about
FK506-binding protein of the hyperthermophilic archaeum, Thermococcus sp. KS-1, a cold-shock-inducible peptidyl-prolyl cis-trans isomerase with activities to trap and refold denatured proteinsProtein disulphide isomerase-assisted functionalization of keratin-based matrices.Chaperoning G protein-coupled receptors: from cell biology to therapeuticsRecognition between flexible protein molecules: induced and assisted folding.Prolyl isomerases in a minimal cell. Catalysis of protein folding by trigger factor from Mycoplasma genitalium.Proteolytically inactive insulin-degrading enzyme inhibits amyloid formation yielding non-neurotoxic aβ peptide aggregatesFK506-Binding protein 22 from a psychrophilic bacterium, a cold shock-inducible peptidyl prolyl isomerase with the ability to assist in protein folding.The alphabet of intrinsic disorder: I. Act like a Pro: On the abundance and roles of proline residues in intrinsically disordered proteins.Procollagen binds to both prolyl 4-hydroxylase/protein disulfide isomerase and HSP47 within the endoplasmic reticulum in the absence of ascorbate.Reverse gyrase has heat-protective DNA chaperone activity independent of supercoiling.Characterization of beta-galactosidase mutations Asp332-->Asn and Arg148-->Ser, and a polymorphism, Ser532-->Gly, in a case of GM1 gangliosidosisHydrogen bonds are a primary driving force for de novo protein folding.Protein disulfide isomerase-mediated cell-free assembly of recombinant interleukin-12 p40 homodimers.The J-domain protein J3 mediates the integration of flowering signals in Arabidopsis.
P2860
Q28343586-4A914B5F-8AE4-4F32-BBFE-660BDBBF1B0DQ33851893-8E66D328-E8CD-401C-8467-21112093F0CAQ33927508-8FD4853A-9513-4031-9A63-327D8C828604Q34141716-E8D708EF-9A1B-4718-96A1-7B7E0DF4D3FBQ34508934-BDA40E72-801C-48C2-B154-3E93DCCB03A3Q34672360-D95976F6-ACE0-428F-A5E3-294AC4365123Q35229519-799BBE50-4C65-48AD-9076-6997CC3F97F5Q38779767-3DCDF7A5-AA2A-4F05-AB49-E4DF06A8BF83Q40903724-F04A7291-8187-4E43-ACA0-B8E8732A87B5Q41337691-C8F9980E-0796-4EEA-B654-87E7EC1236EAQ42158395-B2206A9F-EFE8-4E49-8F4F-58885B75F53AQ47130583-70A65ED0-8AB7-4B47-A492-61A1668F63EFQ50335934-1C123DC1-1459-42BD-BBE3-CE1DBCFA8EC6Q51888088-EEE76279-6D1B-4D65-A470-D3C1A0A9A6FB
P2860
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
Enzymes as chaperones and chaperones as enzymes.
@en
type
label
Enzymes as chaperones and chaperones as enzymes.
@en
prefLabel
Enzymes as chaperones and chaperones as enzymes.
@en
P2860
P1433
P1476
Enzymes as chaperones and chaperones as enzymes.
@en
P2860
P304
P356
10.1016/S0014-5793(98)00272-5
P407
P577
1998-04-01T00:00:00Z