p25alpha is flexible but natively folded and binds tubulin with oligomeric stoichiometry. - Wikidata - awgldk - TriplyDB

p25alpha is flexible but natively folded and binds tubulin with oligomeric stoichiometry.

p25alpha is flexible but natively folded and binds tubulin with oligomeric stoichiometry.

http://www.wikidata.org/entity/Q41910014

about

Phosphoproteomic Analysis of the Mouse Brain Cytosol Reveals a Predominance of Protein Phosphorylation in Regions of Intrinsic Sequence Disorder p25alpha relocalizes in oligodendroglia from myelin to cytoplasmic inclusions in multiple system atrophy Construct optimization for protein NMR structure analysis using amide hydrogen/deuterium exchange mass spectrometry.P25alpha/Tubulin polymerization promoting protein expression by myelinating oligodendrocytes of the developing rat brain.Identification of synaptosomal proteins binding to monomeric and oligomeric α-synuclein.Self protein-protein interactions are involved in TPPP/p25 mediated microtubule bundling Immunohistochemical markers for quantitative studies of neurons and glia in human neocortex.Dual life of TPPP/p25 evolved in physiological and pathological conditions.Drosophila Ringmaker regulates microtubule stabilization and axonal extension during embryonic development An unusual intrinsically disordered protein from the model legume Lotus japonicus stabilizes proteins in vitro.Misfolding of a bacterial autotransporter.The CBS domain protein MJ0729 of Methanocaldococcus jannaschii binds DNA.

P2860

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P2860

p25alpha is flexible but natively folded and binds tubulin with oligomeric stoichiometry.

http://www.wikidata.org/entity/Q41910014

description

2005 nî lūn-bûn

@nan

2005年の論文

@ja

2005年論文

@yue

2005年論文

@zh-hant

2005年論文

@zh-hk

2005年論文

@zh-mo

2005年論文

@zh-tw

2005年论文

@wuu

2005年论文

@zh

2005年论文

@zh-cn

name

p25alpha is flexible but natively folded and binds tubulin with oligomeric stoichiometry.

@en

type

label

p25alpha is flexible but natively folded and binds tubulin with oligomeric stoichiometry.

@en

prefLabel

p25alpha is flexible but natively folded and binds tubulin with oligomeric stoichiometry.

@en

P1433

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P1476

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P1433

Protein Science

P1476

p25alpha is flexible but natively folded and binds tubulin with oligomeric stoichiometry.

@en

P2093

Ditte M S Lundvig

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

Jakob R Pedersen

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

Lotte H Nielsen

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

P2860

p25alpha Stimulates alpha-synuclein aggregation and is co-localized with aggregated alpha-synuclein in alpha-synucleinopathies

TPPP/p25 promotes tubulin assemblies and blocks mitotic spindle formation

Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2

Calculation of protein extinction coefficients from amino acid sequence data

Expression of the Oct-1 transcription factor and characterization of its interactions with the Bob1 coactivator

Intrinsically disordered protein

The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure

p27 binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding

Intrinsically unstructured proteins

Why are "natively unfolded" proteins unstructured under physiologic conditions?

P304

1396-1409

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

P31

scholarly article

P356

10.1110/PS.041285605

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

P433

6

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

P478

14

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

P50

Reinhard Wimmer

Poul Henning Jensen

P577

2005-05-09T00:00:00Z

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P5875

7858293

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P698

15883183

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P921

P932

2253386

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