about
Guidelines for the use and interpretation of assays for monitoring autophagyNix, a receptor protein for mitophagy in mammalsArchitectural role of mitochondrial transcription factor A in maintenance of human mitochondrial DNACasein kinase 2 is essential for mitophagy.Atg32 is a mitochondrial protein that confers selectivity during mitophagyA genomic screen for yeast mutants defective in selective mitochondria autophagy.Protein instability and functional defects caused by mutations of dihydro-orotate dehydrogenase in Miller syndrome patientsp32/gC1qR is indispensable for fetal development and mitochondrial translation: importance of its RNA-binding abilityA genomic screen for yeast mutants defective in mitophagy.Monitoring mitophagy in yeast: the Om45-GFP processing assayMitochondria autophagy in yeast.Mitophagy in yeast occurs through a selective mechanismHuman mitochondrial DNA is packaged with TFAM.Leigh syndrome with nephropathy and CoQ10 deficiency due to decaprenyl diphosphate synthase subunit 2 (PDSS2) mutationsMitophagy is primarily due to alternative autophagy and requires the MAPK1 and MAPK14 signaling pathways.The molecular mechanism of mitochondria autophagy in yeast.Mitochondrial division occurs concurrently with autophagosome formation but independently of Drp1 during mitophagy.Phosphorylation of Serine 114 on Atg32 mediates mitophagy.Mitophagy in yeast: Molecular mechanisms and physiological role.Mitophagy in Yeast: A Screen of Mitophagy-Deficient Mutants.Mitochondrial abnormalities drive cell death in Wolfram syndrome 2.Mitophagy plays an essential role in reducing mitochondrial production of reactive oxygen species and mutation of mitochondrial DNA by maintaining mitochondrial quantity and quality in yeast.Constitutive Activation of PINK1 Protein Leads to Proteasome-mediated and Non-apoptotic Cell Death Independently of Mitochondrial Autophagy.The physiological role of mitophagy: new insights into phosphorylation events.The tenth membrane region of band 3 is initially exposed to the luminal side of the endoplasmic reticulum and then integrated into a partially folded band 3 intermediate.Effects of overexpression of mitochondrial transcription factor A on lifespan and oxidative stress response in Drosophila melanogaster.Assays for autophagy II: Mitochondrial autophagy.Mutation and functional analysis of ABCC2/multidrug resistance protein 2 in a Japanese patient with Dubin-Johnson syndrome.Mitochondrial nucleoid and transcription factor A.The N-terminal region of the transmembrane domain of human erythrocyte band 3. Residues critical for membrane insertion and transport activity.Reverse of age-dependent memory impairment and mitochondrial DNA damage in microglia by an overexpression of human mitochondrial transcription factor a in mice.How autophagy eats large mitochondria: Autophagosome formation coupled with mitochondrial fragmentation.PP2A-like protein phosphatase Ppg1: an emerging negative regulator of mitophagy in yeastDetection of Hypoxia-Induced and Iron Depletion-Induced Mitophagy in Mammalian CellsLocalization of mRNAs encoding human mitochondrial oxidative phosphorylation proteinsRibonucleoprotein Y-box-binding protein-1 regulates mitochondrial oxidative phosphorylation (OXPHOS) protein expression after serum stimulation through binding to OXPHOS mRNA[Mitophagy: selective degradation of mitochondria by autophagy]Atg32 Is a tag for mitochondria degradation in yeast[Molecular mechanism of mitochondria autophagy]The C-terminal Tail of Mitochondrial Transcription Factor A Markedly Strengthens its General Binding to DNA
P50
Q21996341-B90D5CBC-6D7B-450E-86B5-A6079F180718Q24301612-F0721307-72D3-4987-819C-16C87804D11CQ24561728-325DF320-DE31-44E8-A8CF-948811B40CB4Q27934580-9EE06C73-12D1-40DF-95D1-55C8AB82C192Q27936726-4734E70C-D39F-4EF1-AF32-DFB7E8ED5727Q27938385-6FBD3733-62CC-45A8-84F6-84ED6CEEE3C4Q28274852-F297D4DF-3E42-4AE3-9F9D-555DA64ACFD1Q28587023-99D26035-BB40-43D6-8001-BC0FAABA0AB7Q33549146-F2EFCC85-F65A-4F11-A280-F5EBA886AE2BQ33771828-56A66C5B-1038-4447-A0AB-17F3D5F1E7C6Q34805874-8C1F5E9E-857E-4D0D-B7B0-002D0A613C05Q34837659-D4FDFCC9-3D4C-4956-8E78-101F63E38C8EQ34908739-BC67F100-0E03-4609-B636-ED8017AFE8ECQ35221744-EBBEBB6C-4EAC-4C58-8507-45D847737175Q35852737-5EB162D5-751E-49F2-A12E-988A9C05224BQ36773264-CC286E50-D9F4-456D-BA74-BF41781EE86BQ37488331-3FFD3541-7A99-4ED2-AE6A-85AB59192073Q38274635-2931B3D7-ECDE-4888-846F-5DE26CAB45F5Q38325180-8B0566B2-890B-40D0-8936-807E0792EAEDQ38889645-6A2608B8-21C1-4E3A-802A-A12924ADC382Q39427543-0F00FAA9-3E17-4D66-8A53-D8601E10C36DQ40810283-F4871F0A-50DB-4270-96CD-7D4F0AF45C49Q42084360-561E136C-48B9-4E19-9FAF-A43A91C863B9Q42182324-7ECEFEAF-2865-4320-9B35-0C08E58E8D70Q44220119-F5009B3A-EEB9-4EFC-8DF5-8EB999A73479Q44793249-0A4F00CE-33A6-4B67-8FB6-1A7B29BF91A9Q45775752-5BD37A24-0515-46A3-B92A-37FF0043A1D0Q45932997-A2F651D9-D94C-4F50-8446-BF91F38D46C5Q47652488-C7FF0736-BA5F-4C5A-BB4B-A0A32CDA97A8Q48842337-E1E28369-C692-46AC-91FD-5A6ADA8A7F39Q48959209-3FB4DEE3-B2AF-4863-9FB2-907BEC3BE266Q50637676-764ABF67-303D-4B55-900C-97D9328045E0Q57649428-500BEDFF-189D-45B6-8A44-A77095725EE4Q57649433-5894161E-47E0-442F-A13F-0D80CC7BFD79Q57649469-4CB3AF10-CF12-41E7-A069-22833399C414Q57649480-57D1A751-25C8-4B72-A0EC-21F8F8C8ED8DQ57649492-39489E44-F772-49A4-9D8F-D6349AFB1B0AQ57649513-9FB3721D-0547-4432-9BFE-B9C51189D7A7Q57649522-09BA3DB1-CCF6-4F8C-9780-ACA8008D7CD9Q57649545-F2CEE0EF-8506-497D-97A7-5DB0F7C9FE71
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Tomotake Kanki
@ast
Tomotake Kanki
@en
Tomotake Kanki
@es
Tomotake Kanki
@nl
Tomotake Kanki
@sl
type
label
Tomotake Kanki
@ast
Tomotake Kanki
@en
Tomotake Kanki
@es
Tomotake Kanki
@nl
Tomotake Kanki
@sl
prefLabel
Tomotake Kanki
@ast
Tomotake Kanki
@en
Tomotake Kanki
@es
Tomotake Kanki
@nl
Tomotake Kanki
@sl
P1053
H-7250-2012
P106
P31
P3829
P496
0000-0001-9646-5379
P569
2000-01-01T00:00:00Z