Repositioning of transmembrane alpha-helices during membrane protein folding.
about
OST4 is a subunit of the mammalian oligosaccharyltransferase required for efficient N-glycosylationPredicting three-dimensional structures of transmembrane domains of β-barrel membrane proteins.Why is the biological hydrophobicity scale more accurate than earlier experimental hydrophobicity scales?Changed membrane integration and catalytic site conformation are two mechanisms behind the increased Aβ42/Aβ40 ratio by presenilin 1 familial Alzheimer-linked mutations.Evaluation of cell-free protein synthesis for the crystallization of membrane proteins--a case study on a member of the glutamate transporter family from Staphylothermus marinus.MPRAP: an accessibility predictor for a-helical transmembrane proteins that performs well inside and outside the membraneGO-PROMTO illuminates protein membrane topologies of glycan biosynthetic enzymes in the Golgi apparatus of living tissues.Membrane protein insertion at the endoplasmic reticulum.The energetics of transmembrane helix insertion into a lipid bilayer.Mechanisms of integral membrane protein insertion and foldingAlteration of CFTR transmembrane span integration by disease-causing mutations.Marginally hydrophobic transmembrane α-helices shaping membrane protein folding.A Versatile Strategy for Production of Membrane Proteins with Diverse Topologies: Application to Investigation of Bacterial Homologues of Human Divalent Metal Ion and Nucleoside Transporters.Understanding integration of α-helical membrane proteins: the next stepsEvolution of YidC/Oxa1/Alb3 insertases: three independent gene duplications followed by functional specialization in bacteria, mitochondria and chloroplasts.Computational studies of membrane proteins: models and predictions for biological understanding.Adaptation of low-resolution methods for the study of yeast microsomal polytopic membrane proteins: a methodological review.Life at the border: adaptation of proteins to anisotropic membrane environment.The safety dance: biophysics of membrane protein folding and misfolding in a cellular contextImproved topology prediction using the terminal hydrophobic helices rule.Positional editing of transmembrane domains during ion channel assembly.Folding of Aquaporin 1: multiple evidence that helix 3 can shift out of the membrane core.Quality control of integral membrane proteins by assembly-dependent membrane integration.Orientational preferences of neighboring helices can drive ER insertion of a marginally hydrophobic transmembrane helix.Influence of Pathogenic Mutations on the Energetics of Translocon-Mediated Bilayer Integration of Transmembrane Helices.Membrane protein shaving with thermolysin can be used to evaluate topology predictors.The de novo design of a biocompatible and functional integral membrane protein using minimal sequence complexity
P2860
Q28941760-6A3D2AC0-0659-48DC-B3EB-761E6130E3F6Q30155413-ED249202-5783-476F-A697-C21EE9201201Q30361608-18DBBB19-B9B3-46B9-939F-64CE46467AF2Q30363483-26684539-5A3C-45FB-BF17-B14844DF295FQ30425362-27329DD4-90E1-42E9-8D91-7E5466D4C001Q33611134-64C35BD1-84A8-401E-8383-43E40DDDEC89Q34170804-784AA4ED-06A0-496E-B404-5390D2CADDF2Q34179638-C821B241-1C46-47A3-888D-A34A65DE8957Q34202203-5DCCF253-2084-458D-9A74-AC88E6CE7EBBQ35118815-E9CC6A5C-3631-47E5-B6C3-E8C8BE2C4CC4Q35579788-A49D794F-FCA0-4A14-98C0-BE720007DDFAQ35846068-FB372473-9B1E-4953-A672-E81F17C88E91Q35852694-B5C30A02-FC15-4768-8D6F-DF33A6973F62Q36570393-DC2832F7-1FF4-471E-8AD5-792239ACD608Q37824861-501AEFD7-DE00-4BD3-A998-47E6F396A412Q37952425-26F4D0BC-9D0F-48DC-B263-BC536B01ED9BQ38077207-19E770E1-66D2-4BD8-990D-DF61BD043EAFQ38221738-401AF0F2-04B2-4D01-BA44-0DA058E3BFEDQ38270911-41BF0B43-C704-4544-846F-72D72FF447DDQ38384568-D74FE64E-9EB2-4DDC-B6C4-9BC6847F3625Q39472094-44107A09-E65B-456F-AFAF-A50C753A0229Q41963693-7307B845-0DAC-4F71-915A-9CB3530A0D16Q42601207-EC460F71-E434-44D3-963D-BDE5E66502AFQ42949708-2C184CD7-F7E4-4F24-AA4C-EC3593377E62Q43190054-BE0F26C3-820A-45BB-A981-E0B14257E47FQ54315009-7782140C-F1D7-44C7-BE98-C8064531257EQ57062484-02F57EC2-1492-4726-B032-5DD9A1DD1895
P2860
Repositioning of transmembrane alpha-helices during membrane protein folding.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年学术文章
@wuu
2010年学术文章
@zh
2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
@zh-sg
2010年學術文章
@yue
2010年學術文章
@zh-hant
name
Repositioning of transmembrane alpha-helices during membrane protein folding.
@en
Repositioning of transmembrane alpha-helices during membrane protein folding.
@nl
type
label
Repositioning of transmembrane alpha-helices during membrane protein folding.
@en
Repositioning of transmembrane alpha-helices during membrane protein folding.
@nl
prefLabel
Repositioning of transmembrane alpha-helices during membrane protein folding.
@en
Repositioning of transmembrane alpha-helices during membrane protein folding.
@nl
P2093
P50
P1476
Repositioning of transmembrane alpha-helices during membrane protein folding.
@en
P2093
Anni Kauko
Estelle Thebaud
Linnea E Hedin
P304
P356
10.1016/J.JMB.2010.01.042
P407
P577
2010-01-25T00:00:00Z