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- Currently displaying 1241 - 1260 of 2455 publications
Preventing peptide and protein misbehavior.
Proc Natl Acad Sci U S A
(2015)
112
5267
(doi: 10.1073/pnas.1505170112)
Investigating the Mechanisms of Amylolysis of Starch Granules by Solution-State NMR
Biomacromolecules
(2015)
16
1614
(doi: 10.1021/acs.biomac.5b00190)
Structural characterization of toxic oligomers that are kinetically trapped during alpha-synuclein fibril formation
Proceedings of the National Academy of Sciences
(2015)
112
E1994
(doi: 10.1073/pnas.1421204112.)
Structure of a Single-Chain Fv Bound to the 17 N-Terminal Residues of Huntingtin Provides Insights into Pathogenic Amyloid Formation and Suppression
Journal of molecular biology
(2015)
427
2166
(doi: 10.1016/j.jmb.2015.03.021)
Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation.
Proceedings of the National Academy of Sciences
(2015)
112
E1994
(doi: 10.1073/pnas.1421204112)
Folic acid-tagged protein nanoemulsions loaded with CORM-2 enhance the survival of mice bearing subcutaneous A20 lymphoma tumors.
Nanomedicine: Nanotechnology, Biology and Medicine
(2015)
11
1077
(doi: 10.1016/j.nano.2015.02.022)
Structure and dynamics of the integrin LFA-1 I-domain in the inactive state underlie its inside-out/outside-in signaling and allosteric mechanisms.
Structure
(2015)
23
745
(doi: 10.1016/j.str.2014.12.020)
A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers.
Nature Structural and Molecular Biology
(2015)
22
207
(doi: 10.1038/nsmb.2971)
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: α-Synuclein/Hsp70 shifts immunity toward a modulatory phenotype.
Immunity, inflammation and disease
(2015)
2
226
(doi: 10.1002/iid3.39)
A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers
Nature Structural & Molecular Biology
(2015)
22
207
(doi: 10.1038/nsmb.2971)
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation
Nature chemical biology
(2015)
11
229
(doi: 10.1038/nchembio.1750)
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)
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)
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)
The Computational Studies of Co-Translational Protein Folding
Biophysical Journal
(2015)
108
515a
(doi: 10.1016/j.bpj.2014.11.2823)