GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.
about
Heterozygous yeast deletion collection screens reveal essential targets of Hsp90NMR characterization of the interaction of GroEL with amyloid β as a model ligandStructural basis for the unfolding of anthrax lethal factor by protective antigen oligomersStructural and Functional Conservation of Mycobacterium tuberculosis GroEL Paralogs Suggests that GroEL1 Is a ChaperoninDecoding Structural Properties of a Partially Unfolded Protein Substrate: En Route to Chaperone Binding.Probing the transient dark state of substrate binding to GroEL by relaxation-based solution NMRHow do chaperonins fold protein?The synthetic and biological studies of discorhabdins and related compounds.Forces Driving Chaperone ActionGroup II archaeal chaperonin recognition of partially folded human γD-crystallin mutantsSingle-molecule observation of protein folding in symmetric GroEL-(GroES)2 complexes.Formation of the chaperonin complex studied by 2D NMR spectroscopy.Sequence features governing aggregation or degradation of prion-like proteins
P2860
Q21134948-B62AE8D7-C803-4541-984D-4F14D9C3C72FQ24338819-06D0ABB1-A51E-464A-A814-85774DED3D3FQ27665492-1848E35E-D1D0-477F-9B47-845710218B63Q27666001-15153D95-4296-470E-89D6-E0A143080769Q35783768-87128075-0D6D-4BF3-870C-0C860AA5DE9CQ37010689-39459F66-BF37-46CA-8E31-39CD7303C504Q38919368-EA7B55C3-FF23-4A59-8A91-79C7002A5006Q39539429-A80CBA89-D014-45F4-BBBE-97F5BEFDA799Q41832929-523FADAB-FBC6-4330-A04D-0325FA4CAEEDQ41990114-EF519D42-F593-42E6-A830-6DEBC6863F51Q42118511-209A55E9-4910-4B1F-9F75-AB8D6CBEC7DEQ44667117-3FDC3DFB-EF22-471F-A1E3-896EC3FF5E95Q58622949-1E949F5C-07C9-4284-8F97-F0A28983174F
P2860
GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.
@en
GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.
@nl
type
label
GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.
@en
GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.
@nl
prefLabel
GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.
@en
GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.
@nl
P2093
P2860
P356
P1476
GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.
@en
P2093
Lingling Chen
Xinfeng Gao
P2860
P304
P356
10.1074/JBC.M804818200
P407
P577
2008-12-12T00:00:00Z