179 related articles for article (PubMed ID: 7890640)
1. Preparation and characterization of latent alpha 1-antitrypsin.
Lomas DA; Elliott PR; Chang WS; Wardell MR; Carrell RW
J Biol Chem; 1995 Mar; 270(10):5282-8. PubMed ID: 7890640
[TBL] [Abstract][Full Text] [Related]
2. Preparative induction and characterization of L-antithrombin: a structural homologue of latent plasminogen activator inhibitor-1.
Wardell MR; Chang WS; Bruce D; Skinner R; Lesk AM; Carrell RW
Biochemistry; 1997 Oct; 36(42):13133-42. PubMed ID: 9335576
[TBL] [Abstract][Full Text] [Related]
3. alpha 1-Antitrypsin Mmalton (Phe52-deleted) forms loop-sheet polymers in vivo. Evidence for the C sheet mechanism of polymerization.
Lomas DA; Elliott PR; Sidhar SK; Foreman RC; Finch JT; Cox DW; Whisstock JC; Carrell RW
J Biol Chem; 1995 Jul; 270(28):16864-70. PubMed ID: 7622502
[TBL] [Abstract][Full Text] [Related]
4. 6-mer peptide selectively anneals to a pathogenic serpin conformation and blocks polymerization. Implications for the prevention of Z alpha(1)-antitrypsin-related cirrhosis.
Mahadeva R; Dafforn TR; Carrell RW; Lomas DA
J Biol Chem; 2002 Mar; 277(9):6771-4. PubMed ID: 11773044
[TBL] [Abstract][Full Text] [Related]
5. Secondary structure changes stabilize the reactive-centre cleaved form of SERPINs. A study by 1H nuclear magnetic resonance and Fourier transform infrared spectroscopy.
Perkins SJ; Smith KF; Nealis AS; Haris PI; Chapman D; Bauer CJ; Harrison RA
J Mol Biol; 1992 Dec; 228(4):1235-54. PubMed ID: 1335516
[TBL] [Abstract][Full Text] [Related]
6. Type-1 plasminogen-activator inhibitor -- conformational differences between latent, active, reactive-centre-cleaved and plasminogen-activator-complexed forms, as probed by proteolytic susceptibility.
Egelund R; Schousboe SL; Sottrup-Jensen L; Rodenburg KW; Andreasen PA
Eur J Biochem; 1997 Sep; 248(3):775-85. PubMed ID: 9342229
[TBL] [Abstract][Full Text] [Related]
7. Commercial plasma alpha1-antitrypsin (Prolastin) contains a conformationally inactive, latent component.
Lomas DA; Elliott PR; Carrell RW
Eur Respir J; 1997 Mar; 10(3):672-5. PubMed ID: 9073003
[TBL] [Abstract][Full Text] [Related]
8. Characterization of a human alpha1-antitrypsin variant that is as stable as ovalbumin.
Lee KN; Im H; Kang SW; Yu MH
J Biol Chem; 1998 Jan; 273(5):2509-16. PubMed ID: 9446551
[TBL] [Abstract][Full Text] [Related]
9. The citrate ion increases the conformational stability of alpha(1)-antitrypsin.
Bottomley SP; Tew DJ
Biochim Biophys Acta; 2000 Aug; 1481(1):11-7. PubMed ID: 10962087
[TBL] [Abstract][Full Text] [Related]
10. Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop.
Wei A; Rubin H; Cooperman BS; Christianson DW
Nat Struct Biol; 1994 Apr; 1(4):251-8. PubMed ID: 7656054
[TBL] [Abstract][Full Text] [Related]
11. Polymerization of plasminogen activator inhibitor-1.
Zhou A; Faint R; Charlton P; Dafforn TR; Carrell RW; Lomas DA
J Biol Chem; 2001 Mar; 276(12):9115-22. PubMed ID: 11102455
[TBL] [Abstract][Full Text] [Related]
12. Effect of the Z mutation on the physical and inhibitory properties of alpha 1-antitrypsin.
Lomas DA; Evans DL; Stone SR; Chang WS; Carrell RW
Biochemistry; 1993 Jan; 32(2):500-8. PubMed ID: 8422359
[TBL] [Abstract][Full Text] [Related]
13. Structural factors affecting the choice between latency transition and polymerization in inhibitory serpins.
Yi JY; Im H
Protein Sci; 2007 May; 16(5):833-41. PubMed ID: 17400919
[TBL] [Abstract][Full Text] [Related]
14. Conformational changes of the reactive-centre loop and beta-strand 5A accompany temperature-dependent inhibitor-substrate transition of plasminogen-activator inhibitor 1.
Kjøller L; Martensen PM; Sottrup-Jensen L; Justesen J; Rodenburg KW; Andreasen PA
Eur J Biochem; 1996 Oct; 241(1):38-46. PubMed ID: 8898886
[TBL] [Abstract][Full Text] [Related]
15. Inhibitory conformation of the reactive loop of alpha 1-antitrypsin.
Elliott PR; Lomas DA; Carrell RW; Abrahams JP
Nat Struct Biol; 1996 Aug; 3(8):676-81. PubMed ID: 8756325
[TBL] [Abstract][Full Text] [Related]
16. Crystallography of serpins and serpin complexes.
Dunstone MA; Whisstock JC
Methods Enzymol; 2011; 501():63-87. PubMed ID: 22078531
[TBL] [Abstract][Full Text] [Related]
17. Analysis of the plasma elimination kinetics and conformational stabilities of native, proteinase-complexed, and reactive site cleaved serpins: comparison of alpha 1-proteinase inhibitor, alpha 1-antichymotrypsin, antithrombin III, alpha 2-antiplasmin, angiotensinogen, and ovalbumin.
Mast AE; Enghild JJ; Pizzo SV; Salvesen G
Biochemistry; 1991 Feb; 30(6):1723-30. PubMed ID: 1704258
[TBL] [Abstract][Full Text] [Related]
18. Wild-type alpha 1-antitrypsin is in the canonical inhibitory conformation.
Elliott PR; Abrahams JP; Lomas DA
J Mol Biol; 1998 Jan; 275(3):419-25. PubMed ID: 9466920
[TBL] [Abstract][Full Text] [Related]
19. Conformational changes in serpins: I. The native and cleaved conformations of alpha(1)-antitrypsin.
Whisstock JC; Skinner R; Carrell RW; Lesk AM
J Mol Biol; 2000 Feb; 296(2):685-99. PubMed ID: 10669617
[TBL] [Abstract][Full Text] [Related]
20. Conformational changes in serpins: I. The native and cleaved conformations of alpha(1)-antitrypsin.
Whisstock JC; Skinner R; Carrell RW; Lesk AM
J Mol Biol; 2000 Jan; 295(3):651-65. PubMed ID: 10623554
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
