The condensing activities of the Mycobacterium tuberculosis type II fatty acid synthase are differentially regulated by phosphorylation (Q28487302)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16873379%20AND%20SRC:MED&resulttype=core&format=json

27 December 2019

title

The condensing activities of the Mycobacterium tuberculosis type II fatty acid synthase are differentially regulated by phosphorylation (English)

2 references

24 January 2017

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16873379%20AND%20SRC:MED&resulttype=core&format=json

Mycobacterium tuberculosis

27 December 2019

main subject

fatty acid

0 references

0 references

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1

1 reference

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27 December 2019

Gurdyal Besra

series ordinal

3

1 reference

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27 December 2019

5

Laurent Kremer

2 references

24 January 2017

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27 December 2019

author name string

Alistair K Brown

series ordinal

2

1 reference

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27 December 2019

Alain J Cozzone

series ordinal

4

1 reference

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27 December 2019

language of work or name

English

0 references

publication date

27 July 2006

1 reference

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Journal of Biological Chemistry

27 December 2019

published in

2 references

24 January 2017

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27 December 2019

volume

281

2 references

24 January 2017

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27 December 2019

page(s)

30094-30103

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27 December 2019

issue

40

2 references

24 January 2017

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The Envelope of Mycobacteria

27 December 2019

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Purification and biochemical characterization of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthases KasA and KasB

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Mycolic acid biosynthesis and enzymic characterization of the beta-ketoacyl-ACP synthase A-condensing enzyme from Mycobacterium tuberculosis

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A serine/threonine protein kinase from Mycobacterium tuberculosis

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Protein PknE, a novel transmembrane eukaryotic-like serine/threonine kinase from Mycobacterium tuberculosis

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Evidence that a eukaryotic-type serine/threonine protein kinase from Mycobacterium tuberculosis regulates morphological changes associated with cell division

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Phosphoprotein phosphatase of Mycobacterium tuberculosis dephosphorylates serine–threonine kinases PknA and PknB

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PknB kinase activity is regulated by phosphorylation in two Thr residues and dephosphorylation by PstP, the cognate phospho-Ser/Thr phosphatase, in Mycobacterium tuberculosis

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Serine/threonine protein kinases PknF and PknG of Mycobacterium tuberculosis: characterization and localization

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Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases

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Cloning, overexpression, and characterization of a serine/threonine protein kinase pknI from Mycobacterium tuberculosis H37Rv

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An FHA phosphoprotein recognition domain mediates protein EmbR phosphorylation by PknH, a Ser/Thr protein kinase from Mycobacterium tuberculosis

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Proteomic identification of M. tuberculosis protein kinase substrates: PknB recruits GarA, a FHA domain-containing protein, through activation loop-mediated interactions

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The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: substrate identification and regulation of cell shape

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The serine/threonine kinase PknB of Mycobacterium tuberculosis phosphorylates PBPA, a penicillin-binding protein required for cell division

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Protein-protein interactions within the Fatty Acid Synthase-II system of Mycobacterium tuberculosis are essential for mycobacterial viability

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Biochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA:AcpM transacylase (mtFabD), two major components of Mycobacterium tuberculosis fatty acid synthase II

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pH-dependent pore-forming activity of OmpATb from Mycobacterium tuberculosis and characterization of the channel by peptidic dissection

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Identifiers

DOI

10.1074/JBC.M601691200

2 references

Consolidated OpenCitations Corpus – April 2017

785139

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16873379%20AND%20SRC:MED&resulttype=core&format=json

27 December 2019

785139

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

2 references

785139