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- Currently displaying 1501 - 1520 of 2456 publications
Chemical site-selective radiolabelling of proteins using fluorosugars
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(2012)
243
Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomers.
Journal of Cell Science
(2012)
125
2416
(doi: 10.1242/jcs.098434)
The nature and significance of protein aggregation phenomena
PRION
(2012)
6
10
The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide.
Nature Structural & Molecular Biology
(2012)
19
79
(doi: 10.1038/nsmb.2191)
Selenenylsulfide-linked homogeneous glycopeptides and glycoproteins: synthesis of human "hepatic Se metabolite A".
Angew Chem Int Ed Engl
(2011)
51
1432
(doi: 10.1002/anie.201106658)
A traceless vascular-targeting antibody-drug conjugate for cancer therapy
Angew. Chem. Int. Ed.
(2011)
51
941
(doi: 10.1002/anie.201106527)
Hydrophobicity and Conformational Change as Mechanistic Determinants for Nonspecific Modulators of Amyloid beta Self-Assembly
Biochemistry
(2011)
51
126
(doi: 10.1021/bi201745g)
Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility.
Proc Natl Acad Sci U S A
(2011)
108
21057
(doi: 10.1073/pnas.1112197108)
Sequence-based prediction of protein solubility.
Journal of molecular biology
(2011)
421
237
(doi: 10.1016/j.jmb.2011.12.005)
Clusterin facilitates in vivo clearance of extracellular misfolded proteins
Cellular and Molecular Life Sciences
(2011)
68
3919
(doi: 10.1007/s00018-011-0684-8)
Protein solubility and protein homeostasis: A generic view of protein misfolding disorders
Cold Spring Harbor Perspectives in Biology
(2011)
3
(doi: 10.1101/cshperspect.a010454)
Determination of conformational equilibria in proteins using residual dipolar couplings
Journal of chemical theory and computation
(2011)
7
4189
(doi: 10.1021/ct200361b)
Coarse-grained model for protein folding based on structural profiles
Physical Review E Statistical Nonlinear and Soft Matter Physics
(2011)
84
041934
(doi: 10.1103/physreve.84.041934)
Coarse-grained model for protein folding based on structural profiles.
Physical review. E, Statistical, nonlinear, and soft matter physics
(2011)
84
041934
(doi: 10.1103/PhysRevE.84.041934)
Probing small molecule binding to amyloid fibrils
Phys Chem Chem Phys
(2011)
13
20044
(doi: 10.1039/c1cp22283j)
Inversion of the Balance between Hydrophobic and Hydrogen Bonding Interactions in Protein Folding and Aggregation.
PLoS Computational Biology
(2011)
7
e1002169
(doi: 10.1371/journal.pcbi.1002169)
Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongation.
Biophys J
(2011)
101
1681
(doi: 10.1016/j.bpj.2011.07.056)
Using SideāChain Aromatic Proton Chemical Shifts for a Quantitative Analysis of Protein Structures
Angewandte Chemie International Edition
(2011)
50
9620
(doi: 10.1002/anie.201101641)
Using side-chain aromatic proton chemical shifts for a quantitative analysis of protein structures
Angewandte Chemie International Edition
(2011)
50
9620
(doi: 10.1002/anie.201101641)