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Items: 1 to 20 of 158

1.

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.

2.

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.

3.

Noncovalent interactions of the Apple 4 domain that mediate coagulation factor XI homodimerization.

Dorfman R, Walsh PN.

J Biol Chem. 2001 Mar 2;276(9):6429-38. Epub 2000 Nov 22.

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.

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.

6.
7.

Thermodynamic analysis of unfolding and dissociation in lactose repressor protein.

Barry JK, Matthews KS.

Biochemistry. 1999 May 18;38(20):6520-8.

PMID:
10350470
8.

Organophosphorus hydrolase is a remarkably stable enzyme that unfolds through a homodimeric intermediate.

Grimsley JK, Scholtz JM, Pace CN, Wild JR.

Biochemistry. 1997 Nov 25;36(47):14366-74.

PMID:
9398154
9.
11.

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
12.

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.

13.

Folding of Escherichia coli DsbC: characterization of a monomeric folding intermediate.

Ke H, Zhang S, Li J, Howlett GJ, Wang CC.

Biochemistry. 2006 Dec 19;45(50):15100-10.

PMID:
17154548
14.

Chemical denaturation of a homodimeric lysine-49 phospholipase A2: a stable dimer interface and a native monomeric intermediate.

Ruller R, Ferreira TL, de Oliveira AH, Ward RJ.

Arch Biochem Biophys. 2003 Mar 1;411(1):112-20.

PMID:
12590929
15.

Unfolding pathway of the dimeric and tetrameric forms of phosphofructokinase-2 from Escherichia coli.

Baez M, Cabrera R, Guixé V, Babul J.

Biochemistry. 2007 May 22;46(20):6141-8. Epub 2007 May 1.

PMID:
17469854
16.

Guanidinium chloride denaturation of the dimeric Bacillus licheniformis BlaI repressor highlights an independent domain unfolding pathway.

Vreuls C, Filée P, Van Melckebeke H, Aerts T, De Deyn P, Llabrès G, Matagne A, Simorre JP, Frère JM, Joris B.

Biochem J. 2004 Nov 15;384(Pt 1):179-90.

17.

Unfolding and refolding of dimeric creatine kinase equilibrium and kinetic studies.

Fan YX, Zhou JM, Kihara H, Tsou CL.

Protein Sci. 1998 Dec;7(12):2631-41.

18.

Equilibrium unfolding of dimeric desulfoferrodoxin involves a monomeric intermediate: iron cofactors dissociate after polypeptide unfolding.

Apiyo D, Jones K, Guidry J, Wittung-Stafshede P.

Biochemistry. 2001 Apr 24;40(16):4940-8.

PMID:
11305909
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.

SecA folds via a dimeric intermediate.

Doyle SM, Braswell EH, Teschke CM.

Biochemistry. 2000 Sep 26;39(38):11667-76.

PMID:
10995234
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