the American Chemical Society. 130:11921-11927
We have developed a computational design strategy based on the α-helical coiled-coil to generate modular peptide motifs capable of assembling into metalloporphyrin arrays of varying lengths. The current study highlights the extension of a two-metall
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3973259c44233ff21491cca8ed19cff1
https://doi.org/10.1021/ja800697g
https://doi.org/10.1021/ja800697g
Autor:
Thomas Walz, Calvin K. Yip, James D. Lear, Paul C. Billings, Wenman Wu, Sergei Shikov, Dipali Sinha, Peter N. Walsh
Publikováno v:
Journal of Biological Chemistry. 283:18655-18664
Coagulation factor XI (FXI) is a covalent homodimer consisting of two identical subunits of 80 kDa linked by a disulfide bond formed by Cys-321 within the Apple 4 domain of each subunit. Because FXI(C321S) is a noncovalent dimer, residues within the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::823ce61692666dfd2317b2c589967aa5
https://doi.org/10.1074/jbc.m802275200
https://doi.org/10.1074/jbc.m802275200
Autor:
Chunlong Ma, Amanda L. Stouffer, Lawrence H. Pinto, Lidia Cristian, James D. Lear, Yuki Ohigashi, Robert A. Lamb, William F. DeGrado
Publikováno v:
Structure. 16:1067-1076
Summary We explore the interplay between amino acid sequence, thermodynamic stability, and functional fitness in the M2 proton channel of influenza A virus. Electrophysiological measurements show that drug-resistant mutations have minimal effects on
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3023a69100e6c4ae4c6f42cefd0134bb
https://doi.org/10.1016/j.str.2008.04.011
https://doi.org/10.1016/j.str.2008.04.011
Autor:
William F. DeGrado, Hang Yin, Rustem I. Litvinov, Gaston Vilaire, James D. Lear, Robin Walters, Joel S. Bennett, Joanna S.G. Slusky, Bryan W. Berger, Gregory A. Caputo
Publikováno v:
Science. 315:1817-1822
A variety of methods exist for the design or selection of antibodies and other proteins that recognize the water-soluble regions of proteins; however, companion methods for targeting transmembrane (TM) regions are not available. Here, we describe a m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b5547faa6ec1b98ebc5c1a49a8e19cc4
https://doi.org/10.1126/science.1136782
https://doi.org/10.1126/science.1136782
Autor:
Michael E. Hodsdon, James D. Lear, Danielle A. Guarracino, Alanna Schepartz, Tereece N. Banks, HyoJin R. Chiang
Publikováno v:
Organic Letters. 8:807-810
We report a systematic analysis of the relationship between salt bridge composition and 14-helix structure within a family of model beta-peptides in aqueous buffer. We find an inverse relationship between side-chain length and the extent of 14-helix
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c113194f536cc343eae36349e4370a72
https://doi.org/10.1021/ol0527532
https://doi.org/10.1021/ol0527532
Autor:
Christopher C. Moser, P. Leslie Dutton, Shixin Ye, J. Kent Blasie, Dror Noy, Bohdana M. Discher, James D. Lear, Joseph Strzalka
Publikováno v:
Biochemistry. 44:12329-12343
We have designed polypeptides combining selected lipophilic (LP) and hydrophilic (HP) sequences that assemble into amphiphilic (AP) alpha-helical bundles to reproduce key structure characteristics and functional elements of natural membrane proteins.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d2824f63568d7faafecbddba3219cd2
https://doi.org/10.1021/bi050695m
https://doi.org/10.1021/bi050695m
Publikováno v:
Biochemistry. 44:10416-10422
Factor XI, unlike other coagulation proteins, is a homodimer of two identical subunits linked by a single disulfide bond formed by Cys321. The present study was undertaken to understand the physiological significance of the dimeric nature of factor X
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b4a99b8ef9315ae3c94394ea98ed6c8f
https://doi.org/10.1021/bi050361x
https://doi.org/10.1021/bi050361x
Publikováno v:
Journal of Molecular Biology. 347:169-179
The driving forces behind the folding processes of integral membrane proteins after insertion into the bilayer, is currently under debate. The M2 protein from the influenza A virus is an ideal system to study lateral association of transmembrane heli
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f969b78a248de5fc424e78f4cc03f10
https://doi.org/10.1016/j.jmb.2005.01.023
https://doi.org/10.1016/j.jmb.2005.01.023