Free Glycine Accelerates the Autoproteolytic Activation of Human Asparaginase - Wikidata - wikimedia - TriplyDB

Free Glycine Accelerates the Autoproteolytic Activation of Human Asparaginase

Free Glycine Accelerates the Autoproteolytic Activation of Human Asparaginase

http://www.wikidata.org/entity/Q27677456

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Structural and Kinetic Characterization of Guinea Pig l -Asparaginase Type III Elucidation of the Specific Function of the Conserved Threonine Triad Responsible for Human l-Asparaginase Autocleavage and Substrate Hydrolysis Exploring the role of conformational heterogeneity in cis-autoproteolytic activation of ThnT.Na⁺/K⁺ exchange switches the catalytic apparatus of potassium-dependent plant L-asparaginase Identification of Small Molecule Compounds for Pharmacological Chaperone Therapy of Aspartylglucosaminuria Human 60-kDa lysophospholipase contains an N-terminal L-asparaginase domain that is allosterically regulated by L-asparagine.Intramolecular Cleavage of the hASRGL1 Homodimer Occurs in Two Stages A novel L-asparaginase from Aquabacterium sp. A7-Y with self-cleavage activation.Characterization of Three L-Asparaginases from Maritime Pine (Pinus pinaster Ait.).

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P2860

Free Glycine Accelerates the Autoproteolytic Activation of Human Asparaginase

http://www.wikidata.org/entity/Q27677456

description

2013 nî lūn-bûn

@nan

2013 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

name

Free Glycine Accelerates the Autoproteolytic Activation of Human Asparaginase

@ast

Free Glycine Accelerates the Autoproteolytic Activation of Human Asparaginase

@en

Free Glycine Accelerates the Autoproteolytic Activation of Human Asparaginase

@nl

type

label

Free Glycine Accelerates the Autoproteolytic Activation of Human Asparaginase

@ast

Free Glycine Accelerates the Autoproteolytic Activation of Human Asparaginase

@en

Free Glycine Accelerates the Autoproteolytic Activation of Human Asparaginase

@nl

prefLabel

Free Glycine Accelerates the Autoproteolytic Activation of Human Asparaginase

@ast

Free Glycine Accelerates the Autoproteolytic Activation of Human Asparaginase

@en

Free Glycine Accelerates the Autoproteolytic Activation of Human Asparaginase

@nl

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J.CHEMBIOL.2013.03.006

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Chemistry and Biology

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Free Glycine Accelerates the Autoproteolytic Activation of Human Asparaginase

@en

P2093

Christos S Karamitros

http://www.w3.org/2001/XMLSchema#string

Julian Nomme

http://www.w3.org/2001/XMLSchema#string

Manfred Konrad

http://www.w3.org/2001/XMLSchema#string

Theresa McSorley

http://www.w3.org/2001/XMLSchema#string

Ying Su

http://www.w3.org/2001/XMLSchema#string

P2860

Taspase1: a threonine aspartase required for cleavage of MLL and proper HOX gene expression

The human asparaginase-like protein 1 hASRGL1 is an Ntn hydrolase with beta-aspartyl peptidase activity

Understanding the Warburg effect: the metabolic requirements of cell proliferation

Structural insights into the mechanism of intramolecular proteolysis

A dual role for an aspartic acid in glycosylasparaginase autoproteolysis

The mechanism of autocatalytic activation of plant-type L-asparaginases

Structures of Apo and Product-Bound Human l -Asparaginase: Insights into the Mechanism of Autoproteolysis and Substrate Hydrolysis

Small Molecule Activation of PKM2 in Cancer Cells Induces Serine Auxotrophy

Serine is a natural ligand and allosteric activator of pyruvate kinase M2

Three-dimensional structure of human lysosomal aspartylglucosaminidase

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533-40

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10.1016/J.CHEMBIOL.2013.03.006

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4

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20

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236250351

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23601642

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clinical chemistry

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3633088

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