Results 11 to 20 of about 574,974 (306)

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

Crystal Structure of Human Nocturnin Catalytic Domain [PDF]

open access: yesScientific Reports, 2018
Abstract Nocturnin (NOCT) helps the circadian clock to adjust metabolism according to day and night activity. NOCT is upregulated in early evening and it has been proposed that NOCT serves as a deadenylase for metabolic enzyme mRNAs. We present a 2.7-Å crystal structure of the catalytic domain of human NOCT.
Michael A. Estrella   +2 more
openaire   +2 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

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

RpfC (Rv1884) atomic structure shows high structural conservation within the resuscitation promoting factor catalytic domain [PDF]

open access: yes, 2014
We report the first structure of the catalytic domain of RpfC (Rv1884), one of theresuscitation-promoting factors (RPFs) from Mycobacterium tuberculosis.
Bagneris, Claire   +8 more
core   +1 more source

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

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