Sarah Shammas
Cited by
Cited by
Metastability of native proteins and the phenomenon of amyloid formation
AJ Baldwin, TPJ Knowles, GG Tartaglia, AW Fitzpatrick, GL Devlin, ...
Journal of the American Chemical Society 133 (36), 14160-14163, 2011
Plasticity of an ultrafast interaction between nucleoporins and nuclear transport receptors
S Milles, D Mercadante, IV Aramburu, MR Jensen, N Banterle, C Koehler, ...
Cell 163 (3), 734-745, 2015
A mechanistic model of tau amyloid aggregation based on direct observation of oligomers
SL Shammas, GA Garcia, S Kumar, M Kjaergaard, MH Horrocks, N Shivji, ...
Nature communications 6 (1), 1-10, 2015
Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongation
SL Shammas, CA Waudby, S Wang, AK Buell, TPJ Knowles, H Ecroyd, ...
Biophysical journal 101 (7), 1681-1689, 2011
Insights into coupled folding and binding mechanisms from kinetic studies
SL Shammas, MD Crabtree, L Dahal, BIM Wicky, J Clarke
Journal of Biological Chemistry 291 (13), 6689-6695, 2016
Perturbation of the stability of amyloid fibrils through alteration of electrostatic interactions
SL Shammas, TPJ Knowles, AJ Baldwin, CE MacPhee, ME Welland, ...
Biophysical journal 100 (11), 2783-2791, 2011
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, ...
Proceedings of the National Academy of Sciences 111 (43), 15420-15425, 2014
Remarkably fast coupled folding and binding of the intrinsically disordered transactivation domain of cMyb to CBP KIX
SL Shammas, AJ Travis, J Clarke
The journal of physical chemistry B 117 (42), 13346-13356, 2013
Transient misfolding dominates multidomain protein folding
A Borgia, KR Kemplen, MB Borgia, A Soranno, S Shammas, B Wunderlich, ...
Nature communications 6 (1), 1-10, 2015
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 111 (33), 12055-12060, 2014
Intrinsic determinants of neurotoxic aggregate formation by the amyloid β peptide
AC Brorsson, B Bolognesi, GG Tartaglia, SL Shammas, G Favrin, I Watson, ...
Biophysical journal 98 (8), 1677-1684, 2010
Hsp70 inhibits the nucleation and elongation of tau and sequesters tau aggregates with high affinity
F Kundel, S De, P Flagmeier, MH Horrocks, M Kjaergaard, SL Shammas, ...
ACS chemical biology 13 (3), 636-646, 2018
Affinity of IDPs to their targets is modulated by ion-specific changes in kinetics and residual structure
BIM Wicky, SL Shammas, J Clarke
Proceedings of the National Academy of Sciences 114 (37), 9882-9887, 2017
Separating the effects of internal friction and transition state energy to explain the slow, frustrated folding of spectrin domains
BG Wensley, LG Kwa, SL Shammas, JM Rogers, S Browning, Z Yang, ...
Proceedings of the National Academy of Sciences 109 (44), 17795-17799, 2012
Slow, reversible, coupled folding and binding of the spectrin tetramerization domain
SL Shammas, JM Rogers, SA Hill, J Clarke
Biophysical journal 103 (10), 2203-2214, 2012
Mechanistic roles of protein disorder within transcription
SL Shammas
Current opinion in structural biology 42, 155-161, 2017
pKID binds to KIX via an unstructured transition state with nonnative interactions
L Dahal, TOC Kwan, SL Shammas, J Clarke
Biophysical journal 113 (12), 2713-2722, 2017
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, ...
Biochemistry 56 (18), 2379-2384, 2017
Role of non-native electrostatic interactions in the coupled folding and binding of PUMA with Mcl-1
WT Chu, J Clarke, SL Shammas, J Wang
PLoS computational biology 13 (4), e1005468, 2017
Two differential binding mechanisms of FG-nucleoporins and nuclear transport receptors
PS Tan, IV Aramburu, D Mercadante, S Tyagi, A Chowdhury, D Spitz, ...
Cell reports 22 (13), 3660-3671, 2018
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