Import and insertion of proteins into the mitochondrial outer membrane.
about
Recruitment of an alternatively spliced form of synaptojanin 2 to mitochondria by the interaction with the PDZ domain of a mitochondrial outer membrane protein.Mitochondrial fusion in human cells is efficient, requires the inner membrane potential, and is mediated by mitofusins.An unexpected localization of basonuclin in the centrosome, mitochondria, and acrosome of developing spermatidsBiogenesis of the mitochondrial TOM complex: Mim1 promotes insertion and assembly of signal-anchored receptors.Interactions of the human mitochondrial protein import receptor, hTom20, with precursor proteins in vitro reveal pleiotropic specificities and different receptor domain requirementsBax-induced cytochrome c release from mitochondria depends on alpha-helices-5 and -6The N-terminal domain of rat liver carnitine palmitoyltransferase 1 contains an internal mitochondrial import signal and residues essential for folding of its C-terminal catalytic domainThe Neurospora crassa TOB complex: analysis of the topology and function of Tob38 and Tob37Signal-anchored proteins follow a unique insertion pathway into the outer membrane of mitochondria.Plectin isoform 1b mediates mitochondrion-intermediate filament network linkage and controls organelle shape.Localization of the Carnation Italian ringspot virus replication protein p36 to the mitochondrial outer membrane is mediated by an internal targeting signal and the TOM complex.Targeting and insertion of nuclear-encoded preproteins into the mitochondrial outer membrane.Membrane association of greasy grouper nervous necrosis virus protein A and characterization of its mitochondrial localization targeting signalMitochondrial targeting and membrane anchoring of a viral replicase in plant and yeast cells.Localization of a peripheral membrane protein: Gbetagamma targets Galpha(Z).Finding the right organelle. Targeting signals in mitochondrial outer-membrane proteins.Viral product trafficking to mitochondria, mechanisms and roles in pathogenesis.An internal targeting signal directing proteins into the mitochondrial intermembrane spaceThe human mitochondrial import receptor, hTom20p, prevents a cryptic matrix targeting sequence from gaining access to the protein translocation machinery.Regulation of chloroplast protein import through a protochlorophyllide-responsive transit peptide.Role of the intermembrane-space domain of the preprotein receptor Tom22 in protein import into mitochondria.The N-terminal end of Bax contains a mitochondrial-targeting signal.Structural requirements of Tom40 for assembly into preexisting TOM complexes of mitochondriaDistribution and apoptotic function of outer membrane proteins depend on mitochondrial fusion.The mitochondrial amidoxime-reducing component (mARC1) is a novel signal-anchored protein of the outer mitochondrial membrane.Characterization of signal that directs C-tail-anchored proteins to mammalian mitochondrial outer membraneThe hypoxia-induced dehydrogenase HorA is required for coenzyme Q10 biosynthesis, azole sensitivity and virulence of Aspergillus fumigatus.Effects of carboxyl-terminal truncations on the activity and solubility of human monoamine oxidase B.A role for N-myristoylation in protein targeting: NADH-cytochrome b5 reductase requires myristic acid for association with outer mitochondrial but not ER membranes.Protein targeting and translocation; a comparative survey.Insertion of the 70-kDa peroxisomal membrane protein into peroxisomal membranes in vivo and in vitro.The luminal N-terminus of yeast Nvj1 is an inner nuclear membrane anchor.N-myristoylation determines dual targeting of mammalian NADH-cytochrome b5 reductase to ER and mitochondrial outer membranes by a mechanism of kinetic partitioningBiogenesis of Tom40, core component of the TOM complex of mitochondria.Characterization of the signal that directs Tom20 to the mitochondrial outer membrane.Targeting and assembly of mitochondrial tail-anchored protein Tom5 to the TOM complex depend on a signal distinct from that of tail-anchored proteins dispersed in the membrane.The most C-terminal tri-glycine segment within the polyglycine stretch of the pea Toc75 transit peptide plays a critical role for targeting the protein to the chloroplast outer envelope membrane.Targeting and assembly of rat mitochondrial translocase of outer membrane 22 (TOM22) into the TOM complex.Biogenesis of a Mitochondrial Outer Membrane Protein in Trypanosoma brucei: TARGETING SIGNAL AND DEPENDENCE ON A UNIQUE BIOGENESIS FACTOR.Heterotrimer formation, together with isoprenylation, is required for plasma membrane targeting of Gbetagamma.
P2860
Q24534146-B61CCDBA-3F6D-45EA-8790-E37001EF16E3Q24541558-0B501234-C6BC-4588-AB1B-D98B198AE8D6Q24678556-A9666BFC-F950-4DC7-BCF3-A9A45BD3634EQ27937853-E2231C46-02D1-4D35-9C44-887B27D94ECCQ28242996-237F6BD8-DF6B-4D21-898A-BADD03F2B428Q28509283-233C66E4-955C-45AE-8442-D827D20EA48DQ28567275-C512540C-B239-4277-9364-02EE46730E9CQ30155458-92C78DF9-6111-4B6E-9ECA-D02449836674Q30160816-14AB13C4-AB2A-482C-A736-CDD390EF6568Q30482303-B3476DE4-A629-49FC-BA8C-1AF933571DE0Q33371376-4E4E88BA-1B63-4306-AD38-0849A7AD580FQ33866727-77B625D9-944D-4BAF-A85C-F64DD88E904DQ34192684-BCFD59FF-5140-4AD1-94AC-FC84A261C358Q34348543-99EF9AB5-B824-41E7-88A9-094C177EBF02Q35004171-06502CC1-C449-4E59-8029-F3669933D91CQ35551096-51D08825-D049-43EA-ABE1-CD34744766FFQ35619821-9D12007F-F67B-4842-A64F-A30310766A73Q35708721-AC89C564-11C8-4810-8A45-6BD7238C9186Q36237000-9C352463-FD6D-4F02-B3C7-03D59232E228Q36565768-5A34C49E-5831-421E-B74B-EBEA377FB338Q38354888-D57F23DF-C385-4E92-9153-C04493AAE50CQ38358682-297DDAA2-7B16-4813-AD60-FD68BC4CB3F4Q38720218-709539DC-83FA-413F-8B1C-B22B05C6614BQ38996618-BC658CD9-B5E3-4AF6-BACE-D6AC3EB519D2Q39255375-05FE36A9-C3E2-4C4C-AF9A-C1EB1D522FF7Q39586462-D9498CE4-D623-4671-A405-FF38228B657CQ40749853-6899C206-8290-42FB-9B09-547E528A732CQ40803629-58A49C03-2E0F-40DB-BBEF-D11B16F99B54Q41147696-782339AE-0B74-423D-A029-8232F6019B87Q41220629-92E2EABB-1B72-4F2B-ACF7-3CC26D9F8123Q41227531-A8B9C162-0052-43BB-9AAB-FDC71F710FD3Q41622389-F16C6311-1167-4E7C-9A23-4D566102F43EQ41847788-1D2A9DDE-D2B0-4341-8E14-61496157E0AAQ42058401-6FE05E4E-A8F1-4FAB-8277-EE547B0CE2D0Q42943589-FF1A1E76-827D-4FB5-8CD1-D2970D11B9C8Q44535709-B1E81E3C-B10F-4282-BC9D-25BAC336B68CQ46159899-F35016F0-09C1-4867-A957-1FE9F051F322Q48034397-44F4F10F-8AB1-4B15-A1F2-67224580BEF3Q51182729-8AAD8069-7C28-43BE-94FD-11FA1A19F5CCQ52549569-81EBEE6A-9E91-46D7-95B3-325DAAF93B79
P2860
Import and insertion of proteins into the mitochondrial outer membrane.
description
1995 nî lūn-bûn
@nan
1995 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Import and insertion of proteins into the mitochondrial outer membrane.
@ast
Import and insertion of proteins into the mitochondrial outer membrane.
@en
type
label
Import and insertion of proteins into the mitochondrial outer membrane.
@ast
Import and insertion of proteins into the mitochondrial outer membrane.
@en
prefLabel
Import and insertion of proteins into the mitochondrial outer membrane.
@ast
Import and insertion of proteins into the mitochondrial outer membrane.
@en
P2093
P2860
P1433
P1476
Import and insertion of proteins into the mitochondrial outer membrane
@en
P2093
D G Millar
N A Steenaart
P2860
P356
10.1111/J.1432-1033.1995.TB20354.X
P407
P577
1995-01-01T00:00:00Z