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The Clarke Group

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  • Currently displaying 1 - 20 of 145 publications
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,
2379
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,
e1005468
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,
221
Editorial overview: Protein Folding and Binding, Complexity Comes of Age
J Clarke, RV Pappu
– Current opinion in structural biology
(2017)
42,
v
Protein folding - on and off the ribosome: Using Physics and Chemistry to understand Biology
J Clarke
– PROTEIN SCIENCE
(2016)
25,
175
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,
339
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,
357A
The Role of Disorder in Protein Folding
J Clarke
– BIOPHYSICAL JOURNAL
(2016)
110,
196A
Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies
SL Shammas, MD Crabtree, L Dahal, BIM Wicky, J Clarke
– J Biol Chem
(2016)
291,
6689
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,
476
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,
734
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
– Journal of molecular biology
(2014)
427,
2159
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,
7271
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,
8861
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,
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 of the United States of America
(2014)
111,
15420
Allostery within a transcription coactivator is predominantly mediated through dissociation rate constants
SL Shammas, AJ Travis, J Clarke
– Proceedings of the National Academy of Sciences of the United States of America
(2014)
111,
12055
Coupled folding and binding of the disordered protein PUMA does not require particular residual structure.
JM Rogers, CT Wong, J Clarke
– Journal of the American Chemical Society
(2014)
136,
5197
Mechanism of assembly of the non-covalent spectrin tetramerization domain from intrinsically disordered partners
SA Hill, LG Kwa, SL Shammas, JC Lee, J Clarke
– Journal of Molecular Biology
(2014)
426,
21
The folding of a family of three-helix bundle proteins: spectrin R15 has a robust folding nucleus, unlike its homologous neighbours.
LG Kwa, BG Wensley, CG Alexander, SJ Browning, BR Lichman, J Clarke
– Journal of molecular biology
(2014)
426,
1600