about
sameAs
Expression, folding, and proton transport activity of human uncoupling protein-1 (UCP1) in lipid membranes: evidence for associated functional formsTargeting and assembly of components of the TOC protein import complex at the chloroplast outer envelope membrane.The roles of toc34 and toc75 in targeting the toc159 preprotein receptor to chloroplasts.The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domainsDistinct pathways mediate the sorting of tail-anchored proteins to the plastid outer envelope.A comparative study on conformation and ligand binding of the neuronal uncoupling proteins.Toward understanding the mechanism of ion transport activity of neuronal uncoupling proteins UCP2, UCP4, and UCP5.A split-ubiquitin yeast two-hybrid screen to examine the substrate specificity of atToc159 and atToc132, two Arabidopsis chloroplast preprotein import receptors.Molecular characterization and expression analysis of chloroplast protein import components in tomato (Solanum lycopersicum).Folding and self-association of atTic20 in lipid membranes: implications for understanding protein transport across the inner envelope membrane of chloroplasts.The targeting of the atToc159 preprotein receptor to the chloroplast outer membrane is mediated by its GTPase domain and is regulated by GTP.Essential role of the G-domain in targeting of the protein import receptor atToc159 to the chloroplast outer membrane.A CD study of uncoupling protein-1 and its transmembrane and matrix-loop domains.The relationship between NMDA receptor function and the high ammonia tolerance of anoxia-tolerant goldfish.Co-association of cytochrome f catabolites and plastid-lipid-associated protein with chloroplast lipid particlesLipid metabolism during plant senescenceIn vivo analysis of the role of atTic20 in protein import into chloroplastsAntibody production in plantsThe production of antibodies in plants: an idea whose time has come?Import pathways of chloroplast interior proteins and the outer-membrane protein OEP14 converge at Toc75In vitro analysis of chloroplast protein importpH-induced changes in intrinsically disordered proteinsRole of positively charged residues of the second transmembrane domain in the ion transport activity and conformation of human uncoupling protein-2
P50
Q28115281-9D2731E1-4FE7-4E0B-A844-318A7DF31CBAQ30153378-24CE2344-DA65-4EED-87D2-D9FB89774B41Q30164531-6F2E2A9C-E7D2-4361-8D27-E4C62BC48E1FQ33521382-17CB6954-1AF1-4DF4-908C-0A6941053B05Q33564134-55BF7288-DA67-405C-B725-4A716870A24AQ34087364-A0D63DDC-8743-4DD9-B30B-CC4C59F46F81Q34270188-CADF2825-D976-4E09-AFA4-D35F0B9D2E09Q35149307-21964DEB-A1B6-4782-811D-1BDD8FCD6C32Q35153974-CDC8D499-7DFD-43AD-9681-F6EE88077780Q35536206-AF4EF7EC-0C02-4031-8D70-EDBD34AE294CQ36324275-A416372A-63F5-45CF-85C9-C2D696F68ED1Q36324307-E6FFD2DD-082F-4F31-8317-CBA71D0FCAAFQ46780654-5EDAA4C4-E35A-41B4-B3D4-511D3199D3D6Q48528745-85C38CB3-ECDA-496A-8ECC-68FA30896B34Q74302621-5E58D9F8-05D4-4962-A233-FE50AF8C7519Q77601525-384BC647-4AA9-438D-B3AF-4A02FD661BEAQ77809714-4B451B7F-5FD8-4CFC-A4AD-CBB2DA7262BFQ79138282-9C36F7FD-0801-49B7-820F-8C9A65E199A2Q79139153-29CD152D-311C-4AE2-B841-9FA0B5314C87Q80349520-F71CB777-7E2B-4DB8-9A81-4FE6C8F0D07FQ80568516-D0F6D8A8-5179-4C58-AAB9-4A011342EC6AQ84597350-98A73C6F-8C8B-4A62-940E-6BC2232402B1Q86957626-474B9944-C1AC-4F8A-8AB6-AE4AF8DD80DC
P50
description
onderzoeker
@nl
researcher ORCID ID = 0000-0002-2855-5126
@en
name
Matthew D Smith
@ast
Matthew D Smith
@en
Matthew D Smith
@es
Matthew D Smith
@nl
type
label
Matthew D Smith
@ast
Matthew D Smith
@en
Matthew D Smith
@es
Matthew D Smith
@nl
prefLabel
Matthew D Smith
@ast
Matthew D Smith
@en
Matthew D Smith
@es
Matthew D Smith
@nl
P106
P31
P496
0000-0002-2855-5126