Methods for analysis of O-linked modifications on epidermal growth factor-like and thrombospondin type 1 repeats (Q36667093)

15 August 2017

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title

Methods for analysis of O-linked modifications on epidermal growth factor-like and thrombospondin type 1 repeats (English)

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15 August 2017

author name string

Aleksandra Nita-Lazar

series ordinal

1

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15 August 2017

Robert S Haltiwanger

series ordinal

2

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15 August 2017

language of work or name

English

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publication date

1 January 2006

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15 August 2017

published in

Methods in Enzymology

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15 August 2017

volume

417

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15 August 2017

page(s)

93-111

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CADASIL mutations impair Notch3 glycosylation by Fringe

15 August 2017

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Mitotic arrest with nocodazole induces selective changes in the level of O-linked N-acetylglucosamine and accumulation of incompletely processed N-glycans on proteins from HT29 cells

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Modulation of receptor signaling by glycosylation: fringe is an O-fucose-beta1,3-N-acetylglucosaminyltransferase

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Protein O-fucosyltransferase 2 adds O-fucose to thrombospondin type 1 repeats

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Two distinct pathways for O-fucosylation of epidermal growth factor-like or thrombospondin type 1 repeats

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Fringe is a glycosyltransferase that modifies Notch

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Mammalian Notch1 is modified with two unusual forms of O-linked glycosylation found on epidermal growth factor-like modules

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Regulation of notch signaling by o-linked fucose.

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Highly conserved O-fucose sites have distinct effects on Notch1 function

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Lunatic fringe, manic fringe, and radical fringe recognize similar specificity determinants in O-fucosylated epidermal growth factor-like repeats

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7 January 2021

Glycosylation engineering

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7 January 2021

Complementation between mutants of CHO cells resistant to a variety of plant lectins

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Identifiers

DOI

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15 August 2017

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