Bioinformatic analysis of α/β-hydrolase fold enzymes reveals subfamily-specific positions responsible for discrimination of amidase and lipase activities.

Bioinformatic analysis of α/β-hydrolase fold enzymes reveals subfamily-specific positions responsible for discrimination of amidase and lipase activities.

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http://www.wikidata.org/entity/Q34435878
BioGPS descriptors for rational engineering of enzyme promiscuity and structure based bioinformatic analysisZebra: a web server for bioinformatic analysis of diverse protein families.BioCatNet: A Database System for the Integration of Enzyme Sequences and Biocatalytic Experiments.Identification of residues of the archaeal RNA-binding Nip7 proteins specific to environmental conditions.Computational design of a pH stable enzyme: understanding molecular mechanism of penicillin acylase's adaptation to alkaline conditionsComputational Identification of Amino-Acid Mutations that Further Improve the Activity of a Chalcone-Flavonone Isomerase from Glycine maxTargeting lipid esterases in mycobacteria grown under different physiological conditions using activity-based profiling with tetrahydrolipstatin (THL).Robust enzyme design: bioinformatic tools for improved protein stability.Parallel workflow manager for non-parallel bioinformatic applications to solve large-scale biological problems on a supercomputer.Study of Functional and Allosteric Sites in Protein SuperfamiliesIn silico screening of 393 mutants facilitates enzyme engineering of amidase activity in CalB.pocketZebra: a web-server for automated selection and classification of subfamily-specific binding sites by bioinformatic analysis of diverse protein families.Mustguseal: a Server for Multiple Structure-Guided Sequence Alignment of Protein Families.Ligand-based Modeling for the Prediction of Pharmacophore Features for Multi-targeted Inhibition of the Arachidonic Acid Cascade.In silico and empirical approaches toward understanding the structural adaptation of the alkaline-stable lipase KV1 from Acinetobacter haemolyticus.Alpha/beta-hydrolases: A unique structural motif coordinates catalytic acid residue in 40 protein fold families.
P2860

Bioinformatic analysis of α/β-hydrolase fold enzymes reveals subfamily-specific positions responsible for discrimination of amidase and lipase activities.

Item
http://www.wikidata.org/entity/Q34435878
description
2012 nî lūn-bûn
@nan
2012 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Bioinformatic analysis of α/β- ...... amidase and lipase activities.
@ast
Bioinformatic analysis of α/β- ...... amidase and lipase activities.
@en
Bioinformatic analysis of α/β- ...... amidase and lipase activities.
@nl
type
label
Bioinformatic analysis of α/β- ...... amidase and lipase activities.
@ast
Bioinformatic analysis of α/β- ...... amidase and lipase activities.
@en
Bioinformatic analysis of α/β- ...... amidase and lipase activities.
@nl
prefLabel
Bioinformatic analysis of α/β- ...... amidase and lipase activities.
@ast
Bioinformatic analysis of α/β- ...... amidase and lipase activities.
@en
Bioinformatic analysis of α/β- ...... amidase and lipase activities.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P433
P478
P577
P5875
P698
P921
P356
P1433
P1476
Bioinformatic analysis of α/β- ...... amidase and lipase activities.
@en
P2093
P2860
P304
P31
P356
P433
P478
P577
P5875
P698
P921