PKA Type II&#160; Holoenzyme Reveals a Combinatorial Strategy for Isoform Diversity (Q27648758)

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8 January 2020

title

PKA type IIalpha holoenzyme reveals a combinatorial strategy for isoform diversity (English)

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8 January 2020

2

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8 January 2020

author name string

Jian Wu

series ordinal

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17932298%20AND%20SRC:MED&resulttype=core&format=json

8 January 2020

Sventja von Daake

series ordinal

3

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8 January 2020

Susan S Taylor

series ordinal

4

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8 January 2020

language of work or name

English

0 references

publication date

1 October 2007

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8 January 2020

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17932298%20AND%20SRC:MED&resulttype=core&format=json

8 January 2020

volume

318

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8 January 2020

issue

5848

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8 January 2020

page(s)

274-279

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PKA-I holoenzyme structure reveals a mechanism for cAMP-dependent activation

8 January 2020

cites work

1 reference

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Dynamic features of cAMP-dependent protein kinase revealed by apoenzyme crystal structure

20 March 2017

1 reference

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Crystal structure of a transition state mimic of the catalytic subunit of cAMP-dependent protein kinase

20 March 2017

1 reference

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Molecular basis for regulatory subunit diversity in cAMP-dependent protein kinase: crystal structure of the type II beta regulatory subunit

20 March 2017

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Regulatory subunit of protein kinase A: structure of deletion mutant with cAMP binding domains

20 March 2017

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Crystal structure of a complex between the catalytic and regulatory (RIalpha) subunits of PKA

20 March 2017

1 reference

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The hallmark of AGC kinase functional divergence is its C-terminal tail, a cis-acting regulatory module

20 March 2017

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Capturing cyclic nucleotides in action: snapshots from crystallographic studies

29 September 2017

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cAMP activation of PKA defines an ancient signaling mechanism.

29 September 2017

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Using substrate-binding variants of the cAMP-dependent protein kinase to identify novel targets and a kinase domain important for substrate interactions in Saccharomyces cerevisiae

29 September 2017

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The cAMP binding domain: an ancient signaling module

29 September 2017

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The essential role of RI alpha in the maintenance of regulated PKA activity

29 September 2017

1 reference

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Dissecting cAMP binding domain A in the RIalpha subunit of cAMP-dependent protein kinase. Distinct subsites for recognition of cAMP and the catalytic subunit

29 September 2017

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Role of the receptor in the mechanism of action of adenosine 3':5'-cyclic monophosphate

29 September 2017

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cAMP-dependent protein kinase: framework for a diverse family of regulatory enzymes

29 September 2017

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Consequences of cAMP and catalytic-subunit binding on the flexibility of the A-kinase regulatory subunit

29 September 2017

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2.2 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor

21 January 2018

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Conformational differences among solution structures of the type Ialpha, IIalpha and IIbeta protein kinase A regulatory subunit homodimers: role of the linker regions

21 January 2018

1 reference

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The conformationally dynamic C helix of the RIalpha subunit of protein kinase A mediates isoform-specific domain reorganization upon C subunit binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1146447

C subunits binding to the protein kinase A RI alpha dimer induce a large conformational change

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1146447

Interaction of the regulatory and catalytic subunits of cAMP-dependent protein kinase. Electrostatic sites on the type Ialpha regulatory subunit

21 January 2018

1 reference

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Physiological inhibitors of the catalytic subunit of cAMP-dependent protein kinase: effect of magnesium-ATP on protein-protein interactions

21 January 2018

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Phosphorylation of a cyclic adenosine 3':5'-monophosphate-dependent protein kinase from bovine cardiac muscle

21 January 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/17932298

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1126/SCIENCE.1146447

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17932298%20AND%20SRC:MED&resulttype=core&format=json

8 January 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17932298%20AND%20SRC:MED&resulttype=core&format=json

8 January 2020

PubMed publication ID

17932298

1 reference