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Items: 1 to 20 of 94

1.

Solution structure of the A4 domain of factor XI sheds light on the mechanism of zymogen activation.

Samuel D, Cheng H, Riley PW, Canutescu AA, Nagaswami C, Weisel JW, Bu Z, Walsh PN, Roder H.

Proc Natl Acad Sci U S A. 2007 Oct 2;104(40):15693-8. Epub 2007 Sep 20.

2.

Crystal structure of the factor XI zymogen reveals a pathway for transactivation.

Papagrigoriou E, McEwan PA, Walsh PN, Emsley J.

Nat Struct Mol Biol. 2006 Jun;13(6):557-8. Epub 2006 May 14.

PMID:
16699514
3.

Dimer dissociation and unfolding mechanism of coagulation factor XI apple 4 domain: spectroscopic and mutational analysis.

Riley PW, Cheng H, Samuel D, Roder H, Walsh PN.

J Mol Biol. 2007 Mar 23;367(2):558-73. Epub 2006 Dec 29.

4.

Factor XI apple domains and protein dimerization.

Cheng Q, Sun MF, Kravtsov DV, Aktimur A, Gailani D.

J Thromb Haemost. 2003 Nov;1(11):2340-7.

5.
6.

Factor XI homodimer structure is essential for normal proteolytic activation by factor XIIa, thrombin, and factor XIa.

Wu W, Sinha D, Shikov S, Yip CK, Walz T, Billings PC, Lear JD, Walsh PN.

J Biol Chem. 2008 Jul 4;283(27):18655-64. doi: 10.1074/jbc.M802275200. Epub 2008 Apr 25.

7.

Structure and function of factor XI.

Emsley J, McEwan PA, Gailani D.

Blood. 2010 Apr 1;115(13):2569-77. doi: 10.1182/blood-2009-09-199182. Epub 2010 Jan 28. Review.

8.

Structural and functional features of factor XI.

Gailani D, Smith SB.

J Thromb Haemost. 2009 Jul;7 Suppl 1:75-8. doi: 10.1111/j.1538-7836.2009.03414.x. Review.

9.

Characterization of the H-kininogen-binding site on factor XI: a comparison of factor XI and plasma prekallikrein.

Renné T, Gailani D, Meijers JC, Müller-Esterl W.

J Biol Chem. 2002 Feb 15;277(7):4892-9. Epub 2001 Nov 30.

10.

Structural analysis of eight novel and 112 previously reported missense mutations in the interactive FXI mutation database reveals new insight on FXI deficiency.

Saunders RE, Shiltagh N, Gomez K, Mellars G, Cooper C, Perry DJ, Tuddenham EG, Perkins SJ.

Thromb Haemost. 2009 Aug;102(2):287-301. doi: 10.1160/TH09-01-0044.

PMID:
19652879
11.

Coagulation factor XII protease domain crystal structure.

Pathak M, Wilmann P, Awford J, Li C, Hamad BK, Fischer PM, Dreveny I, Dekker LV, Emsley J.

J Thromb Haemost. 2015 Apr;13(4):580-91. doi: 10.1111/jth.12849. Epub 2015 Mar 11.

12.

A binding site for thrombin in the apple 1 domain of factor XI.

Baglia FA, Walsh PN.

J Biol Chem. 1996 Feb 16;271(7):3652-8.

13.

Three residues at the interface of factor XI (FXI) monomers augment covalent dimerization of FXI.

Zucker M, Zivelin A, Landau M, Rosenberg N, Seligsohn U.

J Thromb Haemost. 2009 Jun;7(6):970-5. doi: 10.1111/j.1538-7836.2009.03353.x.

14.

Identification of a binding site for glycoprotein Ibalpha in the Apple 3 domain of factor XI.

Baglia FA, Gailani D, López JA, Walsh PN.

J Biol Chem. 2004 Oct 29;279(44):45470-6. Epub 2004 Aug 17.

16.

Activation of the zymogen to urokinase-type plasminogen activator is associated with increased interdomain flexibility.

Behrens MA, Botkjaer KA, Goswami S, Oliveira CL, Jensen JK, Schar CR, Declerck PJ, Peterson CB, Andreasen PA, Pedersen JS.

J Mol Biol. 2011 Aug 12;411(2):417-29. doi: 10.1016/j.jmb.2011.05.026. Epub 2011 Jun 6.

PMID:
21669207
17.

Crystal structure of the proenzyme domain of plasminogen.

Peisach E, Wang J, de los Santos T, Reich E, Ringe D.

Biochemistry. 1999 Aug 24;38(34):11180-8.

PMID:
10460175
18.

A novel factor XI missense mutation (Val371Ile) in the activation loop is responsible for a case of mild type II factor XI deficiency.

Bozzao C, Rimoldi V, Asselta R, Landau M, Ghiotto R, Tenchini ML, De Cristofaro R, Castaman G, Duga S.

FEBS J. 2007 Dec;274(23):6128-38. Epub 2007 Oct 30.

19.

Apple four in human blood coagulation factor XI mediates dimer formation.

Meijers JC, Mulvihill ER, Davie EW, Chung DW.

Biochemistry. 1992 May 19;31(19):4680-4.

PMID:
1581318
20.

Solution structure of the transcriptional activation domain of the bacteriophage T4 protein, MotA.

Li N, Zhang W, White SW, Kriwacki RW.

Biochemistry. 2001 Apr 10;40(14):4293-302.

PMID:
11284685

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