Results 11 to 20 of about 349,791 (266)

SCOPEC: a database of protein catalytic domains [PDF]

open access: yesBioinformatics, 2004
Abstract Motivation: Domains are the units of protein structure, function and evolution. It is therefore essential to utilize knowledge of domains when studying the evolution of function, or when assigning function to genome sequence data.
Richard A. George   +4 more
openaire   +2 more sources

Architecture and function of metallopeptidase catalytic domains [PDF]

open access: yesProtein Science, 2013
AbstractThe cleavage of peptide bonds by metallopeptidases (MPs) is essential for life. These ubiquitous enzymes participate in all major physiological processes, and so their deregulation leads to diseases ranging from cancer and metastasis, inflammation, and microbial infection to neurological insults and cardiovascular disorders.
Nýria Cerdý-Costa   +1 more
openaire   +3 more sources

Minimal catalytic domain of N-acetylglucosaminyltransferase V [PDF]

open access: yesGlycobiology, 2000
UDP-GlcNAc: Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T ...
Korczak B.   +4 more
openaire   +3 more sources

Expression, Purification and evaluation of the Immunogenicity of RecombinantC-terminus of the Receptor-Binding Domain of Neurotoxin Botulinum Protein Type B (BoNT/B-HcC) [PDF]

open access: yesمجله علمی دانشگاه علوم پزشکی کردستان, 2023
Background and Aim: Botulism, a syndrome caused by food poisoning, results from use of food contaminated with the botulinum toxin, which is very dangerous and deadly.
Hossein Samiei Abianeh   +5 more
doaj  

The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains [PDF]

open access: yesBMC Genomics, 2007
AbstractBackgroundThe genomes of the three parasitic protozoaTrypanosoma cruzi,Trypanosoma bruceiandLeishmania majorare the main subject of this study. These parasites are responsible for devastating human diseases known as Chagas disease, African sleeping sickness and cutaneous Leishmaniasis, respectively, that affect millions of people in the ...
Brenchley, Rachel   +7 more
openaire   +4 more sources

Structural-Functional Analysis Reveals a Specific Domain Organization in Family GH20 Hexosaminidases. [PDF]

open access: yesPLoS ONE, 2015
Hexosaminidases are involved in important biological processes catalyzing the hydrolysis of N-acetyl-hexosaminyl residues in glycosaminoglycans and glycoconjugates.
Cristina Val-Cid   +3 more
doaj   +1 more source

Structural Insight of a Trimodular Halophilic Cellulase with a Family 46 Carbohydrate-Binding Module. [PDF]

open access: yesPLoS ONE, 2015
Cellulases are the key enzymes used in the biofuel industry. A typical cellulase contains a catalytic domain connected to a carbohydrate-binding module (CBM) through a flexible linker.
Huaidong Zhang   +6 more
doaj   +1 more source

Kinetic Analysis of the Catalytic Domain of Human Cdc25B [PDF]

open access: yesJournal of Biological Chemistry, 1996
The Cdc25 cell cycle regulator is a member of the dual-specificity class of protein-tyrosine phosphatases that hydrolyze phosphotyrosine- and phosphothreonine-containing substrates. To study the mechanism of Cdc25B, we have overexpressed and purified the catalytic domain of human Cdc25B (Xu, X., and Burke, S. P. (1996) J. Biol. Chem.
E B, Gottlin   +6 more
openaire   +2 more sources

Structural and functional characterization of mature forms of metalloprotease E495 from Arctic sea-ice bacterium Pseudoalteromonas sp. SM495. [PDF]

open access: yesPLoS ONE, 2012
E495 is the most abundant protease secreted by the Arctic sea-ice bacterium Pseudoalteromonas sp. SM495. As a thermolysin family metalloprotease, E495 was found to have multiple active forms in the culture of strain SM495.
Hai-Lun He   +8 more
doaj   +1 more source

Modulation of catalytic activity in multi-domain protein tyrosine phosphatases. [PDF]

open access: yesPLoS ONE, 2011
Signaling mechanisms involving protein tyrosine phosphatases govern several cellular and developmental processes. These enzymes are regulated by several mechanisms which include variation in the catalytic turnover rate based on redox stimuli, subcellular
Lalima L Madan   +5 more
doaj   +1 more source

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