The Clarke Group

Publications

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  • Currently displaying 21 - 40 of 167 publications
Author(s)
Publication title
Journal Name
Publication year
Conserved Helix-Flanking Prolines Modulate Intrinsically Disordered Protein:Target Affinity by Altering the Lifetime of the Bound Complex
MD Crabtree, W Borcherds, A Poosapati, SL Shammas, GW Daughdrill, J Clarke
Biochemistry
(2017)
56
(doi: 10.1021/acs.biochem.7b00179)
Role of Non-Native Electrostatic Interactions in the Coupled Folding and Binding of PUMA with Mcl-1
W-T Chu, J Clarke, SL Shammas, J Wang
PLoS computational biology
(2017)
13
(doi: 10.1371/journal.pcbi.1005468)
Effect of Transient Helicity of cMyb TAD on its Binding Affinity to the Kix Domain of CBP/p300
A Poosapati, W Borcherds, MD Carbtree, SL Shammas, J Clarke, GW Daughdrill
FASEB JOURNAL
(2017)
31
Cotranslational folding of spectrin domains via partially structured states
OB Nilsson, AA Nickson, JJ Hollins, S Wickles, A Steward, R Beckmann, G von Heijne, J Clarke
Nature Structural & Molecular Biology
(2017)
24
(doi: 10.1038/nsmb.3355)
What Encodes Coupled Folding and Binding Reactions: IDPS or Partner Proteins?
MD Crabtree, CATF Mendonca, Q Bubb, SL Shammas, J Clarke
Biophysical Journal
(2017)
112
(doi: 10.1016/j.bpj.2016.11.2603)
Editorial overview: Protein Folding and Binding, Complexity Comes of Age.
J Clarke, RV Pappu
Current Opinion in Structural Biology
(2017)
42
(doi: 10.1016/j.sbi.2017.03.004)
Disorder drives cooperative folding in a multi-domain protein
DT Gruszka, CATF Mendonça, E Paci, F Whelan, J Hawkhead, JR Potts, J Clarke
Proceedings of the National Academy of Sciences
(2016)
113
(doi: 10.1073/pnas.1608762113)
Cotranslational folding studies of spectrin and Ig-like domains show folding occurs close to the ribosome
A Steward, OB Nilsson, AA Nickson, JJ Hollins, S Wickles, A Marsden, C Mendonca, R Beckmann, G von Heijne, J Clarke
PROTEIN SCIENCE
(2016)
25
Protein folding - on and off the ribosome: Using Physics and Chemistry to understand Biology
J Clarke
PROTEIN SCIENCE
(2016)
25
GADIS: Algorithm for designing sequences to achieve target secondary structure profiles of intrinsically disordered proteins.
TS Harmon, MD Crabtree, SL Shammas, AE Posey, J Clarke, RV Pappu
Protein Engineering Design and Selection
(2016)
29
(doi: 10.1093/protein/gzw034)
Plasticity of Nucleoporin Nuclear Transport Receptor Interactions - Molecular Description of a Highly Dynamic, Ultrafast Interaction Mechanism
IV Aramburu, D Mercadante, S Milles, M Ringkjobing, N Banterle, C Koehler, S Tyagi, J Clarke, SL Shammas, M Blackledge, F Graeter, EA Lemke
BIOPHYSICAL JOURNAL
(2016)
110
The Role of Disorder in Protein Folding
J Clarke
Biophysical Journal
(2016)
110
(doi: 10.1016/j.bpj.2015.11.1095)
Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies*
SL Shammas, MD Crabtree, L Dahal, BIM Wicky, J Clarke
Journal of Biological Chemistry
(2016)
291
(doi: 10.1074/jbc.R115.692715)
De Novo Evolutionary Emergence of a Symmetrical Protein Is Shaped by Folding Constraints.
RG Smock, I Yadid, O Dym, J Clarke, DS Tawfik
Cell
(2016)
164
(doi: 10.1016/j.cell.2015.12.024)
Transient misfolding dominates multidomain protein folding.
A Borgia, KR Kemplen, MB Borgia, A Soranno, S Shammas, B Wunderlich, D Nettels, RB Best, J Clarke, B Schuler
Nature communications
(2015)
6
(doi: 10.1038/ncomms9861)
Plasticity of an ultrafast interaction between nucleoporins and nuclear transport receptors.
S Milles, D Mercadante, IV Aramburu, MR Jensen, N Banterle, C Koehler, S Tyagi, J Clarke, SL Shammas, M Blackledge, F Gräter, EA Lemke
Cell
(2015)
163
(doi: 10.1016/j.cell.2015.09.047)
Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein.
DT Gruszka, F Whelan, OE Farrance, HKH Fung, E Paci, CM Jeffries, DI Svergun, C Baldock, CG Baumann, DJ Brockwell, JR Potts, J Clarke
Nature Communications
(2015)
6
(doi: 10.1038/ncomms8271)
The response of greek key proteins to changes in connectivity depends on the nature of their secondary structure
KR Kemplen, D De Sancho, J Clarke
J Mol Biol
(2015)
427
(doi: 10.1016/j.jmb.2015.03.020)
Evolution of oligomeric state through allosteric pathways that mimic ligand binding.
T Perica, Y Kondo, SP Tiwari, SH McLaughlin, KR Kemplen, X Zhang, A Steward, N Reuter, J Clarke, SA Teichmann
Science
(2014)
346
(doi: 10.1126/science.1254346)
Interplay between partner and ligand facilitates the folding and binding of an intrinsically disordered protein.
JM Rogers, V Oleinikovas, SL Shammas, CT Wong, D De Sancho, CM Baker, J Clarke
Proceedings of the National Academy of Sciences
(2014)
111
(doi: 10.1073/pnas.1409122111)
Yusuf Hamied Department of Chemistry
Lensfield Road
Cambridge
CB2 1EW
T: +44 (0) 1223 336300
enquiries@ch.cam.ac.uk
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