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- Currently displaying 1401 - 1420 of 2508 publications
Single‐Molecule Imaging Reveals that Small Amyloid‐β1–42 Oligomers Interact with the Cellular Prion Protein (PrPC)
Chembiochem
(2014)
15
2515
(doi: 10.1002/cbic.201402377)
Cysteine-selective reactions for antibody conjugation
Angewandte Chemie International Edition
(2014)
53
10585
(doi: 10.1002/anie.201405702)
Understanding the frustration arising from the competition between function, misfolding, and aggregation in a globular protein.
Proceedings of the National Academy of Sciences of the United States of America
(2014)
111
14141
(doi: 10.1073/pnas.1405233111)
Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation.
J Biol Chem
(2014)
289
31066
(doi: 10.1074/jbc.M114.595124)
Identification and characterization of PKCPγ, a kinase associated with SCA14, as an amyloidogenic protein
Hum Mol Genet
(2014)
24
525
(doi: 10.1093/hmg/ddu472)
Equilibrium simulations of proteins using molecular fragment replacement and NMR chemical shifts.
Proceedings of the National Academy of Sciences
(2014)
111
13852
(doi: 10.1073/pnas.1404948111)
NMR characterization of the conformational fluctuations of the human lymphocyte function‐associated antigen‐1 I‐domain
Protein Science
(2014)
23
1596
(doi: 10.1002/pro.2538)
Antibodies and protein misfolding: From structural research tools to therapeutic strategies
Biochimica et biophysica acta
(2014)
1844
1907
(doi: 10.1016/j.bbapap.2014.08.016)
The physical chemistry of the amyloid phenomenon: thermodynamics and kinetics of filamentous protein aggregation.
Essays in Biochemistry
(2014)
56
11
(doi: 10.1042/BSE0560011)
Highlights from the 49th EUCHEM Conference on Stereochemistry, Burgenstock, Switzerland, May 2014
Chemical Communications
(2014)
50
10752
(doi: 10.1039/c4cc90250e)
Toxicity of Protein Oligomers Is Rationalized by a Function Combining Size and Surface Hydrophobicity
ACS Chemical Biology
(2014)
9
2309
(doi: 10.1021/cb500505m)
Archaeal MBF1 binds to 30S and 70S ribosomes via its helix–turn–helix domain
Biochem J
(2014)
462
373
(doi: 10.1042/BJ20131474)
Carbon-monoxide-releasing molecules for the delivery of therapeutic co in vivo
Angewandte Chemie (International ed. in English)
(2014)
53
9712
(doi: 10.1002/anie.201311225)
Easyworm: an open-source software tool to determine the mechanical properties of worm-like chains
Source Code for Biology and Medicine
(2014)
9
16
(doi: 10.1186/1751-0473-9-16)
Amyloid Beta Peptide Aβ40 and Aβ42 Form Separate Fibrils in Binary Mixtures
PROTEIN SCIENCE
(2014)
23
79
Cyclophilin A catalyzes proline isomerization by an electrostatic handle mechanism.
Proceedings of the National Academy of Sciences of the United States of America
(2014)
111
10203
(doi: 10.1073/pnas.1404220111)
Statistical Mechanics of the Denatured State of a Protein Using Replica-Averaged Metadynamics
J Am Chem Soc
(2014)
136
8982
(doi: 10.1021/ja5027584)
Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides
Proceedings of the National Academy of Sciences of the United States of America
(2014)
111
9384
(doi: 10.1073/pnas.1401564111)
The amyloid state and its association with protein misfolding diseases (vol 15, pg 384, 2014)
Nature Reviews Molecular Cell Biology
(2014)
15
496
(doi: 10.1038/nrm3826)
A tensor-free method for the structural and dynamical refinement of proteins using residual dipolar couplings
J Phys Chem B
(2014)
119
653
(doi: 10.1021/jp5021824)