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- Currently displaying 1341 - 1360 of 2338 publications
Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers
Proceedings of the National Academy of Sciences
(2012)
109
12479
(doi: 10.1073/pnas.1117799109)
Nanobodies as structural probes of protein misfolding and fibril formation.
Methods in molecular biology (Clifton, N.J.)
(2012)
911
533
(doi: 10.1007/978-1-61779-968-6_34)
Rapid distinction of intracellular and extracellular proteins using NMR diffusion measurements
Journal of the American Chemical Society
(2012)
134
11312
(doi: 10.1021/ja304912c)
Generation of carbon monoxide releasing molecules (CO-RMs) as drug candidates for the treatment of acute liver injury: Targeting of CO-RMs to the liver
Organometallics
(2012)
31
5810
(doi: 10.1021/om300360c)
Determination of structural fluctuations of proteins from structure-based calculations of residual dipolar couplings.
J Biomol NMR
(2012)
53
281
(doi: 10.1007/s10858-012-9644-3)
Trigger factor slows Co-translational folding through kinetic trapping while sterically protecting the nascent chain from aberrant cytosolic interactions
Journal of the American Chemical Society
(2012)
134
10920
(doi: 10.1021/ja302305u)
Fucose-specific conjugation of hydrazide derivatives to a vascular-targeting monoclonal antibody in IgG format
Chem Commun (Camb)
(2012)
48
7100
(doi: 10.1039/c2cc32412a)
Selenium-Enhanced Electron Microscopic Imaging of Different Aggregate Forms of a Segment of the Amyloid β Peptide in Cells
ACS Nano
(2012)
6
4740
(doi: 10.1021/nn204859e)
Characterizing Intermolecular Interactions That Initiate Native-Like Protein Aggregation
Biophysical Journal
(2012)
102
2595
(doi: 10.1016/j.bpj.2012.03.057)
Prediction of variable translation rate effects on cotranslational protein folding.
Nature communications
(2012)
3
868
(doi: 10.1038/ncomms1850)
Direct observation of the interconversion of normal and toxic forms of α-synuclein
Cell
(2012)
149
1048
(doi: 10.1016/j.cell.2012.03.037)
Role of elongation and secondary pathways in S6 amyloid fibril growth.
Biophysical Journal
(2012)
102
2167
(doi: 10.1016/j.bpj.2012.03.047)
Fibrillogenic propensity of the GroEL apical domain: A Janus-faced minichaperone
FEBS Letters
(2012)
586
1120
Structure of an intermediate state in protein folding and aggregation.
Science
(2012)
336
362
(doi: 10.1126/science.1214203)
Intrinsic disorder modulates protein self-assembly and aggregation
Proc Natl Acad Sci U S A
(2012)
109
6951
(doi: 10.1073/pnas.1118048109)
Detailed Analysis of the Energy Barriers for Amyloid Fibril Growth
Angewandte Chemie International Edition
(2012)
51
5247
(doi: 10.1002/anie.201108040)
Analyse der Energiebarrieren für das Wachstum von Amyloidfibrillen
Angewandte Chemie
(2012)
124
5339
(doi: 10.1002/ange.201108040)
1H, 13C and 15N resonance assignments of human muscle acylphosphatase
Biomolecular NMR Assignments
(2012)
6
27
(doi: 10.1007/s12104-011-9318-1)
Proteome folding and aggregation
Current Opinion in Structural Biology
(2012)
22
138
(doi: 10.1016/j.sbi.2012.01.005)
Expression in Drosophila of tandem amyloid β peptides provides insights into links between aggregation and neurotoxicity
Journal of Biological Chemistry
(2012)
287
20748
(doi: 10.1074/jbc.m112.350124)