Detalhe da pesquisa
1.
The non-prion SUP35 preexists in large chaperone-containing molecular complexes.
Proteins
; 90(3): 869-880, 2022 03.
Artigo
em Inglês
| MEDLINE | ID: mdl-34791707
2.
On the utility of fluorescence-detection analytical ultracentrifugation in probing biomolecular interactions in complex solutions: a case study in milk.
Eur Biophys J
; 49(8): 677-685, 2020 Dec.
Artigo
em Inglês
| MEDLINE | ID: mdl-33052462
3.
Defining the protein complexome of translation termination factor eRF1: Identification of four novel eRF1-containing complexes that range from 20S to 57S in size.
Proteins
; 86(2): 177-191, 2018 02.
Artigo
em Inglês
| MEDLINE | ID: mdl-29139201
4.
Sedimentation Velocity Analysis with Fluorescence Detection of Mutant Huntingtin Exon 1 Aggregation in Drosophila melanogaster and Caenorhabditis elegans.
Biochemistry
; 56(35): 4676-4688, 2017 09 05.
Artigo
em Inglês
| MEDLINE | ID: mdl-28786671
5.
The Charge Properties of Phospholipid Nanodiscs.
Biophys J
; 111(5): 989-98, 2016 Sep 06.
Artigo
em Inglês
| MEDLINE | ID: mdl-27602726
6.
Influence of Phosphatidylcholine and Calcium on Self-Association and Bile Salt Mixed Micellar Binding of the Natural Bile Pigment, Bilirubin Ditaurate.
Biochemistry
; 54(45): 6783-95, 2015 Nov 17.
Artigo
em Inglês
| MEDLINE | ID: mdl-26506107
7.
Self-assembly of aqueous bilirubin ditaurate, a natural conjugated bile pigment, to contraposing enantiomeric dimers and M(-) and P(+) tetramers and their selective hydrophilic disaggregation by monomers and micelles of bile salts.
Biochemistry
; 54(7): 1542-57, 2015 Feb 24.
Artigo
em Inglês
| MEDLINE | ID: mdl-25671490
8.
Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity.
Cancer Cell
; 11(6): 483-97, 2007 Jun.
Artigo
em Inglês
| MEDLINE | ID: mdl-17560331
9.
Characterization of conformational changes and protein-protein interactions of rod photoreceptor phosphodiesterase (PDE6).
J Biol Chem
; 287(24): 20111-21, 2012 Jun 08.
Artigo
em Inglês
| MEDLINE | ID: mdl-22514270
10.
The RRM1 domain of the poly(A)-binding protein from Saccharomyces cerevisiae is critical to control of mRNA deadenylation.
Mol Genet Genomics
; 288(9): 401-12, 2013 Sep.
Artigo
em Inglês
| MEDLINE | ID: mdl-23793387
11.
Differential temperature-dependent multimeric assemblies of replication and repair polymerases on DNA increase processivity.
Biochemistry
; 51(37): 7367-82, 2012 Sep 18.
Artigo
em Inglês
| MEDLINE | ID: mdl-22906116
12.
Detection of high-molecular-weight amyloid serum protein complexes using biological on-line tracer sedimentation.
Anal Biochem
; 425(2): 151-6, 2012 Jun 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-22465331
13.
Effect of PEGylation on protein hydrodynamics.
Mol Pharm
; 9(4): 762-73, 2012 Apr 02.
Artigo
em Inglês
| MEDLINE | ID: mdl-22353017
14.
The influence of charge distribution on self-association and viscosity behavior of monoclonal antibody solutions.
Mol Pharm
; 9(4): 791-802, 2012 Apr 02.
Artigo
em Inglês
| MEDLINE | ID: mdl-22352470
15.
Use of Debye-Hückel-Henry charge measurements in early antibody development elucidates effects of non-specific association.
Antib Ther
; 5(3): 211-215, 2022 Jul.
Artigo
em Inglês
| MEDLINE | ID: mdl-35983303
16.
Multiple conformations of the cytidine repressor DNA-binding domain coalesce to one upon recognition of a specific DNA surface.
Biochemistry
; 50(31): 6622-32, 2011 Aug 09.
Artigo
em Inglês
| MEDLINE | ID: mdl-21688840
17.
The sedimentation properties of ferritins. New insights and analysis of methods of nanoparticle preparation.
Biochim Biophys Acta
; 1800(8): 858-70, 2010 Aug.
Artigo
em Inglês
| MEDLINE | ID: mdl-20307627
18.
The Open AUC Project.
Eur Biophys J
; 39(3): 347-59, 2010 Feb.
Artigo
em Inglês
| MEDLINE | ID: mdl-19296095
19.
PAB1 self-association precludes its binding to poly(A), thereby accelerating CCR4 deadenylation in vivo.
Mol Cell Biol
; 27(17): 6243-53, 2007 Sep.
Artigo
em Inglês
| MEDLINE | ID: mdl-17620415
20.
The Molecular Interaction Process.
J Pharm Sci
; 109(1): 154-160, 2020 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-31676268