Molecular defects that cause loss of polysialic acid in the complementation group 2A10. (Q47841500)

6 February 2018

title

Molecular defects that cause loss of polysialic acid in the complementation group 2A10. (English)

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6 February 2018

author name string

Windfuhr M

1

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6 February 2018

Manegold A

2

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6 February 2018

Muhlenhoff M

3

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6 February 2018

Eckhardt M

4

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6 February 2018

Gerardy-Schahn R

5

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6 February 2018

language of work or name

English

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publication date

1 October 2000

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6 February 2018

Journal of Biological Chemistry

published in

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6 February 2018

volume

275

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6 February 2018

issue

42

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6 February 2018

page(s)

32861-32870

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6 February 2018

The neural cell adhesion molecule (NCAM) in development and plasticity of the nervous system.

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Identification of a peptide sequence involved in homophilic binding in the neural cell adhesion molecule NCAM

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The first immunoglobulin-like neural cell adhesion molecule (NCAM) domain is involved in double-reciprocal interaction with the second immunoglobulin-like NCAM domain and in heparin binding.

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Polysialic acid and the regulation of cell interactions

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Distribution and possible roles of the highly polysialylated neural cell adhesion molecule (NCAM-H) in the developing and adult central nervous system

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PSA-NCAM is required for activity-induced synaptic plasticity.

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The role of polysialic acid in migration of olfactory bulb interneuron precursors in the subventricular zone.

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Neurite outgrowth in response to transfected N-CAM changes during development and is modulated by polysialic acid

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Serum polysialylated neural cell adhesion molecule in childhood neuroblastoma

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A human polysialyltransferase directs in vitro synthesis of polysialic acid

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Differential and cooperative polysialylation of the neural cell adhesion molecule by two polysialyltransferases, PST and STX.

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In vivo autopolysialylation and localization of the polysialyltransferases PST and STX.

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Polysialyltransferase-1 autopolysialylation is not requisite for polysialylation of neural cell adhesion molecule

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Oligomerization of a membrane protein correlates with its retention in the Golgi complex

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Post-translational modifications distinguish cell surface from Golgi-retained beta 1,4 galactosyltransferase molecules. Golgi localization involves active retention.

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Mutation of the sialyltransferase S-sialylmotif alters the kinetics of the donor and acceptor substrates

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Developmental expression and characterization of the alpha2,8-polysialyltransferase activity in embryonic chick brain

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21 January 2018

Identifiers

DOI

10.1074/JBC.M003507200

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6 February 2018

PubMed ID

10921918

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6 February 2018