Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Mark R. Parsons"'
Autor:
Shalini Iyer, Penelope J. La-Borde, Karl A.P. Payne, Mark R. Parsons, Anthony J. Turner, R. Elwyn Isaac, K. Ravi Acharya
Publikováno v:
FEBS Open Bio, Vol 5, Iss 1, Pp 292-302 (2015)
Eukaryotic aminopeptidase P1 (APP1), also known as X‐prolyl aminopeptidase (XPNPEP1) in human tissues, is a cytosolic exopeptidase that preferentially removes amino acids from the N‐terminus of peptides possessing a penultimate N‐terminal proli
Externí odkaz:
https://doaj.org/article/a81b952de5dc4dc08fa330f7521a86c9
Publikováno v:
The American Journal of Medicine. 131:e39-e42
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85731c01e8a084c307e226781ab8f537
https://doi.org/10.1016/j.amjmed.2017.08.032
https://doi.org/10.1016/j.amjmed.2017.08.032
Autor:
Peter F. Knowles, Thembaninkosi G. Gaule, Simon E. V. Phillips, Mark R. Parsons, Christian R. Kurtis, Michael J. McPherson
Publikováno v:
Journal of Neural Transmission. 118:1043-1053
Copper amine oxidases are important for the metabolism of a range of biogenic amines. Here, we focus on substrate specificity in the E. coli copper amine oxidase (ECAO) and specifically the role of Tyr 381. This residue, and its equivalent, in other
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f702ef00d011c39ed433b2b102070c8
https://doi.org/10.1007/s00702-011-0620-y
https://doi.org/10.1007/s00702-011-0620-y
Autor:
Ulrich F. Hartl, Luis Moroder, Manajit Hayer-Hartl, Frank Weber, Mark R. Parsons, Alison E. Ashcroft, Joachim Jäger, Markus Kaiser, Joseph E. Coyle, Achim Brinker, Sheena E. Radford
Publikováno v:
Journal of Biological Chemistry. 277:33115-33126
Advances in understanding how GroEL binds to non-native proteins are reported. Conformational flexibility in the GroEL apical domain, which could account for the variety of substrates that GroEL binds, is illustrated by comparison of several independ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7d92b0c1c93573370a062d2e3de59538
https://doi.org/10.1074/jbc.m203398200
https://doi.org/10.1074/jbc.m203398200
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 58:421-430
In the Gram-positive bacterium Bacillus subtilis the concentration of the amino acid L-arginine is controlled by the transcriptional regulator AhrC. The hexameric AhrC protein binds in an L-arginine-dependent manner to pseudo-palindromic operators wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a0743cfbc52052251708ef9ffb90797
https://doi.org/10.1107/s0907444901021692
https://doi.org/10.1107/s0907444901021692
Publikováno v:
Journal of Molecular Biology. 285:1245-1256
The crystal structure of intact elongation factor Tu (EF-Tu) from Escherichia coli in GDP-bound conformation has been determined using a combination of multiple isomorphous replacement (MIR) and multiwavelength anomalous diffraction (MAD) methods. Th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0950661a0fdfe39024fb4846d54ce1c9
https://doi.org/10.1006/jmbi.1998.2387
https://doi.org/10.1006/jmbi.1998.2387
Publikováno v:
Nature. 376:362-366
The single-stranded DNA (ssDNA) binding protein gp32 from bacteriophage T4 is essential for T4 DNA replication, recombination and repair. In vivo gp32 binds ssDNA as the replication fork advances and stimulates replisome processivity and accuracy by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f999d2ef7d7c650f5570e838caddccfd
https://doi.org/10.1038/376362a0
https://doi.org/10.1038/376362a0
Autor:
Paul Acklam, Deborah Cowen, Glenn A. McConkey, A. Peter Johnson, Paul T. P. Bedingfield, Colin W. G. Fishwick, Fraser Cunningham, Mark R. Parsons
Publikováno v:
Journal of medicinal chemistry. 55(12)
The de novo pyrimidine biosynthesis enzyme dihydroorotate dehydrogenase is an emerging drug target for the treatment of malaria. In this context a key property of Plasmodium falciparum DHODH (PfDHODH) is that it can be selectively inhibited over its
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1831f37a59d3501f8ebad8e6d84c61a2
https://pubmed.ncbi.nlm.nih.gov/22621375
https://pubmed.ncbi.nlm.nih.gov/22621375
Publikováno v:
Handbook of Metalloproteins
Keywords: 2; 4; 5-trihydroxyphenylalanine quinone (TPQ); arthrobacter; E. coli; hansenula; dioxygen binding; electron and proton transfer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a2121b9492e30b16af6eaf0aa43e4fd
https://doi.org/10.1002/9781119951438.eibc0618
https://doi.org/10.1002/9781119951438.eibc0618
