Remarkably fast coupled folding and binding of the intrinsically disordered transactivation domain of cMyb to CBP KIX. - Wikidata - wikimedia - TriplyDB

Remarkably fast coupled folding and binding of the intrinsically disordered transactivation domain of cMyb to CBP KIX.

Remarkably fast coupled folding and binding of the intrinsically disordered transactivation domain of cMyb to CBP KIX.

http://www.wikidata.org/entity/Q42935134

about

Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies Binding Mechanisms of Intrinsically Disordered Proteins: Theory, Simulation, and Experiment The contribution of intrinsically disordered regions to protein function, cellular complexity, and human disease Prepaying the entropic cost for allosteric regulation in KIX Allostery within a transcription coactivator is predominantly mediated through dissociation rate constants Dissecting allosteric effects of activator-coactivator complexes using a covalent small molecule ligand.Coupled folding and binding of the disordered protein PUMA does not require particular residual structure.Interplay between partner and ligand facilitates the folding and binding of an intrinsically disordered protein The binding mechanisms of intrinsically disordered proteins.Intrinsically disordered proteins in cellular signalling and regulation.Conformational propensities of intrinsically disordered proteins influence the mechanism of binding and folding Functional advantages of dynamic protein disorder.Multivalent IDP assemblies: Unique properties of LC8-associated, IDP duplex scaffolds Role of non-native electrostatic interactions in the coupled folding and binding of PUMA with Mcl-1 Impact of the amino acid sequence on the conformation of side chain lactam-bridged octapeptides.Role of Intrinsic Protein Disorder in the Function and Interactions of the Transcriptional Coactivators CREB-binding Protein (CBP) and p300 Order-Disorder Transitions in the Cardiac Troponin Complex.Deciphering the mechanisms of binding induced folding at nearly atomic resolution: The Φ value analysis applied to IDPs.A Quantitative Fluorescence-Based Assay for Assessing LIM Domain-Peptide Interactions.Plasticity of an ultrafast interaction between nucleoporins and nuclear transport receptors.Digested disorder, Quarterly intrinsic disorder digest (October-November-December, 2013).pKID Binds to KIX via an Unstructured Transition State with Nonnative Interactions.Phosphorylation of the IDP KID Modulates Affinity for KIX by Increasing the Lifetime of the Complex.Kinetic mechanism of controlled Fab-arm exchange for the formation of bispecific immunoglobulin G1 antibodies.Affinity of IDPs to their targets is modulated by ion-specific changes in kinetics and residual structure.Fuzzy regions in an intrinsically disordered protein impair protein-protein interactions.Disparate binding kinetics by an intrinsically disordered domain enables temporal regulation of transcriptional complex formation.Conservation of coactivator engagement mechanism enables small-molecule allosteric modulators Tunable order-disorder continuum in protein-DNA interactions

P2860

Q26768540-547D1761-C4EC-4A10-BA30-C4DC00F95AE6 Q28079899-DEDAF537-FDE7-454A-B000-3C967C8ACE70 Q28080017-5602EE8F-11D4-4690-BE9D-ABFEE22659AA Q34082751-898379DA-0F1C-46DD-AAA8-AB00A87B791C Q34082986-2A104ECC-B494-452F-A193-4240BEDC1B71 Q34083040-56280077-F759-46A2-A8CE-9EEC5FB41EE3 Q34411385-8AA3D320-E38C-403B-91EA-0A7D180DBD37 Q34442046-CD817920-4B60-4229-A224-03CE9F812CC8 Q35062460-43E3F40E-1AC0-4620-9872-72C3F4B3DAE1 Q35510300-4E20FE63-107A-4E24-B70B-7766DE2D372F Q35946120-D0BD78F0-DB94-4E58-83CD-75187FD5C5BA Q36101573-761C6282-48F6-413E-BC0B-4FBB2AA0E501 Q36103418-80D9BBAD-5188-4A63-A395-8AAA1F80E55B Q36331739-410012CE-14FE-4141-BB26-24E4D5F64718 Q36332636-6C54A353-75DE-4F38-B84D-13868CDC6C01 Q36727341-C808D752-BA6B-4786-BDE2-A11C7629923A Q38891067-1E8FE163-82EB-4AC7-97B9-5144B79F9C2B Q39148669-4BAEF666-BB1B-436C-9C94-D70C11601495 Q39372345-44D5ECB4-2CC7-4ACA-90AA-7628AE8614BB Q41977391-7A7FEB3E-F1F2-4F43-B51A-846584234EF6 Q42156830-B79FDDB8-0265-44EC-897D-F342014C5C4A Q47270602-4A410C34-FA3B-4CAE-8AFC-D4504CB79352 Q47270610-84C36986-AC48-4CCF-8B96-D69285CA26A4 Q47336563-429270AD-E02D-473E-AA91-C379EE3D273D Q47894286-D1AD8067-C0B8-4D66-99F0-DF41E1813E79 Q50922689-6E2E4483-BC8A-400B-AA77-A4D32DFC5172 Q52318671-C53EE888-1A9E-41DC-BB1B-E265ED9FD11C Q57751804-DD8045B9-77C9-443B-BF5B-CD23947E6635 Q58788126-0EF166C3-5E19-4E89-A0FE-EF77D83781E3

P2860

Remarkably fast coupled folding and binding of the intrinsically disordered transactivation domain of cMyb to CBP KIX.

http://www.wikidata.org/entity/Q42935134

description

2013 nî lūn-bûn

@nan

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

2013年论文

@zh

2013年论文

@zh-cn

name

Remarkably fast coupled foldin ...... ion domain of cMyb to CBP KIX.

@en

Remarkably fast coupled foldin ...... ion domain of cMyb to CBP KIX.

@nl

type

label

Remarkably fast coupled foldin ...... ion domain of cMyb to CBP KIX.

@en

Remarkably fast coupled foldin ...... ion domain of cMyb to CBP KIX.

@nl

prefLabel

Remarkably fast coupled foldin ...... ion domain of cMyb to CBP KIX.

@en

Remarkably fast coupled foldin ...... ion domain of cMyb to CBP KIX.

@nl

P1433

Q42935134-4FBBEAEC-6644-48A1-8D17-CDA68415FE32

P1476

Q42935134-F24891EF-33EC-4A55-8BE4-A1CAE5AA7893

P2093

Q42935134-2A6A6FBF-2A8C-480D-ADA5-EFD6BD590E14

Q42935134-545DB73A-6916-46B2-A9AB-462EB92EF8CF

Q42935134-68CC3661-C8BD-49D6-9DC4-73CEDFE3B3DA

P2860

Q42935134-03299457-7297-4FA7-AB23-FAD943BD6A39

Q42935134-0AE2002B-1C9E-403F-9863-8F8FDB4DEB66

Q42935134-0EF1223C-78DC-45DA-B7C4-40413F19025B

Q42935134-1192D2F8-153A-4D59-ACC4-1053407C0584

Q42935134-13471025-AA12-44A4-A467-6932F0C3E35C

Q42935134-1688E025-8383-4930-B5F3-5FE036938424

Q42935134-188A896D-D1D4-4F06-B9EB-9AA68EC8893F

Q42935134-1F163954-553C-479C-A815-9D65EB5D2538

Q42935134-1FF1F230-5C6D-4622-856C-6BA74DDC89A6

Q42935134-22AA3758-B634-4DC1-9F10-EB5CE07634CE

P304

Q42935134-E3104D84-5C87-4A6C-B5D8-1B7BCDDCA70E

P31

Q42935134-8F3748F2-76DC-44F1-95FD-599A0E6990A6

P356

Q42935134-57491D2E-71CA-4CBC-B9C9-F3762158FAC1

P407

Q42935134-A28481C5-CBD6-4E9D-BD69-F8B740B4637B

P433

Q42935134-DFD51387-D585-4C9C-8632-4607FB87A221

P478

Q42935134-F441C63D-30D2-4784-8A82-136377DD3617

P577

Q42935134-73D4BB43-1631-4429-B0A9-118DD7140848

P5875

Q42935134-9FF0FFEC-43FA-41C7-AADE-1253D98C6F3E

P698

Q42935134-97ADAD1B-084E-4FF6-886B-6B859573208C

P932

Q42935134-BB88E5B4-8306-49F3-8459-C1D781FF9BCD

P356

P1433

Journal of Physical Chemistry B

P1476

Remarkably fast coupled foldin ...... ion domain of cMyb to CBP KIX.

@en

P2093

Alexandra J Travis

http://www.w3.org/2001/XMLSchema#string

Jane Clarke

http://www.w3.org/2001/XMLSchema#string

Sarah L Shammas

http://www.w3.org/2001/XMLSchema#string

P2860

Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life

Mapping the interactions of the p53 transactivation domain with the KIX domain of CBP

Structures of KIX domain of CBP in complex with two FOXO3a transactivation domains reveal promiscuity and plasticity in coactivator recruitment

Calculation of protein extinction coefficients from amino acid sequence data

CBP/p300 in cell growth, transformation, and development

Cooperativity in transcription factor binding to the coactivator CREB-binding protein (CBP). The mixed lineage leukemia protein (MLL) activation domain binds to an allosteric site on the KIX domain

Coupling of folding and binding for unstructured proteins

The transcriptional regulator CBP has defined spatial associations within interphase nuclei.

K2D2: estimation of protein secondary structure from circular dichroism spectra.

Fundamental aspects of protein-protein association kinetics

P304

13346-13356

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1021/JP404267E

http://www.w3.org/2001/XMLSchema#string

P407

P433

42

http://www.w3.org/2001/XMLSchema#string

P478

117

http://www.w3.org/2001/XMLSchema#string

P577

2013-08-15T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

251233421

http://www.w3.org/2001/XMLSchema#string

P698

23875714

http://www.w3.org/2001/XMLSchema#string

P932

3807845

http://www.w3.org/2001/XMLSchema#string