Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Sean G. Jackson"'
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67:412-416
Pleckstrin is a major substrate of protein kinase C in platelets and leukocytes and appears to play an important role in exocytosis through a currently unknown mechanism. Pleckstrin function is regulated by phosphorylation, which is thought to cause
Publikováno v:
Journal of Molecular Biology. 395:491-503
Pseudomonas aeruginosa type IV pili, composed of PilA subunits, are used for attachment and twitching motility on surfaces. P. aeruginosa strains express one of five phylogenetically distinct PilA proteins, four of which are associated with accessory
Autor:
R.L. Summerfield, Kun Zhang, Sean G. Jackson, Murray S. Junop, Xiankun Bao, Richard J. Haslam, Yi Zhang
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 62:324-330
Pleckstrin is an important intracellular protein involved in the phosphoinositide-signalling pathways of platelet activation. This protein contains both N- and C-terminal pleckstrin-homology (PH) domains (N-PH and C-PH). The crystal structure of C-PH
Publikováno v:
Biochemistry. 48(49)
MurA (enolpyruvyl UDP-GlcNAc synthase) catalyzes the first committed step in peptidoglycan biosynthesis. In this study, MurA-catalyzed breakdown of its tetrahedral intermediate (THI), with a k{sub cat}/K{sub M} of 520 M{sup -1} s{sup -1}, was far slo
Autor:
Sean G. Jackson, Murray S. Junop, Carsten Shultz, Kun Zhang, Richard P. Haslam, Yi Zhang, Xiankun Bao
Publikováno v:
The FASEB Journal. 21
Autor:
Debasis Mallik, Stanislas Mayer, Denis M. Daigle, Rachael L. Summerfield, Sean G. Jackson, Murray S. Junop, Eric D. Brown, Margaret Sulek, Organ Michael, Donald W. Hughes
Publikováno v:
Journal of medicinal chemistry. 49(24)
Dihydrofolate reductase (DHFR) is a vital metabolic enzyme and thus a clinically prominent target in the design of antimetabolites. In this work, we identify 1,4-bis-{[N-(1-imino-1-guanidino-methyl)]sulfanylmethyl}-3,6-dimethyl-benzene (compound 1) a
Publikováno v:
BMC Structural Biology
BMC Structural Biology, Vol 11, Iss 1, p 11 (2011)
BMC Structural Biology, Vol 11, Iss 1, p 11 (2011)
Background PH domains represent one of the most common domains in the human proteome. These domains are recognized as important mediators of protein-phosphoinositide and protein-protein interactions. Phosphoinositides are lipid components of the memb
Publikováno v:
BMC Structural Biology
BMC Structural Biology, Vol 7, Iss 1, p 80 (2007)
BMC Structural Biology, Vol 7, Iss 1, p 80 (2007)
Background Pleckstrin homology (PH) domains are one of the most prevalent domains in the human proteome and represent the major phosphoinositide-binding module. These domains are often found in signaling proteins and function predominately by targeti