Detalhe da pesquisa
1.
Role of visual evoked potentials in the assessment and management of optic pathway gliomas in children.
Doc Ophthalmol
; 127(3): 177-90, 2013 Dec.
Artigo
Inglês
| MEDLINE | ID: mdl-23884797
2.
Structural characterisation of apoflavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxin-like topology.
J Mol Biol
; 282(3): 653-66, 1998 Sep 25.
Artigo
Inglês
| MEDLINE | ID: mdl-9737928
3.
(14-38, 30-51) double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: a two-dimensional 1H nuclear magnetic resonance study.
J Mol Biol
; 222(2): 353-71, 1991 Nov 20.
Artigo
Inglês
| MEDLINE | ID: mdl-1960731
4.
Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor.
J Mol Biol
; 222(2): 373-90, 1991 Nov 20.
Artigo
Inglês
| MEDLINE | ID: mdl-1960732
5.
Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitor.
J Mol Biol
; 224(4): 905-11, 1992 Apr 20.
Artigo
Inglês
| MEDLINE | ID: mdl-1373775
6.
Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements.
J Mol Biol
; 229(4): 1125-46, 1993 Feb 20.
Artigo
Inglês
| MEDLINE | ID: mdl-7680380
7.
Local structure due to an aromatic-amide interaction observed by 1H-nuclear magnetic resonance spectroscopy in peptides related to the N terminus of bovine pancreatic trypsin inhibitor.
J Mol Biol
; 230(1): 312-22, 1993 Mar 05.
Artigo
Inglês
| MEDLINE | ID: mdl-7680725
8.
1H NMR analysis of the partly-folded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitor.
J Mol Biol
; 235(3): 1044-61, 1994 Jan 21.
Artigo
Inglês
| MEDLINE | ID: mdl-7507172
9.
Apoflavodoxin (un)folding followed at the residue level by NMR.
Protein Sci
; 9(1): 145-57, 2000 Jan.
Artigo
Inglês
| MEDLINE | ID: mdl-10739257
10.
The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate.
Protein Sci
; 7(11): 2331-44, 1998 Nov.
Artigo
Inglês
| MEDLINE | ID: mdl-9827999
11.
Apparent local stability of the secondary structure of Azotobacter vinelandii holoflavodoxin II as probed by hydrogen exchange: implications for redox potential regulation and flavodoxin folding.
Protein Sci
; 7(2): 306-17, 1998 Feb.
Artigo
Inglês
| MEDLINE | ID: mdl-9521106
12.
The 5-55 single-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor.
FEBS Lett
; 279(1): 61-4, 1991 Feb 11.
Artigo
Inglês
| MEDLINE | ID: mdl-1704858
13.
Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story.
J Biotechnol
; 79(3): 281-98, 2000 May 26.
Artigo
Inglês
| MEDLINE | ID: mdl-10867188
14.
5-fluorotryptophan as dual probe for ground-state heterogeneity and excited-state dynamics in apoflavodoxin.
FEBS Lett
; 583(17): 2785-8, 2009 Sep 03.
Artigo
Inglês
| MEDLINE | ID: mdl-19619543
15.
Three-dimensional correlated NMR study of Megasphaera elsdenii flavodoxin in the oxidized state.
Eur J Biochem
; 195(3): 807-22, 1991 Feb 14.
Artigo
Inglês
| MEDLINE | ID: mdl-1999199
16.
Doubly sensitivity-enhanced 3D TOCSY-HSQC.
J Biomol NMR
; 8(3): 319-30, 1996 Oct.
Artigo
Inglês
| MEDLINE | ID: mdl-20686884
17.
Secondary and tertiary structure characteristics of Megasphaera elsdenii flavodoxin in the reduced state as determined by two-dimensional 1H NMR.
Eur J Biochem
; 189(3): 589-600, 1990 May 20.
Artigo
Inglês
| MEDLINE | ID: mdl-2161759
18.
Solution conformation of a peptide fragment representing a proposed RNA-binding site of a viral coat protein studied by two-dimensional NMR.
Biochemistry
; 30(23): 5722-7, 1991 Jun 11.
Artigo
Inglês
| MEDLINE | ID: mdl-1904274
19.
The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor.
Proc Natl Acad Sci U S A
; 89(15): 6775-9, 1992 Aug 01.
Artigo
Inglês
| MEDLINE | ID: mdl-1379719
20.
Redox properties of wild-type, Cys69Ala, and Cys69Ser Azotobacter vinelandii flavodoxin II as measured by cyclic voltammetry and EPR spectroscopy,.
Eur J Biochem
; 235(1-2): 167-72, 1996 Jan 15.
Artigo
Inglês
| MEDLINE | ID: mdl-8631324