(Q54313663)

English

The over-expression of the wild type or mutant forms of the presenilin-1 protein alters glycoprotein processing in a human neuroblastoma cell line.

scientific article published in July 2003

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

27 May 2018

http://europepmc.org/abstract/MED/12850546

The over-expression of the wild type or mutant forms of the presenilin-1 protein alters glycoprotein processing in a human neuroblastoma cell line. (English)

1 reference

Europe PubMed Central

PubMed publication ID

27 May 2018

http://europepmc.org/abstract/MED/12850546

1 reference

based on heuristic

inferred from title

Kieran C. Breen

3

1 reference

Europe PubMed Central

PubMed publication ID

27 May 2018

http://europepmc.org/abstract/MED/12850546

author name string

Farquhar MJ

1

1 reference

Europe PubMed Central

PubMed publication ID

27 May 2018

http://europepmc.org/abstract/MED/12850546

Gray CW

2

1 reference

Europe PubMed Central

PubMed publication ID

27 May 2018

http://europepmc.org/abstract/MED/12850546

language of work or name

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publication date

1 July 2003

1 reference

Europe PubMed Central

PubMed publication ID

27 May 2018

http://europepmc.org/abstract/MED/12850546

Neuroscience Letters

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Europe PubMed Central

PubMed publication ID

27 May 2018

http://europepmc.org/abstract/MED/12850546

346

1 reference

Europe PubMed Central

PubMed publication ID

27 May 2018

http://europepmc.org/abstract/MED/12850546

1-2

1 reference

Europe PubMed Central

PubMed publication ID

27 May 2018

http://europepmc.org/abstract/MED/12850546

53-56

1 reference

Europe PubMed Central

PubMed publication ID

27 May 2018

http://europepmc.org/abstract/MED/12850546

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Beta amyloid precursor protein mediates neuronal cell-cell and cell-surface adhesion

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The role of glycoproteins in neural development function, and disease

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Presenilin-1 regulates intracellular trafficking and cell surface delivery of beta-amyloid precursor protein

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Alzheimer's disease-associated presenilin 1 in neuronal cells: Evidence for localization to the endoplasmic reticulum-Golgi intermediate compartment

1 reference

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Overexpression of alpha2,3 sialyltransferase in neuroblastoma cells results in an upset in the glycosylation process

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Overexpression of the alpha2,6 (N) sialyltransferase enzyme in human and rat neural cell lines is associated with increased expression of the polysialic acid epitope

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Presenilin-1 affects trafficking and processing of betaAPP and is targeted in a complex with nicastrin to the plasma membrane

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Candidate gene for the chromosome 1 familial Alzheimer's disease locus

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Inhibition of N-glycan processing alters axonal transport of synaptic glycoproteins in vivo.

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Repetitive and transient increases in hippocampal neural cell adhesion molecule polysialylation state following multitrial spatial training.

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Presenilin 1 overexpressions in Chinese hamster ovary (CHO) cells decreases the phosphorylation of retinoblastoma protein: relevance for neurodegeneration.

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gamma-Secretase, Notch, Abeta and Alzheimer's disease: where do the presenilins fit in?

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Nuclear signaling: a common function of presenilin substrates?

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Presenilin-1 is processed into two major cleavage products in neuronal cell lines

1 reference

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Presenilins are not required for A beta 42 production in the early secretory pathway.

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Mature glycosylation and trafficking of nicastrin modulate its binding to presenilins

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Identifiers

10.1016/S0304-3940(03)00544-5

1 reference

Europe PubMed Central

PubMed publication ID

27 May 2018

http://europepmc.org/abstract/MED/12850546

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

27 May 2018

http://europepmc.org/abstract/MED/12850546

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