about
Intrinsically unstructured proteins and their functionsStructure of the PHD zinc finger from human Williams-Beuren syndrome transcription factorThe CH2 domain of CBP/p300 is a novel zinc fingerMonomeric complex of human orphan estrogen related receptor-2 with DNA: a pseudo-dimer interface mediates extended half-site recognitionCooperative regulation of p53 by modulation of ternary complex formation with CBP/p300 and HDM2Role of disorder in IκB-NFκB interactionNMR solution structure of the inserted domain of human leukocyte function associated antigen-1Solution structure and acetyl-lysine binding activity of the GCN5 bromodomainStructural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response.Structure of the nuclear factor ALY: insights into post-transcriptional regulatory and mRNA nuclear export processesInteraction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: regulation by competition between intrinsically unstructured ligands for non-identical binding sitesRecognition of the mRNA AU-rich element by the zinc finger domain of TIS11dEmbryonic Neural Inducing Factor Churchill Is not a DNA-binding Zinc Finger Protein: Solution Structure Reveals a Solvent-exposed β-Sheet and Zinc Binuclear ClusterStructural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation domainsStructure of the p53 Transactivation Domain in Complex with the Nuclear Receptor Coactivator Binding Domain of CREB Binding ProteinDivergent evolution of protein conformational dynamics in dihydrofolate reductase.Structural Characterization of Interactions between the Double-Stranded RNA-Binding Zinc Finger Protein JAZ and Nucleic AcidsHigh-resolution solution structures of oxidized and reduced Escherichia coli thioredoxinNMR solution structure of Cu(I) rusticyanin from Thiobacillus ferrooxidans: structural basis for the extreme acid stability and redox potentialStructure-based design of a constrained peptide mimic of the HIV-1 V3 loop neutralization siteSolution Structure of the KIX Domain of CBP Bound to the Transactivation Domain of CREB: A Model for Activator:Coactivator InteractionsHigh-resolution solution structure of the retinoid X receptor DNA-binding domainRoles of phosphorylation and helix propensity in the binding of the KIX domain of CREB-binding protein by constitutive (c-Myb) and inducible (CREB) activatorsCooperativity 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 domainStructure, dynamics, and catalytic function of dihydrofolate reductaseConformational preferences in the Ser133-phosphorylated and non-phosphorylated forms of the kinase inducible transactivation domain of CREBThe dynamic energy landscape of dihydrofolate reductase catalysisCoupling of folding and binding for unstructured proteinsIdentification of the regions involved in DNA binding by the mouse PEBP2alpha protein.Nuclear magnetic resonance 15N and 1H resonance assignments and global fold of rusticyanin. Insights into the ligation and acid stability of the blue copper site.Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H NMR spectra.Conformational changes in the active site loops of dihydrofolate reductase during the catalytic cycle.Dynamic Interaction of Hsp90 with Its Client Protein p53.CheShift-2 resolves a local inconsistency between two X-ray crystal structures.Copper binding to the prion protein: structural implications of four identical cooperative binding sitesCharacterization of monomeric and dimeric B domain of Staphylococcal protein A.Random coil chemical shifts in acidic 8 M urea: implementation of random coil shift data in NMRView.Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin.Generation of native-like protein structures from limited NMR data, modern force fields and advanced conformational sampling.Immunogenic peptides corresponding to the dominant antigenic region alanine-597 to cysteine-619 in the transmembrane protein of simian immunodeficiency virus have a propensity to fold in aqueous solution.
P50
Q22061731-986131F0-3F27-4181-BC30-DC29CB4D5812Q24290654-4479BBAE-F00F-4E05-B70B-7648BAAC7C99Q24297599-AA7C16F1-07B9-4909-8686-D4ADAF5E1A38Q24298361-D5692E41-5576-43E3-86B5-325EB6B069F5Q24655602-405763A5-1752-495D-A8AF-076369008C63Q26865182-017F8923-FE24-4908-9680-198368CB4F98Q27621156-416FD443-4919-433C-B0EC-CFE14EA53021Q27628617-AA3B9A98-2C81-4944-BB5B-FFB7A12E3719Q27638869-5C57D6D0-24C7-48CB-BD74-736D3F0708A3Q27641440-B2A84F45-4F37-4F9E-A9CC-D375E2FA464CQ27642464-4C9DB2D0-BADE-4AC9-9E00-CEC706B77E33Q27643189-14074580-3289-4200-8A11-62BC7EE70D8AQ27646549-CE30865A-90E9-4335-84F5-32D15F33F517Q27653760-12F9D27B-0BFD-4367-81E2-794CBD23932DQ27665216-CC932243-3F28-4867-B02F-C4BF6BDD3C3BQ27680098-806E1026-72B9-4ED4-B9D0-C4AF4DF89261Q27681695-CED47079-A3C5-4946-840F-4F0978226CEBQ27730312-A250DB23-85A6-4EAA-9803-8803D0904D73Q27734092-2835ED71-27A7-423A-AFCA-62A5B8A35EC2Q27734926-D23E3A63-2ECE-40ED-9B80-0766970AFAAAQ27748755-D6762D5D-A758-4154-B581-A01ACD24C120Q27764990-D5AF2EAE-0113-4CCE-BD3C-EA5E4048DF91Q28219104-FFC46081-2CBE-4215-A3FC-520AFE7BF0A7Q28219772-E68FEC3A-26DF-4A50-A97B-ADFD398BB7B8Q28261353-0BB29397-6A51-4C5C-8247-AE2A4FAF2CC7Q28910220-7E03AEE9-24A1-4F50-A46F-F6D9CAB9D230Q29616409-89D1EB81-AE35-4CD4-864C-2CB9FF90F5E8Q29616417-C7C10962-7E29-468E-9929-FD7C10FD18FCQ30175216-9BBCCDC0-7E23-4052-B3F1-9CC67F79BB68Q30193818-77B28104-E0BA-44CD-BD66-FD2958D76D21Q30326441-C93951E1-E4BF-40A3-914D-728950E91CC7Q30349857-8E8A43B9-9E7F-4D41-908E-6193A8A77F99Q30403624-54D26296-F093-476F-8066-A2ECDF8F0057Q30420918-6674A5B6-66A0-4D7A-A8E5-C5BC80D6DE4AQ30558995-C2D3C946-D11C-49F9-9B1F-FE8DD298BE25Q30583152-C449E0D4-4349-4927-85D5-48D05C724CC6Q30619296-B4903350-FA29-4076-B632-BA5A62FC88F4Q30920034-0F8F37A8-50DE-4D23-8F84-618CD6565E8DQ30982097-DCA14BCE-9D03-44C5-9CC5-DB2D1E9341E0Q31106079-3530D165-581C-4A2E-BF39-597AB87CE8DC
P50
description
British-born biophysicist
@en
biofysicus
@nl
name
H. Jane Dyson
@ast
H. Jane Dyson
@en
H. Jane Dyson
@es
H. Jane Dyson
@fr
H. Jane Dyson
@nl
H. Jane Dyson
@sl
type
label
H. Jane Dyson
@ast
H. Jane Dyson
@en
H. Jane Dyson
@es
H. Jane Dyson
@fr
H. Jane Dyson
@nl
H. Jane Dyson
@sl
altLabel
Helen Jane Dyson
@en
Jane Dyson
@en
prefLabel
H. Jane Dyson
@ast
H. Jane Dyson
@en
H. Jane Dyson
@es
H. Jane Dyson
@fr
H. Jane Dyson
@nl
H. Jane Dyson
@sl
P214
P244
P1053
D-4160-2011
P106
P108
P1153
7102413157
P1207
n2012170546
P21
P214
P244
no2018146831
P31
P3829
P409
P496
0000-0001-6855-3398
P734
P7859
lccn-no2018146831