Homology of SMP domains to the TULIP superfamily of lipid-binding proteins provides a structural basis for lipid exchange between ER and mitochondria.
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PI(4,5)P(2)-dependent and Ca(2+)-regulated ER-PM interactions mediated by the extended synaptotagmins.Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transferStructure and Ca²⁺-binding properties of the tandem C₂ domains of E-Syt2Extended Synaptotagmin (ESyt) Triple Knock-Out Mice Are Viable and Fertile without Obvious Endoplasmic Reticulum DysfunctionPhospholipid transport via mitochondriaPower(2): the power of yeast genetics applied to the powerhouse of the cellThe conserved GTPase Gem1 regulates endoplasmic reticulum-mitochondria connectionsMcp3 is a novel mitochondrial outer membrane protein that follows a unique IMP-dependent biogenesis pathwayA conserved membrane-binding domain targets proteins to organelle contact sites.A new family of StART domain proteins at membrane contact sites has a role in ER-PM sterol transport.Role for two conserved intermembrane space proteins, Ups1p and Ups2p, [corrected] in intra-mitochondrial phospholipid trafficking.Cell wall integrity is linked to mitochondria and phospholipid homeostasis in Candida albicans through the activity of the post-transcriptional regulator Ccr4-Pop2.ER-mitochondrial junctions can be bypassed by dominant mutations in the endosomal protein Vps13.Mitochondrial lipids in neurodegenerationLipid transport by TMEM24 at ER-plasma membrane contacts regulates pulsatile insulin secretionSeparating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of Mdm10Analysis of mutations in Neurospora crassa ERMES components reveals specific functions related to β-barrel protein assembly and maintenance of mitochondrial morphology.Evolutionary relationships of microbial aromatic prenyltransferases.Eukaryote-wide sequence analysis of mitochondrial β-barrel outer membrane proteinsBridging the gap: membrane contact sites in signaling, metabolism, and organelle dynamics.Lipid transfer and signaling at organelle contact sites: the tip of the iceberg.Three-dimensional architecture of extended synaptotagmin-mediated endoplasmic reticulum-plasma membrane contact sites.Conserved SMP domains of the ERMES complex bind phospholipids and mediate tether assemblyGem1 and ERMES do not directly affect phosphatidylserine transport from ER to mitochondria or mitochondrial inheritanceExtended synaptotagmins are Ca2+-dependent lipid transfer proteins at membrane contact sites.Control of plasma membrane lipid homeostasis by the extended synaptotagminsEndoplasmic reticulum-mitochondria contacts: function of the junction.Hallmarks of a new era in mitochondrial biochemistry.An expanded family of proteins with BPI/LBP/PLUNC-like domains in trypanosome parasites: an association with pathogenicity?Bioinformatics of the TULIP domain superfamily.The ERMES complex and ER-mitochondria connections.Functional and morphological impact of ER stress on mitochondria.A close-up view of membrane contact sites between the endoplasmic reticulum and the endolysosomal system: from yeast to man.Role of membrane contact sites in protein import into mitochondria.SMP-domain proteins at membrane contact sites: Structure and functionMembrane Contact Sites: Complex Zones for Membrane Association and Lipid Exchange.Advances on the Transfer of Lipids by Lipid Transfer ProteinsHomeostatic regulation of the PI(4,5)P2-Ca(2+) signaling system at ER-PM junctions.Crystal structure of Mdm12 and combinatorial reconstitution of Mdm12/Mmm1 ERMES complexes for structural studies.ER fatalities-The role of ER-mitochondrial contact sites in yeast life and death decisions.
P2860
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P2860
Homology of SMP domains to the TULIP superfamily of lipid-binding proteins provides a structural basis for lipid exchange between ER and mitochondria.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Homology of SMP domains to the ...... e between ER and mitochondria.
@en
Homology of SMP domains to the ...... e between ER and mitochondria.
@nl
type
label
Homology of SMP domains to the ...... e between ER and mitochondria.
@en
Homology of SMP domains to the ...... e between ER and mitochondria.
@nl
prefLabel
Homology of SMP domains to the ...... e between ER and mitochondria.
@en
Homology of SMP domains to the ...... e between ER and mitochondria.
@nl
P2860
P356
P1433
P1476
Homology of SMP domains to the ...... e between ER and mitochondria.
@en
P2093
Klaus O Kopec
P2860
P304
P356
10.1093/BIOINFORMATICS/BTQ326
P407
P577
2010-06-16T00:00:00Z