S100B(betabeta) inhibits the protein kinase C-dependent phosphorylation of a peptide derived from p53 in a Ca2+-dependent manner. - Wikidata - awgldk - TriplyDB

S100B(betabeta) inhibits the protein kinase C-dependent phosphorylation of a peptide derived from p53 in a Ca2+-dependent manner.

S100B(betabeta) inhibits the protein kinase C-dependent phosphorylation of a peptide derived from p53 in a Ca2+-dependent manner.

http://www.wikidata.org/entity/Q36280846

about

S100A16, a novel calcium-binding protein of the EF-hand superfamily The structure of Ca2+-loaded S100A2 at 1.3-Å resolution The use of dipolar couplings for determining the solution structure of rat apo-S100B(ββ)In vitro screening and structural characterization of inhibitors of the S100B-p53 interaction A logical sequence search for S100B target proteins Complex formation between S100B protein and the p90 ribosomal S6 kinase (RSK) in malignant melanoma is calcium-dependent and inhibits extracellular signal-regulated kinase (ERK)-mediated phosphorylation of RSK The effect of pentamidine on melanoma ex vivo.Mapping the zinc ligands of S100A2 by site-directed mutagenesis.Simultaneous inhibition of key growth pathways in melanoma cells and tumor regression by a designed bidentate constrained helical peptide Covalent small molecule inhibitors of Ca(2+)-bound S100B.Structural changes in the C-terminus of Ca2+-bound rat S100B (beta beta) upon binding to a peptide derived from the C-terminal regulatory domain of p53.Evaluation of potential interactions between the metastasis-associated protein S100A4 and the tumor suppressor protein p53.The evolution of S100B inhibitors for the treatment of malignant melanoma.The calcium-binding protein S100A2 interacts with p53 and modulates its transcriptional activity.A New Technique for Collection of Cerebrospinal Fluid in Rat Pups.Structural and thermodynamic characterization of the recognition of the S100-binding peptides TRTK12 and p53 by calmodulin Thermodynamic and kinetic analysis of peptides derived from CapZ, NDR, p53, HDM2, and HDM4 binding to human S100B The Calcium-Dependent Interaction of S100B with Its Protein Targets.Insight into a novel p53 single point mutation (G389E) by Molecular Dynamics Simulations.Inhibition of p53 transcriptional activity by the S100B calcium-binding protein.Intraperitoneal treatment with S100B enhances hippocampal neurogenesis in juvenile mice and after experimental brain injury.Calcium-dependent interaction of S100B with the C-terminal domain of the tumor suppressor p53.

P2860

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P2860

S100B(betabeta) inhibits the protein kinase C-dependent phosphorylation of a peptide derived from p53 in a Ca2+-dependent manner.

http://www.wikidata.org/entity/Q36280846

description

1998 nî lūn-bûn

@nan

1998年の論文

@ja

1998年学术文章

@wuu

1998年学术文章

@zh-cn

1998年学术文章

@zh-hans

1998年学术文章

@zh-my

1998年学术文章

@zh-sg

1998年學術文章

@yue

1998年學術文章

@zh

1998年學術文章

@zh-hant

name

S100B(betabeta) inhibits the p ...... 53 in a Ca2+-dependent manner.

@ast

S100B(betabeta) inhibits the p ...... 53 in a Ca2+-dependent manner.

@en

type

label

S100B(betabeta) inhibits the p ...... 53 in a Ca2+-dependent manner.

@ast

S100B(betabeta) inhibits the p ...... 53 in a Ca2+-dependent manner.

@en

prefLabel

S100B(betabeta) inhibits the p ...... 53 in a Ca2+-dependent manner.

@ast

S100B(betabeta) inhibits the p ...... 53 in a Ca2+-dependent manner.

@en

P1433

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P2860

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P356

P1433

Protein Science

P1476

S100B(betabeta) inhibits the p ...... 53 in a Ca2+-dependent manner.

@en

P2093

A C Drohat

http://www.w3.org/2001/XMLSchema#string

D J Weber

http://www.w3.org/2001/XMLSchema#string

P T Wilder

http://www.w3.org/2001/XMLSchema#string

R R Rustandi

http://www.w3.org/2001/XMLSchema#string

P2860

Comparison of S100b protein with calmodulin: interactions with melittin and microtubule-associated tau proteins and inhibition of phosphorylation of tau proteins by protein kinase C

Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy

The solution structure of the bovine S100B protein dimer in the calcium-free state

Protein kinase C-mediated phosphorylation and calmodulin binding of recombinant myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein

The S100 family of EF-hand calcium-binding proteins: functions and pathology

The S100 protein family: history, function, and expression

Inhibition by calmodulin of calcium/phospholipid-dependent protein phosphorylation

Oligomerization state of S100B at nanomolar concentration determined by large-zone analytical gel filtration chromatography

Characterization of S-100b binding epitopes. Identification of a novel target, the actin capping protein, CapZ.

Interactions of myogenic bHLH transcription factors with calcium-binding calmodulin and S100a (alpha alpha) proteins.

P304

794-798

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1002/PRO.5560070330

http://www.w3.org/2001/XMLSchema#string

P433

3

http://www.w3.org/2001/XMLSchema#string

P478

7

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P577

1998-03-01T00:00:00Z

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P5875

227637742

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P698

9541413

http://www.w3.org/2001/XMLSchema#string

P921

phosphorylation

P932

2143941

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