gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

SPPL3 signal peptide peptidase-like 3

SPPL3, intramembrane protease, signal peptide peptidase like 3
Top mentioned proteins: Presenilin-1, CAN, Nicastrin, PSL2, APH
Papers on SPPL3
Structure of the transmembrane domain of human nicastrin-a component of γ-secretase.
Kang et al., Singapore, Singapore. In Sci Rep, Dec 2015
Nicastrin is the largest component of γ-secretase that is an intramembrane protease important in the development of Alzheimer's disease.
Catalytic Properties of Intramembrane Aspartyl Protease Substrate Hydrolysis Evaluated Using a FRET Peptide Cleavage Assay.
Lieberman et al., Atlanta, United States. In Acs Chem Biol, Oct 2015
Our study demonstrates previously unappreciated similarities with soluble aspartyl proteases, provides new biochemical features of IAP and inhibitors, and offers tools to study other intramembrane protease family members in molecular detail.
An atomic structure of human γ-secretase.
Shi et al., Beijing, China. In Nature, Oct 2015
Dysfunction of the intramembrane protease γ-secretase is thought to cause Alzheimer's disease, with most mutations derived from Alzheimer's disease mapping to the catalytic subunit presenilin 1 (PS1).
Processing of CD74 by the Intramembrane Protease SPPL2a Is Critical for B Cell Receptor Signaling in Transitional B Cells.
Schröder et al., Kiel, Germany. In J Immunol, Sep 2015
We reported recently that clearance of the final membrane-bound N-terminal fragment (NTF) of CD74 is mediated by the intramembrane protease signal peptide peptidase-like (SPPL)2a, a process critical for B cell development.
Exome sequencing in a breast cancer family without BRCA mutation.
Huh et al., Seoul, South Korea. In Radiat Oncol J, Jun 2015
Using the Sorting Intolerant From Tolerant (SIFT), PolyPhen-2, and MutationTaster algorithms to predict amino acid substitutions, the XCR1, DLL1, TH, ACCS, SPPL3, CCNF, and SRL genes were risky among all three algorithms, while definite candidate genes could not be conclusively determined.
Structural basis of human γ-secretase assembly.
Shi et al., Beijing, China. In Proc Natl Acad Sci U S A, Jun 2015
The four-component intramembrane protease γ-secretase is intricately linked to the development of Alzheimer's disease.
γ-Secretase: a horseshoe structure brings good luck.
Selkoe et al., Boston, United States. In Cell, 2014
The intramembrane protease γ-secretase is a key player in signaling and Alzheimer's disease, but its structural features have remained obscure.
Mechanism of farnesylated CAAX protein processing by the intramembrane protease Rce1.
Barford et al., London, United Kingdom. In Nature, 2014
The major CAAX protease activity is mediated by Rce1 (Ras and a-factor converting enzyme 1), an intramembrane protease (IMP) of the endoplasmic reticulum.
Bioinformatics perspective on rhomboid intramembrane protease evolution and function.
Grishin et al., Dallas, United States. In Biochim Biophys Acta, 2013
Endopeptidase classification based on catalytic mechanism and evolutionary history has proven to be invaluable to the study of proteolytic enzymes.
Mechanism, specificity, and physiology of signal peptide peptidase (SPP) and SPP-like proteases.
Fluhrer et al., München, Germany. In Biochim Biophys Acta, 2013
Signal peptide peptidase (SPP) and the homologous SPP-like (SPPL) proteases SPPL2a, SPPL2b, SPPL2c and SPPL3 belong to the family of GxGD intramembrane proteases.
Structural and mechanistic principles of intramembrane proteolysis--lessons from rhomboids.
Strisovsky, Praha, Czech Republic. In Febs J, 2013
Despite the significant advances achieved so far, to obtain a detailed understanding of the mechanism of any intramembrane protease, high-resolution structural information on the substrate-enzyme complex is required.
Intramembrane cleavage of AMA1 triggers Toxoplasma to switch from an invasive to a replicative mode.
Soldati-Favre et al., Genève, Switzerland. In Science, 2011
Functional analysis of Toxoplasma rhomboid 4, a surface intramembrane protease, by conditional overexpression of a catalytically inactive form produced a profound block in replication.
Taking the plunge: integrating structural, enzymatic and computational insights into a unified model for membrane-immersed rhomboid proteolysis.
Urban, Baltimore, United States. In Biochem J, 2010
Although far from complete, studies with GlpG currently offer the best prospect for achieving a thorough and sophisticated understanding of a simplified intramembrane protease.
Signal peptide peptidases: a family of intramembrane-cleaving proteases that cleave type 2 transmembrane proteins.
Greenbaum et al., Jacksonville, United States. In Semin Cell Dev Biol, 2009
At least two of the human SPPs (SPP and SPPL3) appear to function without additional cofactors, but PSENs function as a protease, called gamma-secretase, only when complexed with Nicastrin, APH-1 and Pen-2.
Crystal structure of a rhomboid family intramembrane protease.
Ha et al., New Haven, United States. In Nature, 2006
Escherichia coli GlpG is an integral membrane protein that belongs to the widespread rhomboid protease family.
Intramembrane proteolytic cleavage by human signal peptide peptidase like 3 and malaria signal peptide peptidase.
Golde et al., Jacksonville, United States. In Faseb J, 2006
SPPL3 cleaves a SPP substrate, but a more distantly related homologue SPPL2b does not, providing strong evidence that the malaria SPP and human SPPL3 have conserved active sites, while the active sites SPPL2b is distinct
Differential localization and identification of a critical aspartate suggest non-redundant proteolytic functions of the presenilin homologues SPPL2b and SPPL3.
Haass et al., München, Germany. In J Biol Chem, 2005
SPPL2b is targeted through the secretory pathway to endosomes/lysosomes, whereas SPP and SPPL3 are restricted to the ER.
Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins.
Martoglio et al., Zürich, Switzerland. In J Biol Chem, 2005
SPP, SPPL2a, -2b, -2c, and -3 probably cleave type II-oriented substrate peptides as shown by consensus analysis
share on facebooktweetadd +1mail to friends