(Q35002612)

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Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1

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Europe PubMed Central

PubMed publication ID

5 August 2017

Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1 (English)

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

1 reference

based on heuristic

inferred from title

Matthew R Pratt

4

object named as

Matthew R Pratt

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Europe PubMed Central

PubMed publication ID

5 August 2017

author name string

Balyn W Zaro

1

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

Yu-Ying Yang

2

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Europe PubMed Central

PubMed publication ID

5 August 2017

Howard C Hang

3

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Europe PubMed Central

PubMed publication ID

5 August 2017

language of work or name

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publication date

3 May 2011

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Europe PubMed Central

PubMed publication ID

5 August 2017

Proceedings of the National Academy of Sciences of the United States of America

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Europe PubMed Central

PubMed publication ID

5 August 2017

108

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Europe PubMed Central

PubMed publication ID

5 August 2017

20

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

8146-8151

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

Metabolic cross-talk allows labeling of O-linked beta-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway

1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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Nedd4 and Nedd4-2: closely related ubiquitin-protein ligases with distinct physiological functions

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

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1 reference

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Chemical approaches to perturb, profile, and perceive glycans

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Large-scale profiling of protein palmitoylation in mammalian cells

1 reference

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8 July 2018

New insights into metabolic signaling and cell survival: the role of beta-O-linkage of N-acetylglucosamine.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

8 July 2018

Direct in-gel fluorescence detection and cellular imaging of O-GlcNAc-modified proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

8 July 2018

Identification of new O-GlcNAc modified proteins using a click-chemistry-based tagging

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

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Activity-based protein profiling: from enzyme chemistry to proteomic chemistry

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

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Chemical approaches to understanding O-GlcNAc glycosylation in the brain

1 reference

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O-GlcNAc modification in diabetes and Alzheimer's disease

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

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Probing the dynamics of O-GlcNAc glycosylation in the brain using quantitative proteomics

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

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Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

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Caenorhabditis elegans ortholog of a diabetes susceptibility locus: oga-1 (O-GlcNAcase) knockout impacts O-GlcNAc cycling, metabolism, and dauer

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

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Chemistry in living systems

1 reference

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The hexosamine signaling pathway: deciphering the "O-GlcNAc code"

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

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Inactivation of phosphorylated endothelial nitric oxide synthase (Ser-1177) by O-GlcNAc in diabetes-associated erectile dysfunction

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1 reference

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1 reference

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O-GlcNAcylation regulates phosphorylation of tau: a mechanism involved in Alzheimer's disease

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

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Profiling enzyme activities in vivo using click chemistry methods

1 reference

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1 reference

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Ogt-dependent X-chromosome-linked protein glycosylation is a requisite modification in somatic cell function and embryo viability

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

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A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

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The coactivator of transcription CREB-binding protein interacts preferentially with the glycosylated form of Stat5.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

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A chemical approach for identifying O-GlcNAc-modified proteins in cells

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

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The many forks in FOXO's road

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

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GlcNAc 2-epimerase can serve a catabolic role in sialic acid metabolism

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

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Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

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The emerging significance of O-GlcNAc in cellular regulation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

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The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny

1 reference

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Sulfotransferases of two specificities function in the reconstitution of high endothelial cell ligands for L-selectin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

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Nedd4-like proteins: an emerging family of ubiquitin-protein ligases implicated in diverse cellular functions

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

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1 reference

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Analysis of nuclear pore protein p62 glycosylation

1 reference

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Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

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1 reference

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1 reference

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2 references

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26 October 2018

https://pubmed.ncbi.nlm.nih.gov/21540332

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Global identification of O-GlcNAc-modified proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

26 October 2018

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1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

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Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress. A survival response of mammalian cells

1 reference

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A chemoenzymatic approach toward the rapid and sensitive detection of O-GlcNAc posttranslational modifications

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

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YY1 is regulated by O-linked N-acetylglucosaminylation (O-glcNAcylation).

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

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Cytosolic O-glycosylation is abundant in nerve terminals

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

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Negative regulation of the forkhead transcription factor FKHR by Akt.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100932

26 October 2018

Identifiers

10.1073/PNAS.1102458108

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

2011PNAS..108.8146Z

0 references

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

ResearchGate publication ID

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