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Results: 1 to 20 of 166

1.

An overview of the serpin superfamily.

Law RH, Zhang Q, McGowan S, Buckle AM, Silverman GA, Wong W, Rosado CJ, Langendorf CG, Pike RN, Bird PI, Whisstock JC.

Genome Biol. 2006;7(5):216. Epub 2006 May 30. Review.

PMID:
16737556
[PubMed - indexed for MEDLINE]
Free PMC Article
2.

The native metastability and misfolding of serine protease inhibitors.

Cho YL, Chae YK, Jung CH, Kim MJ, Na YR, Kim YH, Kang SJ, Im H.

Protein Pept Lett. 2005 Jul;12(5):477-81. Review.

PMID:
16029161
[PubMed - indexed for MEDLINE]
3.

The role of serpins in vertebrate immunity.

Mangan MS, Kaiserman D, Bird PI.

Tissue Antigens. 2008 Jul;72(1):1-10. doi: 10.1111/j.1399-0039.2008.01059.x. Epub 2008 May 20. Review.

PMID:
18498291
[PubMed - indexed for MEDLINE]
4.

Conformational properties of serine proteinase inhibitors (serpins) confer multiple pathophysiological roles.

Janciauskiene S.

Biochim Biophys Acta. 2001 Mar 26;1535(3):221-35. Review.

PMID:
11278163
[PubMed - indexed for MEDLINE]
Free Article
5.

Tip of another iceberg: Drosophila serpins.

Reichhart JM.

Trends Cell Biol. 2005 Dec;15(12):659-65. Epub 2005 Nov 2. Review.

PMID:
16260136
[PubMed - indexed for MEDLINE]
6.

Serpins: finely balanced conformational traps.

Pike RN, Bottomley SP, Irving JA, Bird PI, Whisstock JC.

IUBMB Life. 2002 Jul;54(1):1-7. Review.

PMID:
12387568
[PubMed - indexed for MEDLINE]
7.
8.

Serpins and other covalent protease inhibitors.

Ye S, Goldsmith EJ.

Curr Opin Struct Biol. 2001 Dec;11(6):740-5. Review.

PMID:
11751056
[PubMed - indexed for MEDLINE]
9.

Human clade B serpins (ov-serpins) belong to a cohort of evolutionarily dispersed intracellular proteinase inhibitor clades that protect cells from promiscuous proteolysis.

Silverman GA, Whisstock JC, Askew DJ, Pak SC, Luke CJ, Cataltepe S, Irving JA, Bird PI.

Cell Mol Life Sci. 2004 Feb;61(3):301-25. Review.

PMID:
14770295
[PubMed - indexed for MEDLINE]
10.

The role of conformational change in serpin structure and function.

Gettins P, Patston PA, Schapira M.

Bioessays. 1993 Jul;15(7):461-7. Review.

PMID:
8379949
[PubMed - indexed for MEDLINE]
11.

The 1.5 A crystal structure of a prokaryote serpin: controlling conformational change in a heated environment.

Irving JA, Cabrita LD, Rossjohn J, Pike RN, Bottomley SP, Whisstock JC.

Structure. 2003 Apr;11(4):387-97.

PMID:
12679017
[PubMed - indexed for MEDLINE]
Free Article
12.

Aeropin from the extremophile Pyrobaculum aerophilum bypasses the serpin misfolding trap.

Cabrita LD, Irving JA, Pearce MC, Whisstock JC, Bottomley SP.

J Biol Chem. 2007 Sep 14;282(37):26802-9. Epub 2007 Jul 16.

PMID:
17635906
[PubMed - indexed for MEDLINE]
Free Article
13.

A protein family under 'stress' - serpin stability, folding and misfolding.

Devlin GL, Bottomley SP.

Front Biosci. 2005 Jan 1;10:288-99. Print 2005 Jan 1. Review.

PMID:
15574369
[PubMed - indexed for MEDLINE]
14.

Control of the coagulation system by serpins. Getting by with a little help from glycosaminoglycans.

Pike RN, Buckle AM, le Bonniec BF, Church FC.

FEBS J. 2005 Oct;272(19):4842-51. Review.

PMID:
16176258
[PubMed - indexed for MEDLINE]
Free Article
15.

Focus on molecules: maspin.

Narayan M, Twining S.

Exp Eye Res. 2010 Jan;90(1):2-3. doi: 10.1016/j.exer.2009.07.003. Epub 2009 Jul 15. No abstract available.

PMID:
19615364
[PubMed - indexed for MEDLINE]
Free PMC Article
16.

Different conformational changes within the F-helix occur during serpin folding, polymerization, and proteinase inhibition.

Cabrita LD, Dai W, Bottomley SP.

Biochemistry. 2004 Aug 3;43(30):9834-9.

PMID:
15274637
[PubMed - indexed for MEDLINE]
17.

The molecular aetiology of the serpinopathies.

Davies MJ, Lomas DA.

Int J Biochem Cell Biol. 2008;40(6-7):1273-86. doi: 10.1016/j.biocel.2007.12.017. Epub 2008 Jan 17. Review.

PMID:
18289918
[PubMed - indexed for MEDLINE]
18.

The serpin-proteinase complex revealed.

Lawrence DA.

Nat Struct Biol. 1997 May;4(5):339-41. No abstract available.

PMID:
9145100
[PubMed - indexed for MEDLINE]
19.

Structure of a serpin-protease complex shows inhibition by deformation.

Huntington JA, Read RJ, Carrell RW.

Nature. 2000 Oct 19;407(6806):923-6.

PMID:
11057674
[PubMed - indexed for MEDLINE]
20.

Analysis of surface cavity in serpin family reveals potential binding sites for chemical chaperone to reduce polymerization.

Singh P, Khan MS, Naseem A, Jairajpuri MA.

J Mol Model. 2012 Mar;18(3):1143-51. doi: 10.1007/s00894-011-1110-8. Epub 2011 Jun 17.

PMID:
21681443
[PubMed - indexed for MEDLINE]

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