Zobrazeno 1 - 10
of 99
pro vyhledávání: '"Douglas H. Ohlendorf"'
Autor:
Brittany E. Juhlmann, Anne J. Smith, Jill Suttles, Douglas H. Ohlendorf, Andrew C. Kruse, Mark A. Sanders, David A. Bernlohr, Ann V. Hertzel, Kristina Hellberg, Joseph M. Reynolds
Publikováno v:
Journal of Medicinal Chemistry. 52:6024-6031
Molecular disruption of the lipid carrier AFABP/aP2 in mice results in improved insulin sensitivity and protection from atherosclerosis. Because small molecule inhibitors may be efficacious in defining the mechanism(s) of AFABP/aP2 action, a chemical
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b63bdd3d1915c075d928072e0478be4b
https://doi.org/10.1021/jm900720m
https://doi.org/10.1021/jm900720m
Autor:
Irina V. Getun, Clare Woodward, C. Kent Brown, Douglas H. Ohlendorf, Judit Tulla-Puche, George Barany
Publikováno v:
Journal of Molecular Biology. 375:812-823
Crystal structures, at 1.7 A resolution, were solved for complexes between each of two chemically synthesized partially folded analogues of bovine pancreatic trypsin inhibitor (BPTI) with the proteolytically inactive rat trypsin mutant S195A. The BPT
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92f8347192598fc1fc78d7fbc5bf5a94
https://doi.org/10.1016/j.jmb.2007.10.084
https://doi.org/10.1016/j.jmb.2007.10.084
Autor:
Ke Shi, Keun Seok Seo, Cathleen A. Earhart, Jeff Digre, Fikre Mengistu, C. Kent Brown, Douglas H. Ohlendorf, Patrick M. Schlievert, M. Huseby, Gregory A. Bohach
Publikováno v:
Journal of Bacteriology. 189:8719-8726
Beta toxin is a neutral sphingomyelinase secreted by certain strains of Staphylococcus aureus . This virulence factor lyses erythrocytes in order to evade the host immune system as well as scavenge nutrients. The structure of beta toxin was determine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08899cf139a084a27345b18bb5028ffb
https://doi.org/10.1128/jb.00741-07
https://doi.org/10.1128/jb.00741-07
Autor:
Briana K. Kozlowicz, Ke Shi, Douglas H. Ohlendorf, Cathleen A. Earhart, Zu Yi Gu, Gary M. Dunny
Publikováno v:
Molecular Microbiology. 62:958-969
In many bacteria expression of lateral gene transfer and of virulence factors is controlled by cell–cell signalling systems. Molecular interactions of microbial signal molecules with their cognate receptors are not well understood. For the Enteroco
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18e65c861b2ead2edafc6e2b8d0a6d8f
https://doi.org/10.1111/j.1365-2958.2006.05434.x
https://doi.org/10.1111/j.1365-2958.2006.05434.x
Autor:
Stephen B. Olmsted, Douglas H. Ohlendorf, Cathleeen A. Earhart, Zu Yi Gu, Yury V. Matsuka, P. Patrick Cleary, C. Kent Brown
Publikováno v:
International Congress Series. 1289:211-215
The structure of a 949-residue fragment of complement factor 5a peptidase (SCP) was determined to 1.9 A resolution. The molecule is made of five distinct domains in an elongated head–stalk structure. The structure suggests that activity of SCP can
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::88fd7dde407ff12d6bc7b2314119bd5c
https://doi.org/10.1016/j.ics.2005.11.004
https://doi.org/10.1016/j.ics.2005.11.004
Autor:
Yury V. Matsuka, P. Patrick Cleary, Zu Yi Gu, Douglas H. Ohlendorf, Laurie Anne Winter, C. Kent Brown, Stephen B. Olmsted, Cathleen A. Earhart, Sai Sudha Purushothaman
Publikováno v:
Proceedings of the National Academy of Sciences. 102:18391-18396
The structure of a cell surface enzyme from a Gram-positive pathogen has been determined to 2-Å resolution. Gram-positive pathogens have a thick cell wall to which proteins and carbohydrate are covalently attached. Streptococcal C5a peptidase (SCP),
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac671aa1a1db03218da321300e3b4188
https://doi.org/10.1073/pnas.0504954102
https://doi.org/10.1073/pnas.0504954102
Publikováno v:
Annual Review of Microbiology. 58:555-585
▪ Abstract The catechol dioxygenases allow a wide variety of bacteria to use aromatic compounds as carbon sources by catalyzing the key ring-opening step. These enzymes use specifically either catechol or protocatechuate (2,3-dihydroxybenozate) as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::56d4f6c552c351a8fd2531fcfa2f5bf5
https://doi.org/10.1146/annurev.micro.57.030502.090927
https://doi.org/10.1146/annurev.micro.57.030502.090927
Autor:
John D. Lipscomb, Matthew W. Vetting, Lawrence Que, Lawrence P. Wackett, Douglas H. Ohlendorf
Publikováno v:
Journal of Bacteriology. 186:1945-1958
The X-ray crystal structures of homoprotocatechuate 2,3-dioxygenases isolated fromArthrobacter globiformisandBrevibacterium fuscumhave been determined to high resolution. These enzymes exhibit 83% sequence identity, yet their activities depend on dif
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48f87cd079387b36c4a6e75c4d1c7bf1
https://doi.org/10.1128/jb.186.7.1945-1958.2004
https://doi.org/10.1128/jb.186.7.1945-1958.2004
Autor:
James M. Musser, Harry R. Hill, Kent D. Barbian, John K. McCormick, Robert L. Cole, Patrick M. Schlievert, L. George Veasy, James C. Smoot, Nancy P. Hoe, Laura M. Smoot, Douglas H. Ohlendorf, Ian Strickland, Cathleen A. Earhart, Donald Y.M. Leung
Publikováno v:
Infection and Immunity. 70:7095-7104
The pathogenesis of acute rheumatic fever (ARF) is poorly understood. We identified two contiguous bacteriophage genes, designatedspeLandspeM, encoding novel inferred superantigens in the genome sequence of an ARF strain of serotype M18 group A strep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2df5d59169c1e946c874b6e11f87682
https://doi.org/10.1128/iai.70.12.7095-7104.2002
https://doi.org/10.1128/iai.70.12.7095-7104.2002
Publikováno v:
Journal of Molecular Evolution. 51:520-531
Pathogenic bacteria have evolved a wide variety of toxins to invade and attack host organisms. In particular, strains of the bacteria Staphylococcus aureus and Streptococcus pyogenes produce a family of pyrogenic toxin superantigens (PTSAgs) that can
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f9665c3d431b9d02463d4759768fa83
https://doi.org/10.1007/s002390010116
https://doi.org/10.1007/s002390010116