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- Currently displaying 1 - 20 of 167 publications
Selective Affimers Recognise the BCL‐2 Family Proteins BCL‐xL and MCL‐1 through Noncanonical Structural Motifs**
ChemBioChem
(2020)
22
232
(doi: 10.1002/cbic.202000585)
Disorder in a two-domain neuronal Ca2+-binding protein regulates domain stability and dynamics using ligand mimicry.
Cell Mol Life Sci
(2020)
78
2263
(doi: 10.1007/s00018-020-03639-z)
The folding and unfolding behavior of ribonuclease H on the ribosome.
J Biol Chem
(2020)
295
11410
(doi: 10.1074/jbc.RA120.013909)
Spontaneous oligomerization of BAK/BAX is suppressed by hetero-dimerization with MCL-1
(2019)
756874
(doi: 10.1101/756874)
Extrinsic conditions influence the self-association and structure of IF1, the regulatory protein of mitochondrial ATP synthase
Proc Natl Acad Sci U S A
(2019)
116
10354
(doi: 10.1073/pnas.1903535116)
Adaptation of Proteins to the Cold in Antarctic Fish: A Role for Methionine?
Genome biology and evolution
(2019)
11
220
(doi: 10.1093/gbe/evy262)
The Folding Pathway of an Ig Domain is Conserved On and Off the Ribosome
Proc Natl Acad Sci U S A
(2018)
115
E11284
(doi: 10.1073/pnas.1810523115)
Non-Native Cooperative Interactions Modulate Protein Folding Rates
The journal of physical chemistry. B
(2018)
122
10817
(doi: 10.1021/acs.jpcb.8b08990)
Investigating the Effect of Chain Connectivity on the Folding of a Beta-Sheet Protein On and Off the Ribosome
J Mol Biol
(2018)
430
5207
(doi: 10.1016/j.jmb.2018.10.011)
Promiscuous and selective: how intrinsically disordered BH3- proteins interact with their pro-survival partner MCL-1.
J Mol Biol
(2018)
430
2468
(doi: 10.1016/j.jmb.2018.04.004)
Folding and binding pathways of BH3-only proteins are encoded within their intrinsically disordered sequence, not templated by partner proteins.
J Biol Chem
(2018)
293
9718
(doi: 10.1074/jbc.ra118.002791)
Protein-peptide association kinetics beyond the seconds timescale from atomistic simulations (vol 8, 2017)
Nature Communications
(2018)
9
1073
(doi: 10.1038/s41467-018-03452-0)
Conservation of Folding Mechanism in Cotranslational Folding of Titin I27
Biophysical Journal
(2018)
114
593A
(doi: 10.1016/j.bpj.2017.11.3242)
Phosphorylation of the IDP KID Modulates Affinity for KIX by Increasing the Lifetime of the Complex.
Biophysical Journal
(2017)
113
2706
(doi: 10.1016/j.bpj.2017.10.015)
pKID Binds to KIX via an Unstructured Transition State with Nonnative Interactions.
Biophys J
(2017)
113
2713
(doi: 10.1016/j.bpj.2017.10.016)
Protein-peptide association kinetics beyond the seconds timescale from atomistic simulations.
Nature Communications
(2017)
8
1095
(doi: 10.1038/s41467-017-01163-6)
Affinity of IDPs to their targets is modulated by ion-specific changes in kinetics and residual structure.
Proc Natl Acad Sci U S A
(2017)
114
9882
(doi: 10.1073/pnas.1705105114)
Conserved Helix-Flanking Prolines Modulate Intrinsically Disordered Protein:Target Affinity by Altering the Lifetime of the Bound Complex
Biochemistry
(2017)
56
2379
(doi: 10.1021/acs.biochem.7b00179)
Role of non-native electrostatic interactions in the coupled folding and binding of PUMA with Mcl-1.
PLoS computational biology
(2017)
13
e1005468
(doi: 10.1371/journal.pcbi.1005468)
Cotranslational folding of spectrin domains via partially structured states
Nature structural & molecular biology
(2017)
24
221
(doi: 10.1038/nsmb.3355)