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Guidelines for the use and interpretation of assays for monitoring autophagyGuidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)Membrane morphology is actively transformed by covalent binding of the protein Atg8 to PE-lipidsStructural basis of target recognition by Atg8/LC3 during selective autophagyThe NMR structure of the autophagy-related protein Atg8Structural basis of Atg8 activation by a homodimeric E1, Atg7Autophagy-related Protein 32 Acts as Autophagic Degron and Directly Initiates MitophagyAtg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion.Receptor-mediated selective autophagy degrades the endoplasmic reticulum and the nucleus.The autophagy-related protein kinase Atg1 interacts with the ubiquitin-like protein Atg8 via the Atg8 family interacting motif to facilitate autophagosome formationAtg12-Atg5 conjugate enhances E2 activity of Atg3 by rearranging its catalytic site.Hrr25 phosphorylates the autophagic receptor Atg34 to promote vacuolar transport of α-mannosidase under nitrogen starvation conditions.Hrr25 triggers selective autophagy-related pathways by phosphorylating receptor proteins.Reticulophagy and nucleophagy: New findings and unsolved issuesDynamics and diversity in autophagy mechanisms: lessons from yeastSecretion monitor, SecM, undergoes self-translation arrest in the cytosol.SecM facilitates translocase function of SecA by localizing its biosynthesis[Characterization of yeast Atg proteins].The ribosomal exit tunnel functions as a discriminating gate.Intraribosomal regulation of expression and fate of proteins.Control of SecA and SecM translation by protein secretion.Recruitment of the autophagic machinery to endosomes during infection is mediated by ubiquitin.Translation arrest of SecM is essential for the basal and regulated expression of SecA.Two ubiquitin-like conjugation systems that mediate membrane formation during autophagy.Hrr25: an emerging major player in selective autophagy regulation in Saccharomyces cerevisiae.Localization of Atg3 to autophagy-related membranes and its enhancement by the Atg8-family interacting motif to promote expansion of the membranes.Eating the ER and the nucleus for survival under starvation conditions.Phospholipid methylation controls Atg32-mediated mitophagy and Atg8 recyclingAutophagy-related protein 8 (Atg8) family interacting motif in Atg3 mediates the Atg3-Atg8 interaction and is crucial for the cytoplasm-to-vacuole targeting pathway.[Molecular mechanisms of autophagy in yeast].Appetite for ER/nucleus destruction.Dimeric coiled-coil structure of Saccharomyces cerevisiae Atg16 and its functional significance in autophagy.Lipidation of Atg8: how is substrate specificity determined without a canonical E3 enzyme?Physiological pH and acidic phospholipids contribute to substrate specificity in lipidation of Atg8.[The functions of the ribosomal tunnel in a birth of proteins].[Mechanisms of membrane biogenesis in autophagy].Regulated degradation: controlling the stability of autophagy gene transcripts.Genetically encoded but nonpolypeptide prolyl-tRNA functions in the A site for SecM-mediated ribosomal stall.Atg4 recycles inappropriately lipidated Atg8 to promote autophagosome biogenesisNoncanonical recognition and UBL loading of distinct E2s by autophagy-essential Atg7
P50
Q21996341-571066B3-5E99-412D-B5BA-809A851340E2Q22676705-2A1C5842-83C7-429B-A8CD-76B0CB640558Q27319983-8C9016AE-77E2-45BB-9588-4F3CF831E6E8Q27652961-F8CDBC0B-CA5E-403E-94FE-8B29B906044BQ27661012-37CBA0BF-D48D-4FB5-9394-2E7B5D542D51Q27675401-E2347FF7-16EA-4BBF-B75A-9F3EA42AAB0FQ27677082-2E3A1075-55F7-447E-87C9-AAE4191134A2Q27933991-CFDF88DD-6094-4516-AC3D-DBC1D795F633Q27934756-D365DFED-3CA2-48FB-B974-2088EF9A7CF2Q27936592-CD4DC8EF-670E-44A5-99D7-A639F69BF0A5Q27937261-F2091212-CB20-4C50-AF73-A75A5527784AQ27938922-BD3205E0-0A0A-43BF-A12F-CCF2922E60D0Q27939298-83B49A9D-E879-45C0-9406-388C9C5E2C63Q28084991-AB9D601A-A63F-47A2-953E-AC300B25FD77Q29620685-D78E0A0D-7965-441C-96A5-FC2F75AD42E9Q31923120-99AD4FAD-2449-4C25-B552-E6615FBCC8C8Q33848928-F01F882D-D005-46A8-82B9-4B2BBF27C639Q33998744-D670C195-1821-41A0-B45E-595173CF831DQ34118341-290D348A-6D91-4735-8451-5D63D55BDB68Q35616327-D7FCF12E-0759-4C02-8058-595DE42958D4Q35737959-50426472-6B09-469A-A7F5-4A14F9DB0936Q37233581-E4470FBC-962F-4DBE-B1CB-77998C406E1EQ37483786-03E6790A-F9FE-46DE-B505-E5F1C7F11CC4Q38144273-960E2E3A-51CC-4A8B-8470-48622CF6C69EQ41616963-FC1B42D5-B3B5-4600-8E6F-4086B277EB24Q41792152-F6EBF5E8-01F3-41F9-8DB5-29D588B57CA6Q41845188-9EC2C145-4A43-43D2-B75C-D21CA24D1E52Q41937023-9C391BE2-EC26-4FEB-AAD7-D9D721CC9B88Q41979115-976DC700-9BD0-4BC9-88E5-30B85EDF52B8Q42840861-B84EC187-0D22-4B5D-A614-3B34EEA33615Q42910509-425E7D51-9F7B-4F8A-9EA3-2A17A9402B90Q42943842-6AC4EAA4-A1F5-4D61-9329-6977F026D61DQ46438656-38FB7862-2858-47E2-A310-D1842594EACCQ46547418-8E64B208-1F5A-4098-B18E-2677D558B1AAQ49224486-6F223BCB-A289-4552-80C5-A9B005B45A4CQ53509680-44E14281-77B1-480A-BABB-BF9D7B0014E0Q54256394-1F7C37D5-B046-48C5-9BFF-3ABA1F762359Q54465004-EF7BCCB8-6BCE-4BE8-8F12-2E86313104B7Q54917760-98817A76-E7AA-45C1-B412-637191CF7C41Q54917765-10B71FB9-9BE8-4AF8-BF24-25A94F3B113D
P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Hitoshi Nakatogawa
@ast
Hitoshi Nakatogawa
@en
Hitoshi Nakatogawa
@es
Hitoshi Nakatogawa
@nl
Hitoshi Nakatogawa
@sl
type
label
Hitoshi Nakatogawa
@ast
Hitoshi Nakatogawa
@en
Hitoshi Nakatogawa
@es
Hitoshi Nakatogawa
@nl
Hitoshi Nakatogawa
@sl
prefLabel
Hitoshi Nakatogawa
@ast
Hitoshi Nakatogawa
@en
Hitoshi Nakatogawa
@es
Hitoshi Nakatogawa
@nl
Hitoshi Nakatogawa
@sl
P1053
D-5155-2015
P106
P21
P31
P3829
P496
0000-0002-5828-0741
P569
2000-01-01T00:00:00Z