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cAMP-regulated protein lysine acetylases in mycobacteria
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scholarly article
1 reference
stated in
PubMed
PubMed ID
20507997
retrieved
24 January 2017
title
cAMP-regulated protein lysine acetylases in mycobacteria
(English)
1 reference
stated in
PubMed
PubMed ID
20507997
retrieved
24 January 2017
author
Subhalaxmi Nambi
series ordinal
1
object named as
Subhalaxmi Nambi
1 reference
stated in
PubMed
PubMed ID
20507997
retrieved
24 January 2017
Sandhya Srikant Visweswariah
series ordinal
3
object named as
Sandhya S. Visweswariah
1 reference
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PubMed
PubMed ID
20507997
retrieved
24 January 2017
author name string
Nirmalya Basu
series ordinal
2
1 reference
stated in
PubMed
PubMed ID
20507997
retrieved
24 January 2017
language of work or name
English
0 references
publication date
6 August 2010
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stated in
PubMed
PubMed ID
20507997
retrieved
24 January 2017
published in
Journal of Biological Chemistry
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stated in
PubMed
PubMed ID
20507997
retrieved
24 January 2017
volume
285
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stated in
PubMed
PubMed ID
20507997
retrieved
24 January 2017
issue
32
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stated in
PubMed
PubMed ID
20507997
retrieved
24 January 2017
page(s)
24313–24323
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stated in
PubMed
PubMed ID
20507997
retrieved
24 January 2017
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Overexpression of the chromosomally encoded aminoglycoside acetyltransferase eis confers kanamycin resistance in Mycobacterium tuberculosis
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PKA-I holoenzyme structure reveals a mechanism for cAMP-dependent activation
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Proteome-wide prediction of acetylation substrates
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Profound asymmetry in the structure of the cAMP-free cAMP Receptor Protein (CRP) from Mycobacterium tuberculosis
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Structure and chemistry of the p300/CBP and Rtt109 histone acetyltransferases: implications for histone acetyltransferase evolution and function
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Classification and phylogenetic analysis of the cAMP-dependent protein kinase regulatory subunit family
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Predicted structures of the cGMP binding domains of the cGMP-dependent protein kinase: a key alanine/threonine difference in evolutionary divergence of cAMP and cGMP binding sites
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A bacterial acetyltransferase capable of regioselective N-acetylation of antibiotics and histones
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The role of hydrophobic microenvironments in modulating pKa shifts in proteins.
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In vivo acetylation of CheY, a response regulator in chemotaxis of Escherichia coli
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Functional Classification of cNMP-binding Proteins and Nucleotide Cyclases with Implications for Novel Regulatory Pathways in Mycobacterium tuberculosis
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21 January 2018
Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/20507997
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1074/JBC.M110.118398
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4731818
OpenCitations bibliographic resource ID
4731818
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4731818
PMCID
2915667
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4731818
PubMed ID
20507997
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4731818
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