about
Levels of human Fis1 at the mitochondrial outer membrane regulate mitochondrial morphologyAdaptor proteins MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 recruitment and are specific for mitochondrial fission.Dissection of the mitochondrial import and assembly pathway for human Tom40The morphology proteins Mdm12/Mmm1 function in the major beta-barrel assembly pathway of mitochondria.Alternative function for the mitochondrial SAM complex in biogenesis of alpha-helical TOM proteinsBiogenesis of the mitochondrial TOM complex: Mim1 promotes insertion and assembly of signal-anchored receptors.Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase.Tim29 is a novel subunit of the human TIM22 translocase and is involved in complex assembly and stabilitySorting and assembly of mitochondrial outer membrane proteins.Inhibition of Bak activation by VDAC2 is dependent on the Bak transmembrane anchorImport of nuclear-encoded proteins into mitochondria.Mitochondrial morphology and protein import--a tight connection?Mitochondrial morphology and distribution in mammalian cells.Import of proteins into mitochondria.Diverse mechanisms and machineries for import of mitochondrial proteins.Mitochondrial protein import: precursor oxidation in a ternary complex with disulfide carrier and sulfhydryl oxidaseThe MIA system for protein import into the mitochondrial intermembrane space.Mitochondrial protein quality control in health and disease.Mitochondrial protein import machineries and lipids: a functional connection.The regulation of mitochondrial morphology: intricate mechanisms and dynamic machinery.The MIA pathway: a tight bond between protein transport and oxidative folding in mitochondria.Mechanisms of protein sorting in mitochondriaMitochondrial protein homeostasis.A Farnesylated Coxiella burnetii Effector Forms a Multimeric Complex at the Mitochondrial Outer Membrane during Infection.Cooperative and independent roles of the Drp1 adaptors Mff, MiD49 and MiD51 in mitochondrial fission.Stress-induced OMA1 activation and autocatalytic turnover regulate OPA1-dependent mitochondrial dynamics.Rotavirus NSP6 localizes to mitochondria via a predicted N-terminal a-helix.Targeting mitochondria: how intravacuolar bacterial pathogens manipulate mitochondria.Sengers Syndrome-Associated Mitochondrial Acylglycerol Kinase Is a Subunit of the Human TIM22 Protein Import Complex.Identification of the signal directing Tim9 and Tim10 into the intermembrane space of mitochondria.Mitofusins 'bridge' the gap between oxidative stress and mitochondrial hyperfusionHuntingtin Inclusions Trigger Cellular Quiescence, Deactivate Apoptosis, and Lead to Delayed Necrosis.Mitochondrial protein transport in health and disease.Regulation of mitochondrial protein import by cytosolic kinases.Mitochondrial diseases caused by dysfunctional mitochondrial protein importResponse: The Mitochondrial β-Signal and Protein SortingImpaired Folding of the Mitochondrial Small TIM Chaperones Induces Clearance by the i-AAA ProteaseDissecting membrane insertion of mitochondrial beta-barrel proteinsFunction of hTim8a in complex IV assembly in neuronal cells provides insight into pathomechanism underlying Mohr-Tranebjærg syndromeCorrection: Function of hTim8a in complex IV assembly in neuronal cells provides insight into pathomechanism underlying Mohr-Tranebjærg syndrome
P50
Q24313537-F224BECD-36C5-4025-B4B2-28202BA7ACD4Q24315659-54234CED-8093-4E77-BE49-28173F1F37A9Q24337791-C6EC105A-8630-4DDC-AF70-EE08F3E92CE4Q27931645-4CD8386B-DBBB-4CE5-9E13-3D3FEF161FB4Q27936064-BCC94733-5E86-4A8D-9BB9-C48EC1E48270Q27937853-8EC6DF94-9DAE-4FD0-96EC-A8F35CA126D3Q27938484-899EF4BA-50A2-4F84-9FB1-F2FE2D49F058Q28116190-C4E7ADAD-858A-46C1-A8D7-D9998688C5DEQ30157696-20DB96BD-6A5E-41B3-9C37-90409B88E1A3Q34299265-5DF299DD-876F-46F6-B96B-F536456A5E5AQ35044276-69386A7C-BCEE-4D0E-96AC-55FC4BFE9EAFQ36453558-5144BD1C-B601-4613-AE2D-B6E0533A6C6DQ36666946-0011EF6D-A125-4371-8A5A-C6C4EF0C29CCQ36796315-94B4DEAC-5AE4-44BD-92DA-3737EF47EA69Q36909225-A95B5203-73CB-4748-B62E-64183B155E7CQ36938873-C68442EB-9482-4AA6-95DA-467572546FE6Q36998389-87425ED7-E5AA-4E3C-9B47-9D7F75FB4AC9Q37686252-73205B4D-E4C0-4FE4-8D76-391A44535CF6Q37778874-814A4946-C372-486B-98C4-B1FE00394DA0Q37891347-4B25A2DF-A015-4002-92DE-91E33ADF5F4EQ38009539-DBF13394-49A6-488D-BA3F-AE4F6457B59CQ38048758-E8A2726D-F89F-46EE-8ED9-A2010B48E9FAQ38076092-1979BFBF-7543-47CE-8BFA-50FD22DBA1AEQ38714587-408A434E-DA38-410E-992C-C6FF7929C1A0Q38778376-22F780AE-39DA-478A-8588-49F66B36A5DDQ38798007-2A302FDC-22E3-4A83-BA1C-A3CAE4FC8660Q38832710-C67255B8-A65E-4358-836A-587265757AFAQ38925272-8F44F18C-B725-40B8-B8F1-1440D122D560Q41412885-CDEA31D1-B0FF-4646-87FF-18811B8931BFQ41838204-E11884CF-3CAA-4D44-A1DE-25F09F709EC2Q42530340-959CBA77-1B27-4C35-A013-A138C73969CCQ46372498-BEABCA2A-B498-4AC5-A2D1-0D7577EF4C88Q47814765-F9C61200-98F4-4100-A8A6-51480B33DCFBQ54621528-E6D7B32D-2FD7-4597-B1E9-4CB477493ABFQ57033836-C17B2025-5E0A-4ED7-AD2D-D692BDC77979Q57091896-425122F5-6170-4854-9F75-3A04A83BEA55Q57092419-4774355A-98FB-492A-BCEB-AB42288EE34CQ57752470-BDFA6382-F5EC-4243-BF83-4FDAE9FD4D9DQ83227286-050A6A83-CF44-4442-A587-7B2C593FE9C9Q90422689-02D3D063-2919-41BD-B702-2D20C5592A86
P50
description
hulumtuese
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Diana Stojanovski
@ast
Diana Stojanovski
@en
Diana Stojanovski
@es
Diana Stojanovski
@fr
Diana Stojanovski
@nl
Diana Stojanovski
@sl
type
label
Diana Stojanovski
@ast
Diana Stojanovski
@en
Diana Stojanovski
@es
Diana Stojanovski
@fr
Diana Stojanovski
@nl
Diana Stojanovski
@sl
prefLabel
Diana Stojanovski
@ast
Diana Stojanovski
@en
Diana Stojanovski
@es
Diana Stojanovski
@fr
Diana Stojanovski
@nl
Diana Stojanovski
@sl
P106
P1153
36509569200
P21
P31
P496
0000-0002-0199-3222
P569
2000-01-01T00:00:00Z