Structural and mutational studies on the importance of oligosaccharide binding for the activity of yeast PNGase - Test2 - elhamkhani - TriplyDB

Structural and mutational studies on the importance of oligosaccharide binding for the activity of yeast PNGase

Structural and mutational studies on the importance of oligosaccharide binding for the activity of yeast PNGase

http://www.wikidata.org/entity/Q27652504

about

Structure of the catalytic domain of theSalmonellavirulence factor SseI N-terminal deletion of peptide:N-glycanase results in enhanced deglycosylation activity.Evidence for an essential deglycosylation-independent activity of PNGase in Drosophila melanogaster The cytoplasmic peptide:N-glycanase (NGLY1) - Structure, expression and cellular functions Characterization of the temperature-sensitive mutations un-7 and png-1 in Neurospora crassa.The cytoplasmic peptide:N-glycanase (Ngly1)-basic science encounters a human genetic disorder.Wild type RTA and less toxic variants have distinct requirements for Png1 for their depurination activity and toxicity in Saccharomyces cerevisiae Releasing N-glycan from peptide N-terminus by N-terminal succinylation assisted enzymatic deglycosylation The Neurospora peptide:N-glycanase ortholog PNG1 is essential for cell polarity despite its lack of enzymatic activity.High-Throughput Assays to Assess the Functional Impact of Genetic Variants: A Road Towards Genomic-Driven Medicine.Inhibition of NGLY1 Inactivates the Transcription Factor Nrf1 and Potentiates Proteasome Inhibitor Cytotoxicity.

P2860

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P2860

Structural and mutational studies on the importance of oligosaccharide binding for the activity of yeast PNGase

http://www.wikidata.org/entity/Q27652504

description

2009 nî lūn-bûn

@nan

2009 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի փետրվարին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

Structural and mutational stud ...... r the activity of yeast PNGase

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Structural and mutational stud ...... r the activity of yeast PNGase

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Structural and mutational stud ...... r the activity of yeast PNGase

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type

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Structural and mutational stud ...... r the activity of yeast PNGase

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Structural and mutational stud ...... r the activity of yeast PNGase

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Structural and mutational stud ...... r the activity of yeast PNGase

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Structural and mutational stud ...... r the activity of yeast PNGase

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Structural and mutational stud ...... r the activity of yeast PNGase

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Structural and mutational stud ...... r the activity of yeast PNGase

@en

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Gang Zhao

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Guangtao Li

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Ichiro Matsuo

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Tadashi Suzuki

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William J Lennarz

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Xiaoke Zhou

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

Yukishige Ito

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

P2860

Identification of proteins that interact with mammalian peptide:N-glycanase and implicate this hydrolase in the proteasome-dependent pathway for protein degradation

PNG1, a yeast gene encoding a highly conserved peptide:N-glycanase

Improved methods for building protein models in electron density maps and the location of errors in these models

The three-dimensional structure of PNGase F, a glycosylasparaginase from Flavobacterium meningosepticum

MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes

Refinement of macromolecular structures by the maximum-likelihood method

The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol.

AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation.

The AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-associated E3 ligase autocrine motility factor receptor

Characterisation of peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase A and its N-glycans.

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118-25

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scholarly article

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10.1093/GLYCOB/CWN108

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2

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19

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Hermann Schindelin

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2009-02-01T00:00:00Z

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23316876

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18854368

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oligosaccharide

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