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An atomic structure of human γ-secretase
scientific journal article
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scholarly article
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PubMed
PubMed ID
26280335
retrieved
4 January 2017
title
An atomic structure of human γ-secretase
(English)
1 reference
stated in
PubMed
PubMed ID
26280335
retrieved
4 January 2017
main subject
Presenilin enhancer, gamma-secretase subunit
1 reference
stated in
GOA release 2020-03-11
Aph-1 homolog A, gamma-secretase subunit
1 reference
stated in
GOA release 2020-03-11
Presenilin 1
1 reference
stated in
GOA release 2020-03-11
Nicastrin
1 reference
stated in
GOA release 2020-03-11
author
Yigong Shi
series ordinal
9
0 references
Xiao-chen Bai
object named as
Xiao-chen Bai
series ordinal
1
0 references
Sjors Scheres
series ordinal
8
object named as
Sjors H. W. Scheres
1 reference
stated in
PubMed
PubMed ID
26280335
retrieved
4 January 2017
author name string
Chuangye Yan
series ordinal
2
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stated in
PubMed
PubMed ID
26280335
retrieved
4 January 2017
Guanghui Yang
series ordinal
3
1 reference
stated in
PubMed
PubMed ID
26280335
retrieved
4 January 2017
Peilong Lu
series ordinal
4
1 reference
stated in
PubMed
PubMed ID
26280335
retrieved
4 January 2017
Dan Ma
series ordinal
5
1 reference
stated in
PubMed
PubMed ID
26280335
retrieved
4 January 2017
Linfeng Sun
series ordinal
6
1 reference
stated in
PubMed
PubMed ID
26280335
retrieved
4 January 2017
Rui Zhou
series ordinal
7
1 reference
stated in
PubMed
PubMed ID
26280335
retrieved
4 January 2017
language of work or name
English
0 references
publication date
10 September 2015
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stated in
PubMed
PubMed ID
26280335
retrieved
4 January 2017
published in
Nature
1 reference
stated in
PubMed
PubMed ID
26280335
retrieved
4 January 2017
volume
525
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stated in
PubMed
PubMed ID
26280335
retrieved
4 January 2017
page(s)
212–217
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stated in
PubMed
PubMed ID
26280335
retrieved
4 January 2017
issue
7568
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stated in
PubMed
PubMed ID
26280335
retrieved
4 January 2017
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Three-dimensional structure of human γ-secretase
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APH-1 interacts with mature and immature forms of presenilins and nicastrin and may play a role in maturation of presenilin.nicastrin complexes
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Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity
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Structural basis of human γ-secretase assembly
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PubMed Central
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Cleavage of amyloid precursor protein by an archaeal presenilin homologue PSH
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The dynamic conformational landscape of gamma-secretase.
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Presenilins and γ-secretase: structure, function, and role in Alzheimer Disease
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29 September 2017
Glu-333 of nicastrin directly participates in gamma-secretase activity
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29 September 2017
APH1 polar transmembrane residues regulate the assembly and activity of presenilin complexes
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29 September 2017
The C-terminal PAL motif and transmembrane domain 9 of presenilin 1 are involved in the formation of the catalytic pore of the gamma-secretase.
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PubMed Central
reference URL
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29 September 2017
C-terminal PAL motif of presenilin and presenilin homologues required for normal active site conformation
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PubMed Central
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29 September 2017
Conserved "PAL" sequence in presenilins is essential for gamma-secretase activity, but not required for formation or stabilization of gamma-secretase complexes
1 reference
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PubMed Central
reference URL
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29 September 2017
γ-Secretase is a membrane protein complex comprised of presenilin, nicastrin, aph-1, and pen-2
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4568306
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29 September 2017
The role of presenilin cofactors in the gamma-secretase complex
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PubMed Central
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29 September 2017
Membrane topology of gamma-secretase component PEN-2.
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PubMed Central
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29 September 2017
aph-1 and pen-2 are required for Notch pathway signaling, gamma-secretase cleavage of betaAPP, and presenilin protein accumulation
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PubMed Central
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29 September 2017
APH-1 is a multipass membrane protein essential for the Notch signaling pathway in Caenorhabditis elegans embryos
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PubMed Central
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29 September 2017
Cooperative roles of hydrophilic loop 1 and the C-terminus of presenilin 1 in the substrate-gating mechanism of γ-secretase.
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PubMed Central
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2 June 2018
Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions
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2 June 2018
Semi-automated selection of cryo-EM particles in RELION-1.3.
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2 June 2018
Conformation-independent structural comparison of macromolecules with ProSMART
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2 June 2018
Beam-induced motion correction for sub-megadalton cryo-EM particles.
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2 June 2018
Quantifying the local resolution of cryo-EM density maps
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2 June 2018
High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy
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2 June 2018
Nicastrin functions as a gamma-secretase-substrate receptor
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Crossref
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21 January 2018
Nicastrin overexpression in transgenic mice induces aberrant behavior and APP processing.
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Crossref
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21 January 2018
Peptides based on the presenilin-APP binding domain inhibit APP processing and Aβ production through interfering with the APP transmembrane domain
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Crossref
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21 January 2018
Lessons from a failed γ-secretase Alzheimer trial.
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Crossref
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21 January 2018
Identifiers
DOI
10.1038/NATURE14892
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2967409
Dimensions Publication ID
1015026428
0 references
OpenCitations bibliographic resource ID
2967409
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2967409
PMCID
4568306
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2967409
PubMed ID
26280335
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2967409
ResearchGate publication ID
281081606
0 references
Springer Nature article ID
10.1038/nature14892
0 references
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