about
The quaternary structure of the recombinant bovine odorant-binding protein is modulated by chemical denaturantsStructure and stability of recombinant bovine odorant-binding protein: III. Peculiarities of the wild type bOBP unfolding in crowded milieuElectrostatic effects in the folding of the SH3 domain of the c-Src tyrosine kinase: pH-dependence in 3D-domain swapping and amyloid formationOptical control of protein-protein interactions via blue light-induced domain swapping.Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state nuclear magnetic resonance.Foldon unfolding mediates the interconversion between M(pro)-C monomer and 3D domain-swapped dimerTransient misfolding dominates multidomain protein foldingRole of domain swapping in the hetero-oligomeric cytochrome b6f lipoprotein complexStructure and stability of recombinant bovine odorant-binding protein: I. Design and analysis of monomeric mutants.Structural Interface Forms and Their Involvement in Stabilization of Multidomain Proteins or Protein ComplexesSmall Molecule-Induced Domain Swapping as a Mechanism for Controlling Protein Function and Assembly.Engineered Domain Swapping as an On/Off Switch for Protein Function.Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.Insights into the mechanism of cystatin C oligomer and amyloid formation and its interaction with β-amyloid.
P2860
Q28538377-066BBA4B-0A98-415D-BC9D-54E70D274F1DQ28834433-A4E5A1E6-BAB2-42E6-9F45-7A8D2D572E6BQ30009257-2AB107B8-214B-48EB-8FB5-DBD973E752E1Q30364468-0B06E676-F406-4E10-B9B1-E0C39D6DFB79Q33654425-869AD65B-F202-4E00-90EB-35776342B883Q34414446-3975F624-8C56-4DD8-98D7-266FBE1602ADQ36236356-C4831027-D23E-4999-8D25-DDAA7BB37B09Q36320489-3433BBA9-69C3-4C0C-B39A-79BE3464E0FEQ36354453-B515F837-47AC-47F8-A0F3-D01EFFBFA69BQ40505556-ECBE386B-48A7-45F3-A513-EFBA578519BCQ41614032-0D303FC0-6890-4E87-B2F4-B32C18EA7127Q41857056-FE905559-CF61-4D76-BF9C-C3B91A8A5769Q42600053-1F9CD73C-D545-41C2-9473-FD48E7517048Q47647902-E056B7BC-59CC-47CD-AA75-F50259630292Q50882222-7B864695-158F-416A-A7F5-0507B6794549
P2860
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Domain swapping and amyloid fibril conformation.
@en
Domain swapping and amyloid fibril conformation.
@nl
type
label
Domain swapping and amyloid fibril conformation.
@en
Domain swapping and amyloid fibril conformation.
@nl
prefLabel
Domain swapping and amyloid fibril conformation.
@en
Domain swapping and amyloid fibril conformation.
@nl
P2860
P356
P1433
P1476
Domain swapping and amyloid fibril conformation
@en
P2093
Patrick C A van der Wel
P2860
P304
P356
10.4161/PRI.18987
P577
2012-07-01T00:00:00Z