Chemical Synthesis of a Glycopeptide Derived from Skp1 for Probing Protein Specific Glycosylation.

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O2 sensing associated glycosylation exposes the F-box combining site of the Dictyostelium Skp1 subunit in E3 ubiquitin ligases.Characterization of a cytoplasmic glucosyltransferase that extends the core trisaccharide of the Toxoplasma Skp1 E3 ubiquitin ligase subunit.

P2860

Q42691716-9C2FE711-9138-4584-92F2-08CBE8AE7597 Q47192541-ACF4B942-5A15-42D5-AEB4-77598012F461

P2860

Chemical Synthesis of a Glycopeptide Derived from Skp1 for Probing Protein Specific Glycosylation.

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http://www.wikidata.org/entity/Q43174038

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2015 nî lūn-bûn

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2015年の論文

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2015年学术文章

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2015年学术文章

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2015年学术文章

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2015年學術文章

@zh-hant

name

Chemical Synthesis of a Glycop ...... rotein Specific Glycosylation.

@en

Chemical Synthesis of a Glycop ...... rotein Specific Glycosylation.

@nl

type

Item

label

Chemical Synthesis of a Glycop ...... rotein Specific Glycosylation.

@en

Chemical Synthesis of a Glycop ...... rotein Specific Glycosylation.

@nl

prefLabel

Chemical Synthesis of a Glycop ...... rotein Specific Glycosylation.

@en

Chemical Synthesis of a Glycop ...... rotein Specific Glycosylation.

@nl

P1476

Chemical Synthesis of a Glycop ...... rotein Specific Glycosylation.

@en

P2093

Christopher M Schafer

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

Christopher M West

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

Zoeisha S Chinoy

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

P2860

A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin

The cytoplasmic F-box binding protein SKP1 contains a novel pentasaccharide linked to hydroxyproline in Dictyostelium.

Chemical synthesis of Arabidopsis CLV3 glycopeptide reveals the impact of hydroxyproline arabinosylation on peptide conformation and activity.

Role of the Skp1 prolyl-hydroxylation/glycosylation pathway in oxygen dependent submerged development of Dictyostelium.

Functional glycomic analysis of human milk glycans reveals the presence of virus receptors and embryonic stem cell biomarkers.

Conformational changes associated with post-translational modifications of Pro(143) in Skp1 of Dictyostelium--a dipeptide model system.

Synthesis of peptides and glycopeptides with polyproline II helical topology as potential antifreeze molecules.

Glycosylation of Skp1 promotes formation of Skp1-cullin-1-F-box protein complexes in dictyostelium.

Prolyl hydroxylation- and glycosylation-dependent functions of Skp1 in O2-regulated development of Dictyostelium

Skp1 prolyl 4-hydroxylase of dictyostelium mediates glycosylation-independent and -dependent responses to O2 without affecting Skp1 stability.

P304

11779-11787

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P31

scholarly article

P356

10.1002/CHEM.201501598

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

P407

English

P433

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

P478

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

P50

Geert-Jan Boons

P577

2015-07-15T00:00:00Z

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

P698

26179871

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

P921

glycosylation

P932

4646072

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

Chemical Synthesis of a Glycopeptide Derived from Skp1 for Probing Protein Specific Glycosylation.

about

P2860

P2860

Chemical Synthesis of a Glycopeptide Derived from Skp1 for Probing Protein Specific Glycosylation.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932