Mammalian cells lacking either the cotranslational or posttranslocational oligosaccharyltransferase complex display substrate-dependent defects in asparagine linked glycosylation (Q28941787)

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English	Mammalian cells lacking either the cotranslational or posttranslocational oligosaccharyltransferase complex display substrate-dependent defects in asparagine linked glycosylation	scientific journal article

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scholarly article

1 reference

14 March 2017

Mammalian cells lacking either the cotranslational or posttranslocational oligosaccharyltransferase complex display substrate-dependent defects in asparagine linked glycosylation (English)

1 reference

14 March 2017

Tumor suppressor candidate 3

1 reference

GOA release 2020-03-11

protein N-linked glycosylation via asparagine

1 reference

GOA release 2020-03-11

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based on heuristic

inferred from title

author name string

Natalia A. Cherepanova

1

1 reference

14 March 2017

Reid Gilmore

2

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14 March 2017

language of work or name

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publication date

11 February 2016

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14 March 2017

Scientific Reports

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14 March 2017

6

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14 March 2017

20946

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14 March 2017

copyright license

Creative Commons Attribution 4.0 International

1 February 2016

1 reference

April 2022 Public Data File from Crossref

copyright status

0 references

describes a project that uses

object named as

Image Quant TL

1 reference

CZ Software Mentions: A large dataset of software mentions in the biomedical literature

Oxidoreductase activity is necessary for N-glycosylation of cysteine-proximal acceptor sites in glycoproteins

1 reference

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Structural basis of substrate specificity of human oligosaccharyl transferase subunit N33/Tusc3 and its role in regulating protein N-glycosylation

1 reference

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RNA-guided human genome engineering via Cas9

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Multiplex genome engineering using CRISPR/Cas systems

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The oligosaccharyltransferase subunits OST48, DAD1 and KCP2 function as ubiquitous and selective modulators of mammalian N-glycosylation

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Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency

1 reference

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Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits

1 reference

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Photocross-linking of nascent chains to the STT3 subunit of the oligosaccharyltransferase complex

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DAD1, the defender against apoptotic cell death, is a subunit of the mammalian oligosaccharyltransferase

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High-frequency off-target mutagenesis induced by CRISPR-Cas nucleases in human cells

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Cotranslational stabilization of Sec62/63 within the ER Sec61 translocon is controlled by distinct substrate-driven translocation events

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N-linked protein glycosylation in the ER.

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Extreme C-terminal sites are posttranslocationally glycosylated by the STT3B isoform of the OST.

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1 reference

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based on heuristic

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Model studies on N-glycosylation of proteins

1 reference

https://pubmed.ncbi.nlm.nih.gov/26864433

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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10.1038/SREP20946

1 reference

14 March 2017

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release_eao7s2xzjraslabiamu4y7cure

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24 November 2022

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mapped directly with Wikidata item

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1 reference

14 March 2017

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10.1038/srep20946

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