Phosphoproteomic analysis reveals major default phosphorylation sites outside long intrinsically disordered regions of Arabidopsis plasma membrane proteins.

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Advantages of proteins being disordered.Plant Lectins and Lectin Receptor-Like Kinases: How Do They Sense the Outside?The porcine odorant-binding protein as molecular probe for benzene detection

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Phosphoproteomic analysis reveals major default phosphorylation sites outside long intrinsically disordered regions of Arabidopsis plasma membrane proteins.

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http://www.wikidata.org/entity/Q42010431

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2012 nî lūn-bûn

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2012年の論文

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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name

Phosphoproteomic analysis reve ...... psis plasma membrane proteins.

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Phosphoproteomic analysis reve ...... psis plasma membrane proteins.

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Phosphoproteomic analysis reve ...... psis plasma membrane proteins.

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Phosphoproteomic analysis reve ...... psis plasma membrane proteins.

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Phosphoproteomic analysis reve ...... psis plasma membrane proteins.

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Phosphoproteomic analysis reve ...... psis plasma membrane proteins.

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Phosphoproteomic analysis reve ...... opsis plasma membrane proteins

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P2093

Claude Nespoulous

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Michel Rossignol

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Sonia Hem

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

Valérie Rofidal

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

P2860

Phosphoproteomic Analysis of the Mouse Brain Cytosol Reveals a Predominance of Protein Phosphorylation in Regions of Intrinsic Sequence Disorder

Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life

MeDor: a metaserver for predicting protein disorder

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

The importance of intrinsic disorder for protein phosphorylation

Analysis of structured and intrinsically disordered regions of transmembrane proteins

Understanding protein non-folding.

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

Investigation of transmembrane proteins using a computational approach

GRAS proteins: the versatile roles of intrinsically disordered proteins in plant signalling.

P2888

1477-5956-10-62

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scholarly article

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10.1186/1477-5956-10-62

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Nicolas Sommerer

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2012-10-30T00:00:00Z

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232740279

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1045889012

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23110452

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P921

phosphorylation

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3537754

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Phosphoproteomic analysis reveals major default phosphorylation sites outside long intrinsically disordered regions of Arabidopsis plasma membrane proteins.

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P2860

P2860

Phosphoproteomic analysis reveals major default phosphorylation sites outside long intrinsically disordered regions of Arabidopsis plasma membrane proteins.

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P1476

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