Department of Chemistry

Michele Vendruscolo Publications (2010)


Focus on physical principles of protein behavior in the cell.
Porto M, Roman HE, Vendruscolo M
Proteomics, 2010-12, 23, 4149-4150. DOI: 10.1002/pmic.201090102


Interactions in the native state of monellin, which play a protective role against aggregation.
Szczepankiewicz O, Cabaleiro-Lago C, Tartaglia GG, Vendruscolo M, Hunter T, Hunter GJ, Nilsson H, Thulin E, Linse S
Mol Biosyst, 2011-02, 2, 521-532. DOI: 10.1039/C0MB00155D


Structural characterization of a misfolded intermediate populated during the folding process of a PDZ domain.
Gianni S, Ivarsson Y, De Simone A, Travaglini-Allocatelli C, Brunori M, Vendruscolo M
Nat Struct Mol Biol, 2010-12, 12, 1431-1437. DOI: 10.1038/nsmb.1956


Transient tertiary structure formation within the ribosome exit port.
O'Brien EP, Hsu ST, Christodoulou J, Vendruscolo M, Dobson CM
J Am Chem Soc, 2010, 47, 16928-16937. DOI: 10.1021/ja106530y


Derivation of a solubility condition for proteins from an analysis of the competition between folding and aggregation.
Pechmann S, Vendruscolo M
Mol Biosyst, 2010-12, 12, 2490-2497. DOI: 10.1039/C005160H


Proteome-level interplay between folding and aggregation propensities of proteins.
Tartaglia GG, Vendruscolo M
J Mol Biol, 2010, 5, 919-928. DOI: 10.1016/j.jmb.2010.08.013


Accurate determination of interstrand distances and alignment in amyloid fibrils by magic angle spinning NMR.
Caporini MA, Bajaj VS, Veshtort M, Fitzpatrick A, MacPhee CE, Vendruscolo M, Dobson CM, Griffin RG
J Phys Chem B, 2010, 42, 13555-13561. DOI: 10.1021/jp106675h


Translationally optimal codons associate with aggregation-prone sites in proteins.
Lee Y, Zhou T, Tartaglia GG, Vendruscolo M, Wilke CO
Proteomics, 2010-12, 23, 4163-4171. DOI: 10.1002/pmic.201000229


Enzymatic activity in disordered states of proteins.
Vendruscolo M
Curr Opin Chem Biol, 2010-10, 5, 671-675. DOI: 10.1016/j.cbpa.2010.08.022


Functional interactions as a survival strategy against abnormal aggregation.
Masino L, Nicastro G, Calder L, Vendruscolo M, Pastore A
FASEB J, 2011-01, 1, 45-54. DOI: 10.1096/fj.10-161208


Using NMR chemical shifts as structural restraints in molecular dynamics simulations of proteins.
Robustelli P, Kohlhoff K, Cavalli A, Vendruscolo M
Structure, 2010, 8, 923-933. DOI: 10.1016/j.str.2010.04.016


Physicochemical determinants of chaperone requirements.
Tartaglia GG, Dobson CM, Hartl FU, Vendruscolo M
J Mol Biol, 2010, 3, 579-588. DOI: 10.1016/j.jmb.2010.03.066


The tube model in Gromacs: a platform for the study of protein folding and aggregation
Sandal M, Vendruscolo M
FEBS JOURNAL, 2010-06, 257-257.


An algorithm and experimental protocol to obtain the kinetic parameters of fibrillar growth from a first-principles general model of breakable filament assembly
Cohen SI, Sandal M, Rajah L, Dobson CM, Vendruscolo M, Knowles TPJ
FEBS JOURNAL, 2010-06, 257-257.


Time averaging of NMR chemical shifts in the MLF peptide in the solid state.
De Gortari I, Portella G, Salvatella X, Bajaj VS, van der Wel PC, Yates JR, Segall MD, Pickard CJ, Payne MC, Vendruscolo M
J Am Chem Soc, 2010, 17, 5993-6000. DOI: 10.1021/ja9062629


Intrinsic determinants of neurotoxic aggregate formation by the amyloid beta peptide.
Brorsson AC, Bolognesi B, Tartaglia GG, Shammas SL, Favrin G, Watson I, Lomas DA, Chiti F, Vendruscolo M, Dobson CM, Crowther DC, Luheshi LM
Biophys J, 2010, 8, 1677-1684. DOI: 10.1016/j.bpj.2009.12.4320


Effects of disease-associated mutations on the aggregation process of the 93-residue N-terminal fragment of human apolipoprotein A-I
Raimondi S, Guglielmi F, Giorgetti S, Di Gaetano S, Arciello A, Relini A, Doglia SM, Natalello A, Pucci P, Mangione P, Obici L, Merlini G, Stoppini M, Tartaglia GG, Vendruscolo M, Piccoli R, Bellotti V
AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS, 2010-04, 39-40.


Efficient identification of near-native conformations in ab initio protein structure prediction using structural profiles.
Wolff K, Vendruscolo M, Porto M
Proteins, 2010, 2, 249-258. DOI: 10.1002/prot.22533