Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Helen R, Josephine"'
Autor:
Donghong Min, Helen R Josephine, Hongzhi Li, Clemens Lakner, Iain S MacPherson, Gavin J P Naylor, David Swofford, Lizbeth Hedstrom, Wei Yang
Publikováno v:
PLoS Biology, Vol 6, Iss 8, p e206 (2008)
Inosine monophosphate dehydrogenase (IMPDH) catalyzes an essential step in the biosynthesis of guanine nucleotides. This reaction involves two different chemical transformations, an NAD-linked redox reaction and a hydrolase reaction, that utilize mut
Externí odkaz:
https://doaj.org/article/ddb9bd56b4474bdcb042295fdd6460ad
Publikováno v:
Biochemistry. 49:10674-10681
X-ray crystal structures of enzyme-ligand complexes are widely believed to mimic states in the catalytic cycle, but this presumption has seldom been carefully scrutinized. In the case of Tritrichomonas foetus inosine 5'-monophosphate dehydrogenase (I
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74b889a59500231d33b5a41e6823893e
https://doi.org/10.1021/bi101590c
https://doi.org/10.1021/bi101590c
Publikováno v:
Biochemistry
IMP dehydrogenase (IMPDH) catalyzes two very different chemical transformations, a dehydrogenase reaction and a hydrolysis reaction. The enzyme toggles between the open conformation required for the dehydrogenase reaction and the closed conformation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be009b855c6dc7a71f96cba257aa9023
https://doi.org/10.1021/bi800674a
https://doi.org/10.1021/bi800674a
Autor:
Frank J, Bruzzese, Michael A, Milhollen, James M, Gavin, Helen R, Josephine, James E, Brownell
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 832
The NEDD8 conjugation pathway is initiated by the NEDD8 E1, also known as NEDD8 activating enzyme (NAE) or APPBP1/UBA3 (Gong, Yeh. J Biol Chem 274:12063-12042, 1999). The best described biological role for NEDD8 conjugation is to regulate the activit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::17c7905a642c15531b125a11417e0469
https://pubmed.ncbi.nlm.nih.gov/22350913
https://pubmed.ncbi.nlm.nih.gov/22350913
Publikováno v:
Methods in Molecular Biology ISBN: 9781617794735
The NEDD8 conjugation pathway is initiated by the NEDD8 E1, also known as NEDD8 activating enzyme (NAE) or APPBP1/UBA3 (Gong, Yeh. J Biol Chem 274:12063-12042, 1999). The best described biological role for NEDD8 conjugation is to regulate the activit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::74968cc19dc75958ed74cfc5ba6e5f19
https://doi.org/10.1007/978-1-61779-474-2_40
https://doi.org/10.1007/978-1-61779-474-2_40
Autor:
Clemens Lakner, David L. Swofford, Wei Yang, Hongzhi Li, Iain S. MacPherson, Helen R. Josephine, Lizbeth Hedstrom, Donghong Min, Gavin J. P. Naylor
Publikováno v:
PLoS Biology
PLoS Biology, Vol 6, Iss 8, p e206 (2008)
PLoS Biology, Vol 6, Iss 8, p e206 (2008)
Inosine monophosphate dehydrogenase (IMPDH) catalyzes an essential step in the biosynthesis of guanine nucleotides. This reaction involves two different chemical transformations, an NAD-linked redox reaction and a hydrolase reaction, that utilize mut
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3f938fed9ca8867585e591e7417895c
http://europepmc.org/articles/PMC2525691
http://europepmc.org/articles/PMC2525691
Autor:
Helen R. Josephine, Eric Sauvage, Christopher Davies, Paulette Charlier, Jason Heilemann, R. F. Pratt, Ailsa J. Powell
Publikováno v:
Journal of molecular biology. 381(2)
The X-ray crystal structures of covalent complexes of the Actinomadura R39 DD-peptidase and Escherichia coli penicillin-binding protein 5 with β-lactams bearing peptidoglycan-mimetic side chains have been determined. The structure of the hydrolysis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e606dd6fae5fbab1ca57940b3b7668a8
https://pubmed.ncbi.nlm.nih.gov/18602645
https://pubmed.ncbi.nlm.nih.gov/18602645
The membrane-bound bacterial D-alanyl- D-alanine peptidases or penicillin-binding proteins (PBPs) catalyze the final transpeptidation reaction of bacterial cell wall biosynthesis and are the targets of beta-lactam antibiotics. Rather surprisingly, th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d45b0ab0da02bfdb642a5e6df1cdd0c2
https://europepmc.org/articles/PMC2536641/
https://europepmc.org/articles/PMC2536641/
Autor:
Christopher J. Davies, R. F. Pratt, Robert A. Nicholas, Helen R. Josephine, Paulette Charlier
Publikováno v:
Biochemistry. 45(51)
Beta-lactams exert their antibiotic action through their inhibition of bacterial DD-peptidases (penicillin-binding proteins). Bacteria, in general, carry several such enzymes localized on the outside of their cell membrane to catalyze the final step
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24ffba6d62319f53a63bfa1d030f5fbf
https://pubmed.ncbi.nlm.nih.gov/17176110
https://pubmed.ncbi.nlm.nih.gov/17176110
Autor:
Helen R. Josephine, Alexandre P. Kuzin, Rajesh Nagarajan, Judith A. Kelly, R. F. Pratt, Nicholas R. Silvaggi
Publikováno v:
Journal of molecular biology. 345(3)
The bacterial D-alanyl-D-alanine transpeptidases (DD-peptidases) are the killing targets of beta-lactams, the most important clinical defense against bacterial infections. However, due to the constant development of antibiotic-resistance mechanisms b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a8d75f12dd541150705287d4a634731
https://pubmed.ncbi.nlm.nih.gov/15581896
https://pubmed.ncbi.nlm.nih.gov/15581896