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Items: 1 to 20 of 154

1.

The WXXW motif in the TSR1 of ADAMTS13 is important for its secretion and proteolytic activity.

Ling J, Su J, Ma Z, Ruan C.

Thromb Res. 2013 Jun;131(6):529-34. doi: 10.1016/j.thromres.2013.04.024. Epub 2013 May 14.

PMID:
23683325
2.

Leukocyte proteases cleave von Willebrand factor at or near the ADAMTS13 cleavage site.

Raife TJ, Cao W, Atkinson BS, Bedell B, Montgomery RR, Lentz SR, Johnson GF, Zheng XL.

Blood. 2009 Aug 20;114(8):1666-74. doi: 10.1182/blood-2009-01-195461. Epub 2009 Jun 18.

3.

Thrombospondin-1 and ADAMTS13 competitively bind to VWF A2 and A3 domains in vitro.

Wang A, Liu F, Dong N, Ma Z, Zhang J, Su J, Zhao Y, Ruan C.

Thromb Res. 2010 Oct;126(4):e260-5. doi: 10.1016/j.thromres.2010.07.009. Epub 2010 Aug 11.

PMID:
20705333
4.

FRETS-VWF73 rather than CBA assay reflects ADAMTS13 proteolytic activity in acquired thrombotic thrombocytopenic purpura patients.

Mancini I, Valsecchi C, Lotta LA, Deforche L, Pontiggia S, Bajetta M, Palla R, Vanhoorelbeke K, Peyvandi F.

Thromb Haemost. 2014 Aug;112(2):297-303. doi: 10.1160/TH13-08-0688. Epub 2014 Apr 17.

PMID:
24740645
5.

Mechanism of von Willebrand factor scissile bond cleavage by a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13 (ADAMTS13).

Xiang Y, de Groot R, Crawley JT, Lane DA.

Proc Natl Acad Sci U S A. 2011 Jul 12;108(28):11602-7. doi: 10.1073/pnas.1018559108. Epub 2011 Jun 24.

6.

Amino acid residues Arg(659), Arg(660), and Tyr(661) in the spacer domain of ADAMTS13 are critical for cleavage of von Willebrand factor.

Jin SY, Skipwith CG, Zheng XL.

Blood. 2010 Mar 18;115(11):2300-10. doi: 10.1182/blood-2009-07-235101. Epub 2010 Jan 14.

7.

The co-influence of VWD type 2B/2M mutations in the A1 domain and platelet GPIbα on the rate of cleavage to VWF by ADAMTS13.

Ma Z, Su J, Zhang J, Ling J, Yin J, Bai X, Ruan C.

Thromb Res. 2015 Nov;136(5):987-95. doi: 10.1016/j.thromres.2015.08.008. Epub 2015 Aug 18.

PMID:
26345337
8.

Molecular characterization of four ADAMTS13 mutations responsible for congenital thrombotic thrombocytopenic purpura (Upshaw-Schulman syndrome).

Hommais A, Rayes J, Houllier A, Obert B, Legendre P, Veyradier A, Girma JP, Ribba AS.

Thromb Haemost. 2007 Sep;98(3):593-9.

PMID:
17849048
9.

Zinc and calcium ions cooperatively modulate ADAMTS13 activity.

Anderson PJ, Kokame K, Sadler JE.

J Biol Chem. 2006 Jan 13;281(2):850-7. Epub 2005 Nov 11.

10.

A conformation-sensitive monoclonal antibody against the A2 domain of von Willebrand factor reduces its proteolysis by ADAMTS13.

Zhang J, Ma Z, Dong N, Liu F, Su J, Zhao Y, Shen F, Wang A, Ruan C.

PLoS One. 2011;6(7):e22157. doi: 10.1371/journal.pone.0022157. Epub 2011 Jul 11. Erratum in: PLoS One. 2011;6(9). doi:101371/annotation/fe2ceb97-9332-4479-9827-90dcd4027570.

11.

Light chain of factor VIII is sufficient for accelerating cleavage of von Willebrand factor by ADAMTS13 metalloprotease.

Cao W, Sabatino DE, Altynova E, Lange AM, Casina VC, Camire RM, Zheng XL.

J Biol Chem. 2012 Sep 21;287(39):32459-66. Epub 2012 Aug 1.

12.

Evaluation of a disintegrin-like and metalloprotease with thrombospondin type 1 repeat motifs 13 (ADAMTS13) activity enzyme-linked immunosorbent assay for measuring plasma ADAMTS13 activity in dogs.

Maruyama H, Kaneko M, Otake T, Kano R, Yamaya Y, Watari T, Hasegawa A, Kamata H.

J Vet Diagn Invest. 2014 Mar;26(2):226-31. doi: 10.1177/1040638714523609. Epub 2014 Feb 28.

PMID:
24583948
13.

Mechanistic studies on ADAMTS13 catalysis.

Di Stasio E, Lancellotti S, Peyvandi F, Palla R, Mannucci PM, De Cristofaro R.

Biophys J. 2008 Sep;95(5):2450-61. doi: 10.1529/biophysj.108.131532. Epub 2008 May 23.

14.

N-Glycans of ADAMTS13 modulate its secretion and von Willebrand factor cleaving activity.

Zhou W, Tsai HM.

Blood. 2009 Jan 22;113(4):929-35. doi: 10.1182/blood-2008-07-167775. Epub 2008 Nov 3.

15.

Degradation of circulating von Willebrand factor and its regulator ADAMTS13 implicates secreted Bacillus anthracis metalloproteases in anthrax consumptive coagulopathy.

Chung MC, Popova TG, Jorgensen SC, Dong L, Chandhoke V, Bailey CL, Popov SG.

J Biol Chem. 2008 Apr 11;283(15):9531-42. doi: 10.1074/jbc.M705871200. Epub 2008 Feb 8.

17.

Shear-induced unfolding activates von Willebrand factor A2 domain for proteolysis.

Baldauf C, Schneppenheim R, Stacklies W, Obser T, Pieconka A, Schneppenheim S, Budde U, Zhou J, Gräter F.

J Thromb Haemost. 2009 Dec;7(12):2096-105. doi: 10.1111/j.1538-7836.2009.03640.x. Epub 2009 Oct 8.

18.

[Increased susceptibility of recombinant type 2A von Willebrand factor mutant A1500E to proteolysis by ADAMTS13].

Zhang JY, Su J, Ma ZN, Dong NZ, Wang YC, Ruan CG.

Zhonghua Xue Ye Xue Za Zhi. 2012 Mar;33(3):169-72. Chinese.

PMID:
22781599
19.

The proximal carboxyl-terminal domains of ADAMTS13 determine substrate specificity and are all required for cleavage of von Willebrand factor.

Ai J, Smith P, Wang S, Zhang P, Zheng XL.

J Biol Chem. 2005 Aug 19;280(33):29428-34. Epub 2005 Jun 23.

20.

The p.R1819_C1948delinsS mutation makes von Willebrand factor ADAMTS13-resistant and reduces its collagen-binding capacity.

Daidone V, Saga G, Barbon G, Pontara E, Cattini MG, Morpurgo M, Zanotti G, Casonato A.

Br J Haematol. 2015 Aug;170(4):564-73. doi: 10.1111/bjh.13472. Epub 2015 Apr 23.

PMID:
25904363

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