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Home › Research › Topics › transmembrane-domain

transmembrane-domain

3 studies tagged transmembrane-domain, dated 2009-10-01 to 2017-08-08. Bibliography: BibTeX (.bib) · RIS (.ris)

Newest in this topic

  1. Dimerization of the transmembrane domain of amyloid precursor protein is determined by residues around the γ-secretase cleavage sites 2017-08-08
  2. The amyloid precursor protein has a flexible transmembrane domain and binds cholesterol 2012-06-01
  3. gamma-Secretase: successive tripeptide and tetrapeptide release from the transmembrane domain of beta-carboxyl terminal fragment 2009-10-01

Studies

3 studies carry this tag.

Date range

2009 to 2017

Top journals

  • Science (New York, N.Y.) 1
  • The Journal of biological chemistry 1
  • The Journal of neuroscience : the official journal of the Society for Neuroscience 1

Newest first, then by address. Each study has a usefulness score out of 100 (rubric version 4.0); tap a score to see what makes it up. Tags were assigned automatically from each study's title and summary. The same studies as a filter in the library.

  1. Dimerization of the transmembrane domain of amyloid precursor protein is determined by residues around the γ-secretase cleavage sites

    ✓ Peer-reviewed alzhub usefulness score 41 out of 100. The Journal of biological chemistry 2017-08-08 Biomarkers

    One of the hallmarks of Alzheimer's disease is the formation of extracellular amyloid plaques that consist mainly of abnormally aggregated forms of amyloid β (Aβ) peptides.

  2. The amyloid precursor protein has a flexible transmembrane domain and binds cholesterol

    ✓ Peer-reviewed alzhub usefulness score 41 out of 100. Science (New York, N.Y.) 2012-06-01 Risk genes beyond APOE

    C99 is the transmembrane carboxyl-terminal domain of the amyloid precursor protein that is cleaved by γ-secretase to release the amyloid-β polypeptides, which are associated with Alzheimer's disease.

  3. gamma-Secretase: successive tripeptide and tetrapeptide release from the transmembrane domain of beta-carboxyl terminal fragment

    ✓ Peer-reviewed alzhub usefulness score 36 out of 100. The Journal of neuroscience : the official journal of the Society for Neuroscience 2009-10-01 Risk genes beyond APOE

    Amyloid beta protein (Abeta), a pathogenic molecule associated with Alzheimer's disease, is produced by gamma-secretase, which cleaves the beta-carboxyl terminal fragment (betaCTF) of beta-amyloid precursor protein in the middle of its transmembrane domain.

All topic tags with their study counts