Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Linda, Miallau"'
Autor:
Scarlett Kiyeleko, Sofiane Hocine, Giséle Mautino, Mélaine Kuenemann, Agata Nawrotek, Linda Miallau, Laurent-Michel Vuillard, Olivier Mirguet, Andras Kotschy, Stephen Hanessian
Publikováno v:
Bioorganicmedicinal chemistry letters. 75
We describe the synthesis of a series of 3-t-butyl 5-aminopyrazole p-substituted arylamides as inhibitors of serine-threonine25 (STK25), an enzyme implicated in the progression of non-alcoholic fatty liver disease (NAFLD). Appending a p-N-pyrrolidino
Autor:
William R. Jacobs, Tung Phan, Janet Chiang, Paras Jain, Irina Chernishof, David Eisenberg, Michelle E. Maxson, Linda Miallau, Sum Chan, Christine J. Ahn, Mark A. Arbing, Duilio Cascio
Publikováno v:
Structure. 21:627-637
SummaryThe Mycobacterium tuberculosis (Mtb) genome encodes approximately 90 toxin-antitoxin protein complexes, including three RelBE family members, which are believed to play a major role in bacterial fitness and pathogenicity. We have determined th
Publikováno v:
Acta crystallographica. Section F, Structural biology communications. 72(Pt 12)
The structure of Msmeg_6760, a protein of unknown function, has been determined. Biochemical and bioinformatics analyses determined that Msmeg_6760 interacts with a protein encoded in the same operon, Msmeg_6762, and predicted that the operon is a to
Publikováno v:
Protein Science. 21:1754-1767
VapBC pairs account for 45 out of 88 identified toxin-antitoxin (TA) pairs in the Mycobacterium tuberculosis (Mtb) H37Rv genome. A working model suggests that under times of stress, antitoxin molecules are degraded, releasing the toxins to slow the m
Autor:
Linda Miallau, Gordon A. Leonard, Sean McSweeney, William N. Hunter, Justyna Kalinowska-Tłuścik, Mads Gabrielsen
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66:237-241
4-Diphosphocytidyl-2C-methyl-d-erythritol kinase (IspE; EC 2.7.1.148) contributes to the 1-deoxy-d-xylulose 5-phosphate or mevalonate-independent biosynthetic pathway that produces the isomers isopentenyl diphosphate and dimethylallyl diphosphate. Th
Autor:
Mark A. Arbing, Michael Faller, Duilio Cascio, Feng Guo, Linda Miallau, Janet Chiang, David Eisenberg
Publikováno v:
Journal of Biological Chemistry. 284:276-283
In prokaryotes, cognate toxin-antitoxin pairs have long been known, but no three-dimensional structure has been available for any given complex from Mycobacterium tuberculosis. Here we report the crystal structure and activity of a member of the VapB
Autor:
Andrew B, Min, Linda, Miallau, Michael R, Sawaya, Jeff, Habel, Duilio, Cascio, David, Eisenberg
Publikováno v:
Protein science : a publication of the Protein Society. 21(11)
VapBC pairs account for 45 out of 88 identified toxin-antitoxin (TA) pairs in the Mycobacterium tuberculosis (Mtb) H37Rv genome. A working model suggests that under times of stress, antitoxin molecules are degraded, releasing the toxins to slow the m
Autor:
Nicholas Chim, Edward N. Baker, Celia W. Goulding, Li-Wei Hung, Inna Krieger, Stephanie Swanson, Hongye Li, Thomas C. Terwilliger, Jodie M. Johnston, J. Shaun Lott, Esther M. M. Bulloch, John B. Bruning, Linda Miallau, Robert P. Morse, David Eisenberg, R. Sankaranarayanan, Michael N.G. James, Jeff E. Habel, Haelee Kim, Alexandra Manos-Turvey, Richard J. Payne, Chang-Yub Kim, James C. Sacchettini
Publikováno v:
Tuberculosis (Edinburgh, Scotland). 91(2)
The TB Structural Genomics Consortium is a worldwide organization of collaborators whose mission is the comprehensive structural determination and analyses of Mycobacterium tuberculosis proteins to ultimately aid in tuberculosis diagnosis and treatme
Publikováno v:
The Journal of biological chemistry. 282(27)
High resolution structures of Staphylococcus aureus d-tagatose-6-phosphate kinase (LacC) in two crystal forms are herein reported. The structures define LacC in apoform, in binary complexes with ADP or the co-factor analogue AMP-PNP, and in a ternary
Autor:
Felix Rohdich, William N. Hunter, Wolfgang Eisenreich, Stefan Hecht, Sean McSweeney, Linda Miallau, Gordon A. Leonard, Adelbert Bacher, Magnus S. Alphey, Lauris E. Kemp
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 100(16)
4-Diphosphocytidyl-2 C -methyl- d -erythritol kinase, an essential enzyme in the nonmevalonate pathway of isopentenyl diphosphate and dimethylallyl diphosphate biosynthesis, catalyzes the single ATP-dependent phosphorylation stage affording 4-diphosp