(Q43187910)

English

Substituting N(epsilon)-thioacetyl-lysine for N(epsilon)-acetyl-lysine in peptide substrates as a general approach to inhibiting human NAD(+)-dependent protein deacetylases

scientific article published on 7 January 2008

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

15 November 2017

Substituting N(epsilon)-thioacetyl-lysine for N(epsilon)-acetyl-lysine in peptide substrates as a general approach to inhibiting human NAD(+)-dependent protein deacetylases (English)

1 reference

Europe PubMed Central

PMC publication ID

15 November 2017

author name string

David G Fatkins

1

1 reference

Europe PubMed Central

PMC publication ID

15 November 2017

Weiping Zheng

2

1 reference

Europe PubMed Central

PMC publication ID

15 November 2017

language of work or name

0 references

publication date

7 January 2008

1 reference

Europe PubMed Central

PMC publication ID

15 November 2017

International Journal of Molecular Sciences

1 reference

Europe PubMed Central

PMC publication ID

15 November 2017

9

1 reference

Europe PubMed Central

PMC publication ID

15 November 2017

1

1 reference

Europe PubMed Central

PMC publication ID

15 November 2017

1-11

1 reference

Europe PubMed Central

PMC publication ID

15 November 2017

copyright license

Creative Commons Attribution 4.0 International

7 January 2008

1 reference

April 2022 Public Data File from Crossref

copyright status

0 references

A spectrophotometric assay for histone deacetylase 8.

1 reference

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Histone deacetylase inhibitors: molecular mechanisms of action

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Chemistry of acetyl transfer by histone modifying enzymes: structure, mechanism and implications for effector design

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Histone deacetylases and cancer

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The Sir 2 family of protein deacetylases

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Preparation of enzymatically active recombinant class III protein deacetylases.

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Transmembrane delivery of protein and peptide drugs by TAT-mediated transduction in the treatment of cancer

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Adaptive translocation: the role of hydrogen bonding and membrane potential in the uptake of guanidinium-rich transporters into cells

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The determination of enzyme inhibitor constants

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25 May 2018

Histone Deacetylases: Unique Players in Shaping the Epigenetic Histone Code

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Guanidinium rich peptide transporters and drug delivery

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Structure of a Sir2 enzyme bound to an acetylated p53 peptide

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25 May 2018

SIR2 family of NAD(+)-dependent protein deacetylases.

1 reference

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25 May 2018

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

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Chemistry of gene silencing: the mechanism of NAD+-dependent deacetylation reactions

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Standard Fmoc protocols

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Mechanism-based inhibition of Sir2 deacetylases by thioacetyl-lysine peptide

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1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Nepsilon-thioacetyl-lysine: a multi-facet functional probe for enzymatic protein lysine Nepsilon-deacetylation

1 reference

https://pubmed.ncbi.nlm.nih.gov/19325715

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

N(epsilon)-methanesulfonyl-lysine as a non-hydrolyzable functional surrogate for N(epsilon)-acetyl-lysine

1 reference

https://pubmed.ncbi.nlm.nih.gov/19325715

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.3390/IJMS9010001

1 reference

Europe PubMed Central

PMC publication ID

15 November 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

15 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

15 November 2017

ResearchGate publication ID

0 references

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