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- Currently displaying 1321 - 1340 of 2474 publications
Aggregation-Prone Amyloid-β⋅Cu(II) Species Formed on the Millisecond Timescale under Mildly Acidic Conditions.
ChemBioChem
(2015)
16
1293
(doi: 10.1002/cbic.201500080)
Structure and dynamics of GeoCyp: A thermophilic cyclophilin with a novel substrate binding mechanism that functions efficiently at low temperatures
Biochemistry
(2015)
54
3207
(doi: 10.1021/acs.biochem.5b00263)
The Aβ40 and Aβ42 peptides self-assemble into separate homomolecular fibrils in binary mixtures but cross-react during primary nucleation.
Chemical science
(2015)
6
4215
(doi: 10.1039/c4sc02517b)
Widespread Proteome Remodeling and Aggregation in Aging C. elegans
Cell
(2015)
161
919
(doi: 10.1016/j.cell.2015.03.032)
Dynamic interplay between catalytic and lectin domains of GalNAc-transferases modulates protein O-glycosylation
Nature Communications
(2015)
6
6937
(doi: 10.1038/ncomms7937)
A mechanistic model of tau amyloid aggregation based on direct observation of oligomers.
Nat Commun
(2015)
6
7025
(doi: 10.1038/ncomms8025)
The influence of novel gemini surfactants containing cycloalkyl side-chains on the structural phases of DNA in solution
Colloids and Surfaces B Biointerfaces
(2015)
131
83
Preventing peptide and protein misbehavior.
Proceedings of the National Academy of Sciences of the United States of America
(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 α-synuclein fibril formation.
Proceedings of the National Academy of Sciences of the United States of America
(2015)
112
E1994
(doi: 10.1073/pnas.1421204112)
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.)
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)
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)
