BID, an interaction partner of protein kinase CK2alpha. (Q53628130)

16 May 2018

title

BID, an interaction partner of protein kinase CK2alpha. (English)

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16 May 2018

author name string

Birgitte B Olsen

series ordinal

1

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16 May 2018

Jørgen Petersen

series ordinal

2

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16 May 2018

Olaf-Georg Issinger

series ordinal

3

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16 May 2018

publication date

1 April 2006

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16 May 2018

published in

Biological Chemistry

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16 May 2018

volume

387

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issue

4

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16 May 2018

page(s)

441-449

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16 May 2018

Phosphorylation of calmodulin fragments by protein kinase CK2. Mechanistic aspects and structural consequences.

cites work

1 reference

https://api.crossref.org/works/10.1515%2FBC.2006.059

Crystal structure of the human protein kinase CK2 regulatory subunit reveals its zinc finger-mediated dimerization

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Solution structure of BID, an intracellular amplifier of apoptotic signaling

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Phosphorylation of bid by casein kinases I and II regulates its cleavage by caspase 8.

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Crystal structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit

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Isolation and characterization of recombinant human casein kinase II subunits alpha and beta from bacteria.

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Protein kinase CK2 and its role in cellular proliferation, development and pathology

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Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis

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Casein kinases: pleiotropic mediators of cellular regulation

21 January 2018

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Proapoptotic BID is an ATM effector in the DNA-damage response

21 January 2018

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A brief overview of the present status of the mechanisms involved in electrospray mass spectrometry

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Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns.

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Protein kinase CK2: structure, regulation and role in cellular decisions of life and death

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Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists

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One-thousand-and-one substrates of protein kinase CK2?

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Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 A resolution.

21 January 2018

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Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme

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Utilization of oriented peptide libraries to identify substrate motifs selected by ATM.

21 January 2018

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Characterization, subcellular localization and nuclear targeting of casein kinase 2 from Zea mays

21 January 2018

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Protein kinase CK2: a challenge to canons

21 January 2018

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Biochemical characterization of the recombinant human Drosophila homologues Timekeeper and Andante involved in the Drosophila circadian oscillator.

21 January 2018

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Proposal for a common nomenclature for sequence ions in mass spectra of peptides

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Dual effect of lysine‐rich polypeptides on the activity of protein kinase CK2

21 January 2018

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Phosphoric acid enhances the performance of Fe(III) affinity chromatography and matrix-assisted laser desorption/ionization tandem mass spectrometry for recovery, detection and sequencing of phosphopeptides

21 January 2018

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A majority of casein kinase II alpha subunit is tightly bound to intranuclear components but not to the beta subunit

21 January 2018

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CK2 inhibits apoptosis and changes its cellular localization following ionizing radiation

21 January 2018

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A role for proapoptotic BID in the DNA-damage response

21 January 2018

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Protein kinase CK2: evidence for a protein kinase CK2beta subunit fraction, devoid of the catalytic CK2alpha subunit, in mouse brain and testicles

21 January 2018

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Regulation of dauer larva development in Caenorhabditis elegans by daf-18, a homologue of the tumour suppressor PTEN

21 January 2018

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The effect of polylysine on casein-kinase-2 activity is influenced by both the structure of the protein/peptide substrates and the subunit composition of the enzyme

21 January 2018

1 reference

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Casein kinase 2 down-regulation and activation by polybasic peptides are mediated by acidic residues in the 55-64 region of the beta-subunit. A study with calmodulin as phosphorylatable substrate

21 January 2018

1 reference

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21 January 2018

Identifiers

DOI

10.1515/BC.2006.059

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16 May 2018

1 reference

16 May 2018