相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。Identification of γ-secretase inhibitor potency determinants on presenilin
Byron Zhao et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2008)
Signal peptide peptidase and γ-secretase share equivalent inhibitor binding pharmacology
Lawrence G. Iben et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2007)
Structure of a site-2 protease family intramembrane metalloprotease
Liang Feng et al.
SCIENCE (2007)
Enzymatic analysis of a rhomboid intramembrane protease implicates transmembrane helix 5 as the lateral substrate gate
Rosanna P. Baker et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2007)
Structural analysis of a rhomboid family intramembrane protease reveals a gating mechanism for substrate entry
Zhuoru Wu et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2006)
Structure of the catalytic pore of γ-secretase probed by the accessibility of substituted cysteines
Chihiro Sato et al.
JOURNAL OF NEUROSCIENCE (2006)
Crystal structure of a rhomboid family intramembrane protease
Yongcheng Wang et al.
NATURE (2006)
Contribution of presenilin transmembrane domains 6 and 7 to a water-containing cavity in the γ-secretase complex
Alexandra Tolia et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2006)
Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway
Dragana Spasic et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2006)
Signal peptide peptidase: Biochemical properties and modulation by nonsteroidal antiinflammatory drugs
Toru Sato et al.
BIOCHEMISTRY (2006)
C-terminal fragment of presenilin is the molecular target of a dipeptidic γ-secretase-specific inhibitor DAPT (N-[N-(3,5-difluorophenacetyl)-L-alanyl]-S-phenylglycine t-butyl ester)
Yuichi Morohashi et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2006)
Force-dependent chemical kinetics of disulfide bond reduction observed with single-molecule techniques
Arun P. Wiita et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2006)
DAPT-induced intracellular accumulations of longer amyloid β-proteins:: Further implications for the mechanism of intramembrane cleavage by γ-secretase
S Yagishita et al.
BIOCHEMISTRY (2006)
C-terminal PAL motif of presenilin and presenilin homologues required for normal active site conformation
J Wang et al.
JOURNAL OF NEUROCHEMISTRY (2006)
Calibrated measurement of gating-charge arginine displacement in the KvAP voltage-dependent K+ channel
V Ruta et al.
CELL (2005)
A nine-transmembrane domain topology for presenilin 1
H Laudon et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2005)
Nicastrin functions as a γ-secretase-substrate receptor
S Shah et al.
CELL (2005)
Aph-1 contributes to the stabilization and trafficking of the γ-secretase complex through mechanisms involving intermolecular and intramolecular interactions
M Niimura et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2005)
The initial substrate-binding site of γ-secretase is located on presenilin near the active site
AY Kornilova et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2005)
Longer forms of amyloid β protein:: Implications for the mechanism of intramembrane cleavage by γ-secretase
Y Qi-Takahara et al.
JOURNAL OF NEUROSCIENCE (2005)
Conserved PAL sequence in presenilins is essential for γ-secretase activity, but not required for formation or stabilization of γ-secretase complexes
J Wang et al.
NEUROBIOLOGY OF DISEASE (2004)
Identification of a new presenilin-dependent ζ-cleavage site within the transmembrane domain of amyloid precursor protein
GJ Zhao et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2004)
Functional domains in presenilin 1 -: The TYR-288 residue controls γ-secretase activity and endoproteolysis
H Laudon et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2004)
γ-secretase:: proteasome of the membrane?
R Kopan et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2004)
A signal peptide peptidase (SPP) reporter activity assay based on the cleavage of type II membrane protein substrates provides further evidence for an inverted orientation of the SPP active site relative to presenilin
AC Nyborg et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2004)
Mechanism of γ-secretase cleavage activation:: Is γ-secretase regulated through autoinhibition involving the presenilin-1 exon 9 loop?
KS Knappenberger et al.
BIOCHEMISTRY (2004)
Transmembrane domain II of the Na plus /proline transporter PutP of Escherichia coli forms part of a conformationally flexible, cytoplasmic exposed aqueous cavity within the membrane
T Pirch et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2003)
Intramembrane-cleaving aspartic proteases and disease: presenilins, signal peptide peptidase and their homologs
B Martoglio et al.
HUMAN MOLECULAR GENETICS (2003)
Mechanisms of drug/H+ antiport:: complete cysteine-scanning mutagenesis and the protein engineering approach
N Tamura et al.
CURRENT OPINION IN CHEMICAL BIOLOGY (2003)
γ-secretase is a membrane protein complex comprised of presenilin, nicastrin, aph-1, and pen-2
WT Kimberly et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2003)
Targeting presenilin-type aspartic protease signal peptide peptidase with γ-secretase inhibitors
A Weihofen et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2003)
The principle of gating charge movement in a voltage-dependent K+ channel
YX Jiang et al.
NATURE (2003)
Reconstitution of γ-secretase activity
D Edbauer et al.
NATURE CELL BIOLOGY (2003)
Substrate-induced conformational, changes in the transmembrane segments of human P-glycoprotein - Direct evidence for the substrate-induced fit mechanism for drug binding
TW Loo et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2003)
Aph-1, Pen-2, and nicastrin with presenilin generate an active γ-secretase complex
B De Strooper
NEURON (2003)
PEN-2 and APH-1 coordinately regulate proteolytic processing of presenilin 1
WJ Luo et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2003)
Electrostatic potentials and covalent radii
P Politzer et al.
JOURNAL OF COMPUTATIONAL CHEMISTRY (2003)
Intramembrane-cleaving proteases: controlled liberation of proteins and bioactive peptides
A Weihofen et al.
TRENDS IN CELL BIOLOGY (2003)
Proline-induced distortions of transmembrane helices
FS Cordes et al.
JOURNAL OF MOLECULAR BIOLOGY (2002)
Presenilin-1 affects trafficking and processing of βAPP and is targeted in a complex with nicastrin to the plasma membrane
C Kaether et al.
JOURNAL OF CELL BIOLOGY (2002)
Identification of signal peptide peptidase, a presenilin-type aspartic protease
A Weihofen et al.
SCIENCE (2002)
A novel ε-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with notch processing
A Weidemann et al.
BIOCHEMISTRY (2002)
Interaction with telencephalin and the amyloid precursor protein predicts a ring structure for presenilins
WG Annaert et al.
NEURON (2001)
Presenilin dependent γ-secretase processing of β-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch
M Sastre et al.
EMBO REPORTS (2001)
The kamikaze approach to membrane transport
HR Kaback et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2001)