about
Crystal structure of a protein with an artificial exon-shuffling, module M4-substituted chimera hemoglobin beta alpha, at 2.5 A resolutionDynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbBRedox-dependent domain rearrangement of protein disulfide isomerase coupled with exposure of its substrate-binding hydrophobic surfaceCrystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDIRadically different thioredoxin domain arrangement of ERp46, an efficient disulfide bond introducer of the mammalian PDI familyCritical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB.Progressive quality control of secretory proteins in the early secretory compartment by ERp44The α-proteobacteria Wolbachia pipientis protein disulfide machinery has a regulatory mechanism absent in γ-proteobacteria.Structural basis of a Ni acquisition cycle for [NiFe] hydrogenase by Ni-metallochaperone HypA and its enhancer.Cysteines 208 and 241 in Ero1α are required for maximal catalytic turnoverStructure and mechanisms of the DsbB-DsbA disulfide bond generation machine.Redox-assisted regulation of Ca2+ homeostasis in the endoplasmic reticulum by disulfide reductase ERdj5.Disulfide bond formation system in Escherichia coli.Structural basis of protein disulfide bond generation in the cell.Structure, mechanism, and evolution of Ero1 family enzymes.Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals.Structures and functions of protein disulfide isomerase family members involved in proteostasis in the endoplasmic reticulum.The membrane topology of vitamin K epoxide reductase is conserved between human isoforms and the bacterial enzyme.Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade.A pair of circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of Escherichia coli.A pH-regulated quality control cycle for surveillance of secretory protein assembly.A PDI-catalyzed thiol-disulfide switch regulates the production of hydrogen peroxide by human Ero1.Homodimerization of Nemo-like kinase is essential for activation and nuclear localizationMolecular bases of cyclic and specific disulfide interchange between human ERO1alpha protein and protein-disulfide isomerase (PDI).Cell biology of cysteine-based molecular switchesStructural basis of pH-dependent client binding by ERp44, a key regulator of protein secretion at the ER-Golgi interface.Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics.Inhibition of the functional interplay between endoplasmic reticulum (ER) oxidoreduclin-1α (Ero1α) and protein-disulfide isomerase (PDI) by the endocrine disruptor bisphenol A.Human ER Oxidoreductin-1α (Ero1α) Undergoes Dual Regulation through Complementary Redox Interactions with Protein-Disulfide Isomerase.DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation.Characterization of the menaquinone-dependent disulfide bond formation pathway of Escherichia coli.Preparation of Selenoinsulin as a Long-Lasting Insulin Analogue.The Highly Dynamic Nature of ERdj5 Is Key to Efficient Elimination of Aberrant Protein Oligomers through ER-Associated Degradation.One-Dimensional Sliding of p53 Along DNA Is Accelerated in the Presence of Ca(2+) or Mg(2+) at Millimolar Concentrations.Role of the cytosolic loop of DsbB in catalytic turnover of the ubiquinone-DsbB complex.Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation.Identification of the physiological substrates of PDIp, a pancreas-specific protein disulfide isomerase family memberMethods to identify the substrates of thiol-disulfide oxidoreductasesEro1-Mediated Reoxidation of Protein Disulfide Isomerase Accelerates the Folding of Cone Snail ToxinsZinc regulates ERp44-dependent protein quality control in the early secretory pathway
P50
Q27617570-2A81E758-00DD-41A8-B0B2-2F1FD718BCE5Q27653763-F1E093A1-12FB-47E9-B201-A8AE1C9D199DQ27658361-48CEE7ED-0E5B-45B5-AA6E-933555E69BF1Q27664438-7AFF36CD-CD78-461D-AC04-2304F46645F9Q27688968-A52DD4A0-D786-4797-A8C1-F9E23720F560Q34246180-F8C0F7D0-9B5E-4244-A508-D51D6C2397A0Q34611586-D7D33813-9D4E-4631-BDFF-AB588A28AAE2Q35055321-9448C018-2885-4843-9C43-A07E1140EA18Q35796174-AEB327D2-B373-464D-BF54-484803F6A11CQ36382356-CD04C66E-3B0C-47C1-818D-89E9E763EE3AQ37033153-2F797156-00AC-40B5-B87F-448B5EE7ECFAQ37346866-D63C9E9B-CBB6-41F8-959D-A896962C88B4Q37536471-CFA5A0C7-6D92-45C4-A171-519F96414888Q37778853-AF0E0FF0-1389-46A0-81D4-C42E2DCBBA9AQ37965218-BBF1FF78-1178-4727-AE08-7B06C5AE2665Q38001127-69CDF673-2BBE-4123-B523-D3743F6B4D4CQ38362126-97A21572-4C83-4C0A-9FF7-422FE7988A35Q38803168-70C89444-0BEE-4FE8-AED9-DB44D0057EE9Q39647375-0CC650BD-AA8A-4157-A95A-0FFC92D84DF9Q40456503-1FF84F33-0A20-4170-98C6-04679F639559Q41280647-A46EA8FB-63AF-4735-A7BE-DF980569AE46Q41387700-D918B7D8-5444-4F28-92C1-9984B5B9C66AQ41847569-5A7878EF-3948-48EF-BD9B-86B4FCBCDD8BQ41911143-883399E6-41E0-4F70-ABD0-FDAAFC4306FDQ41975339-8B21975E-E80E-4638-B9BD-8E8024BD72D3Q42290711-2A43C9AB-CB90-4001-97AB-24CBCF9004F3Q42587502-C764EE9C-131A-4627-B06E-AAD3C8A6C734Q42915527-013F1591-D52B-419B-85A7-D0EED2B4FFF0Q43142090-3ED4E387-9EA5-4693-B528-50C65CEE75FBQ44366662-F2D2D09B-418B-4163-8E89-3EB95EB25574Q45044166-DD156E1D-7941-475F-AD8C-E88E9AE402BEQ48296760-361BC66A-DD8D-493D-ABA5-79098615A1F3Q51016604-4931A726-A7AC-48D9-A3B2-56C3F8D08CFEQ53190488-B2FA7822-4F25-44F7-AACE-8921D4E78A11Q53618251-E10E523A-5EC7-40A6-8BD3-34971C52DD7BQ54451866-DD804932-3238-44CE-8388-78C7798BFFDAQ57471356-C5EEC9CC-5A0B-4606-945A-1D09C81B09B5Q57811254-FF9C6B7A-A330-4CF8-B542-E3E9914F76F6Q58584809-BEAB8536-4EB1-4389-AB6A-7BB57F35EF03Q61799397-4252E36B-87EE-42BF-A5D4-9C3B1DCCF61A
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Kenji Inaba
@ast
Kenji Inaba
@en
Kenji Inaba
@es
Kenji Inaba
@nl
type
label
Kenji Inaba
@ast
Kenji Inaba
@en
Kenji Inaba
@es
Kenji Inaba
@nl
prefLabel
Kenji Inaba
@ast
Kenji Inaba
@en
Kenji Inaba
@es
Kenji Inaba
@nl
P106
P1153
35744890100
P31
P496
0000-0001-8229-0467