Detalhe da pesquisa
1.
Atomic Resolution Insights into pH Shift Induced Deprotonation Events in LS-Shaped Aß(1-42) Amyloid Fibrils.
J Am Chem Soc
; 145(4): 2161-2169, 2023 02 01.
Artigo
Inglês
| MEDLINE | ID: mdl-36653015
2.
Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation.
Cell
; 134(5): 793-803, 2008 Sep 05.
Artigo
Inglês
| MEDLINE | ID: mdl-18775312
3.
Structural details of amyloid ß oligomers in complex with human prion protein as revealed by solid-state MAS NMR spectroscopy.
J Biol Chem
; 296: 100499, 2021.
Artigo
Inglês
| MEDLINE | ID: mdl-33667547
4.
A d-enantiomeric peptide interferes with heteroassociation of amyloid-ß oligomers and prion protein.
J Biol Chem
; 293(41): 15748-15764, 2018 10 12.
Artigo
Inglês
| MEDLINE | ID: mdl-30131337
5.
Proton exchange in aqueous urea solutions measured by water-exchange (WEX) NMR spectroscopy and chemical exchange saturation transfer (CEST) imaging in vitro.
Magn Reson Med
; 82(3): 935-947, 2019 09.
Artigo
Inglês
| MEDLINE | ID: mdl-31004385
6.
High-Affinity Binding of Monomeric but Not Oligomeric Amyloid-ß to Ganglioside GM1 Containing Nanodiscs.
Biochemistry
; 55(48): 6662-6672, 2016 Dec 06.
Artigo
Inglês
| MEDLINE | ID: mdl-27933798
7.
The Nedd4-1 WW Domain Recognizes the PY Motif Peptide through Coupled Folding and Binding Equilibria.
Biochemistry
; 55(4): 659-74, 2016 Feb 02.
Artigo
Inglês
| MEDLINE | ID: mdl-26685112
8.
Structure and dynamics of human Nedd4-1 WW3 in complex with the αENaC PY motif.
Biochim Biophys Acta
; 1834(8): 1632-41, 2013 Aug.
Artigo
Inglês
| MEDLINE | ID: mdl-23665454
9.
Phages have adapted the same protein fold to fulfill multiple functions in virion assembly.
Proc Natl Acad Sci U S A
; 107(32): 14384-9, 2010 Aug 10.
Artigo
Inglês
| MEDLINE | ID: mdl-20660769
10.
Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding.
Proc Natl Acad Sci U S A
; 105(29): 9999-10004, 2008 Jul 22.
Artigo
Inglês
| MEDLINE | ID: mdl-18626019
11.
Determination of isoleucine side-chain conformations in ground and excited states of proteins from chemical shifts.
J Am Chem Soc
; 132(22): 7589-91, 2010 Jun 09.
Artigo
Inglês
| MEDLINE | ID: mdl-20465253
12.
Structural properties and dynamic behavior of nonfibrillar oligomers formed by PrP(106-126).
J Am Chem Soc
; 132(22): 7684-95, 2010 Jun 09.
Artigo
Inglês
| MEDLINE | ID: mdl-20465257
13.
Determination of Leu side-chain conformations in excited protein states by NMR relaxation dispersion.
J Am Chem Soc
; 132(1): 42-3, 2010 Jan 13.
Artigo
Inglês
| MEDLINE | ID: mdl-20000605
14.
Mutational investigation of protein folding transition states by Phi-value analysis and beyond: lessons from SH3 domain folding.
Biochem Cell Biol
; 88(2): 231-8, 2010 Apr.
Artigo
Inglês
| MEDLINE | ID: mdl-20453926
15.
A simple method for measuring signs of (1)H (N) chemical shift differences between ground and excited protein states.
J Biomol NMR
; 47(2): 135-41, 2010 Jun.
Artigo
Inglês
| MEDLINE | ID: mdl-20428928
16.
Measurement of signs of chemical shift differences between ground and excited protein states: a comparison between H(S/M)QC and R1rho methods.
J Biomol NMR
; 46(3): 205-16, 2010 Mar.
Artigo
Inglês
| MEDLINE | ID: mdl-20033258
17.
Clustering of human prion protein and α-synuclein oligomers requires the prion protein N-terminus.
Commun Biol
; 3(1): 365, 2020 07 09.
Artigo
Inglês
| MEDLINE | ID: mdl-32647130
18.
TopModel: Template-Based Protein Structure Prediction at Low Sequence Identity Using Top-Down Consensus and Deep Neural Networks.
J Chem Theory Comput
; 16(3): 1953-1967, 2020 Mar 10.
Artigo
Inglês
| MEDLINE | ID: mdl-31967823
19.
Relaxation dispersion NMR spectroscopy as a tool for detailed studies of protein folding.
Biophys J
; 96(6): 2045-54, 2009 Mar 18.
Artigo
Inglês
| MEDLINE | ID: mdl-19289032
20.
Measuring the signs of 1H(alpha) chemical shift differences between ground and excited protein states by off-resonance spin-lock R(1rho) NMR spectroscopy.
J Am Chem Soc
; 131(31): 10832-3, 2009 Aug 12.
Artigo
Inglês
| MEDLINE | ID: mdl-19606858