Regulation of WRN protein cellular localization and enzymatic activities by SIRT1-mediated deacetylation (Q24306868)

Werner syndrome RecQ like helicase

GOA release 2020-03-11

1 reference

negative regulation of helicase activity

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author name string

Kai Li

1

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Alex Casta

2

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Rui Wang

3

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Enerlyn Lozada

4

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Wei Fan

5

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Susan Kane

6

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Qingyuan Ge

7

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Wei Gu

8

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David Orren

9

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Jianyuan Luo

Journal of Biological Chemistry

10

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language of work or name

English

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publication date

21 March 2008

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published in

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volume

283

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page(s)

7590-8

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issue

12

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cites work

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Positional cloning of the Werner's syndrome gene

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The Bloom's syndrome gene product is homologous to RecQ helicases

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Mutations in RECQL4 cause a subset of cases of Rothmund-Thomson syndrome

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An apoptosis-inducing genotoxin differentiates heterozygotic carriers for Werner helicase mutations from wild-type and homozygous mutants

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A deletion within the murine Werner syndrome helicase induces sensitivity to inhibitors of topoisomerase and loss of cellular proliferative capacity

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Mutator phenotype of Werner syndrome is characterized by extensive deletions

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Werner syndrome: molecular insights into the relationships between defective DNA metabolism, genomic instability, cancer and aging

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Werner's syndrome protein (WRN) migrates Holliday junctions and co-localizes with RPA upon replication arrest

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p53 Modulates the exonuclease activity of Werner syndrome protein

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Regulation of the Werner helicase through a direct interaction with a subunit of protein kinase A

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Werner helicase is localized to transcriptionally active nucleoli of cycling cells

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Werner helicase relocates into nuclear foci in response to DNA damaging agents and co-localizes with RPA and Rad51.

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DNA damage-induced translocation of the Werner helicase is regulated by acetylation

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Cellular dynamics and modulation of WRN protein is DNA damage specific

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Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase

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Negative control of p53 by Sir2alpha promotes cell survival under stress

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hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase

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Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence

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Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase

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The mammalian SIR2alpha protein has a role in embryogenesis and gametogenesis

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Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice

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Werner syndrome and the function of the Werner protein; what they can teach us about the molecular aging process.

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Mammalian SIRT1 represses forkhead transcription factors

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Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase

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Bioinformatic analysis of the nucleolus

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Current advances in unraveling the function of the Werner syndrome protein

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Werner syndrome protein is regulated and phosphorylated by DNA-dependent protein kinase

21 January 2018

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Werner protein is a target of DNA-dependent protein kinase in vivo and in vitro, and its catalytic activities are regulated by phosphorylation

21 January 2018

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RecQ helicases: suppressors of tumorigenesis and premature aging.

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Acetylation of the C terminus of Ku70 by CBP and PCAF controls Bax-mediated apoptosis

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Expression and localization of Werner syndrome protein is modulated by SIRT1 and PML.

21 January 2018

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Physical and functional interaction between p53 and the Werner's syndrome protein

21 January 2018

1 reference

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Structure of a Sir2 enzyme bound to an acetylated p53 peptide

21 January 2018

1 reference

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The processing of Holliday junctions by BLM and WRN helicases is regulated by p53

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709707200

p53 modulates RPA-dependent and RPA-independent WRN helicase activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709707200

Chromosome instability in lymphocytes from a patient with Werner's syndrome is not associated with DNA repair defects

21 January 2018

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1074/JBC.M709707200

1 reference

Consolidated OpenCitations Corpus – April 2017

4821151

4821151

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference