Results 11 to 20 of about 365,538 (313)

Functional characterization of the catalytic and bromodomain of FgGCN5 in development, DON production and virulence of Fusarium graminearum

open access: yesJournal of Integrative Agriculture, 2020
FgGCN5, a GCN5 homolog in Fusarium graminearum, plays a critical role in hyphal vegetative growth, asexual and sexual reproduction, deoxynivalenol (DON) biosynthesis and plant infection.
Qian-nan WANG   +2 more
doaj   +1 more source

Crystal Structures Reveal Hidden Domain Mechanics in Protein Kinase A (PKA)

open access: yesBiology, 2023
Cyclic-AMP-dependent protein kinase A (PKA) is a critical enzyme involved in various signaling pathways that plays a crucial role in regulating cellular processes including metabolism, gene transcription, cell proliferation, and differentiation.
Colin L. Welsh   +2 more
doaj   +1 more source

Expression, Characterization and Structure Analysis of a New GH26 Endo-β-1, 4-Mannanase (Man26E) from Enterobacter aerogenes B19

open access: yesApplied Sciences, 2020
β-mannanase is one of the key enzymes to hydrolyze hemicellulose. At present, most β-mannanases are not widely applied because of their low enzyme activity and unsuitable enzymatic properties.
Huijing Liu, Jie Liu, Tangbing Cui
doaj   +1 more source

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  

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

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 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

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