Role of the intermembrane-space domain of the preprotein receptor Tom22 in protein import into mitochondria.
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Identification and functional analysis of human Tom22 for protein import into mitochondriaThe Tim21 binding domain connects the preprotein translocases of both mitochondrial membranes.The role of Djp1 in import of the mitochondrial protein Mim1 demonstrates specificity between a cochaperone and its substrate protein.Preprotein translocase of the outer mitochondrial membrane: molecular dissection and assembly of the general import pore complex.The presequence pathway is involved in protein sorting to the mitochondrial outer membrane.Targeting of tail-anchored proteins to yeast mitochondria in vivo.Targeting and insertion of nuclear-encoded preproteins into the mitochondrial outer membrane.Interaction of mitochondrial targeting signals with acidic receptor domains along the protein import pathway: evidence for the 'acid chain' hypothesis.Identification of mammalian TOM22 as a subunit of the preprotein translocase of the mitochondrial outer membrane.Dual role of the receptor Tom20 in specificity and efficiency of protein import into mitochondria.Genetic analysis of the Drosophila 63F early puff. Characterization of mutations in E63-1 and maggie, a putative Tom22.Inner mitochondrial translocase Tim50 interacts with 3β-hydroxysteroid dehydrogenase type 2 to regulate adrenal and gonadal steroidogenesisSam37 is crucial for formation of the mitochondrial TOM-SAM supercomplex, thereby promoting β-barrel biogenesis.Uncoupling of transfer of the presequence and unfolding of the mature domain in precursor translocation across the mitochondrial outer membrane.Mitochondrial protein import and human health and disease.An Outer Mitochondrial Translocase, Tom22, Is Crucial for Inner Mitochondrial Steroidogenic Regulation in Adrenal and Gonadal Tissues.Role of membrane contact sites in protein import into mitochondria.Role of the negative charges in the cytosolic domain of TOM22 in the import of precursor proteins into mitochondria.Mitochondrial translocation contact sites: separation of dynamic and stabilizing elements in formation of a TOM-TIM-preprotein supercomplexThe intermembrane space domain of mitochondrial Tom22 functions as a trans binding site for preproteins with N-terminal targeting sequences.Functions of the small proteins in the TOM complex of Neurospora crasssaBiogenesis of Tom40, core component of the TOM complex of mitochondria.Biogenesis of Tim23 and Tim17, integral components of the TIM machinery for matrix-targeted preproteinsThe TOM core complex: the general protein import pore of the outer membrane of mitochondria.Mitochondrial inner-membrane protease Yme1 degrades outer-membrane proteins Tom22 and Om45.Targeting and assembly of rat mitochondrial translocase of outer membrane 22 (TOM22) into the TOM complex.Assembly of Tom6 and Tom7 into the TOM core complex of Neurospora crassa.An Import Signal in the Cytosolic Domain of theNeurosporaMitochondrial Outer Membrane Protein TOM22The Isolated Complex of the Translocase of the Outer Membrane of Mitochondria
P2860
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P2860
Role of the intermembrane-space domain of the preprotein receptor Tom22 in protein import into mitochondria.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
Role of the intermembrane-spac ...... tein import into mitochondria.
@en
type
label
Role of the intermembrane-spac ...... tein import into mitochondria.
@en
prefLabel
Role of the intermembrane-spac ...... tein import into mitochondria.
@en
P2093
P2860
P356
P1476
Role of the intermembrane-spac ...... tein import into mitochondria.
@en
P2093
P2860
P304
P356
10.1128/MCB.16.8.4035
P407
P577
1996-08-01T00:00:00Z