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- Currently displaying 1301 - 1320 of 2453 publications
The s2D method: Simultaneous sequence-based prediction of the statistical populations of ordered and disordered regions in proteins
Journal of Molecular Biology
(2015)
427
982
(doi: 10.1016/j.jmb.2014.12.007)
Chaperoned amyloid proteins for immune manipulation: αâSynuclein/Hsp70 shifts immunity toward a modulatory phenotype
Immunity Inflammation and Disease
(2015)
2
226
(doi: 10.1002/iid3.39)
The CamSol method of rational design of protein mutants with enhanced solubility
Journal of Molecular Biology
(2015)
427
478
(doi: 10.1016/j.jmb.2014.09.026)
Analysis of the hierarchical structure of the B. subtilis transcriptional regulatory network.
Molecular bioSystems
(2015)
11
930
(doi: 10.1039/c4mb00298a)
Structure of a low-population intermediate state in the release of an enzyme product.
Elife
(2015)
4
e02777
(doi: 10.7554/eLife.02777)
Kinetics of protein aggregation
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2015)
44
S98
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2015)
44
S101
Rapid sizing of proteins in complex solutions
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2015)
44
S49
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation
Nature Chemical Biology
(2015)
11
229
(doi: 10.1038/nchembio.1750)
Biophysical approaches for the study of interactions between molecular chaperones and protein aggregates.
Chemical communications (Cambridge, England)
(2015)
51
14425
(doi: 10.1039/c5cc03689e)
On the lag phase in amyloid fibril formation.
Physical chemistry chemical physics : PCCP
(2015)
17
7606
(doi: 10.1039/c4cp05563b)
Supersaturation is a major driving force for protein aggregation in neurodegenerative diseases
Trends in Pharmacological Sciences
(2015)
36
72
(doi: 10.1016/j.tips.2014.12.004)
A high power-density, mediator-free, microfluidic biophotovoltaic device for cyanobacterial cells
Advanced Energy Materials
(2015)
5
(doi: 10.1002/aenm.201401299)
Structural characterization of toxic oligomers that are kinetically trapped during alpha-synuclein fibril formation
PROTEIN SCIENCE
(2015)
24
136
Functionalized protein nanoemulsions by incorporation of chemically modified BSA
Rsc Advances
(2015)
5
4976
(doi: 10.1039/c4ra13802c)
The Computational Studies of Co-Translational Protein Folding
Biophysical Journal
(2015)
108
515A
(doi: 10.1016/j.bpj.2014.11.2823)
A microfluidic platform for quantitative measurements of effective protein charges and single ion binding in solution
Physical Chemistry Chemical Physics
(2015)
17
12161
(doi: 10.1039/c5cp00746a)
Thioflavin-T: application for α-synuclein aggregation kinetics
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2015)
44
S99