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Volumn 109, Issue 10, 2012, Pages 3742-3747

Calcium stabilizes the von Willebrand factor A2 domain by promoting refolding

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; VON WILLEBRAND FACTOR; VON WILLEBRAND FACTOR CLEAVING PROTEINASE;

EID: 84857932056     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1121261109     Document Type: Article
Times cited : (42)

References (26)
  • 1
    • 79960640479 scopus 로고    scopus 로고
    • Biology and physics of von Willebrand factor concatamers
    • Springer TA (2011) Biology and physics of von Willebrand factor concatamers. J Thromb Haemost 9(Suppl 1):130-143.
    • (2011) J Thromb Haemost , vol.9 , Issue.SUPPL. 1 , pp. 130-143
    • Springer, T.A.1
  • 2
    • 0018856312 scopus 로고
    • Factor VIII-related protein circulates in normal human plasma as high molecular weight multimers
    • Hoyer LW, Shainoff JR (1980) Factor VIII-related protein circulates in normal human plasma as high molecular weight multimers. Blood 55(6):1056-1059. (Pubitemid 10063385)
    • (1980) Blood , vol.55 , Issue.6 , pp. 1056-1059
    • Hoyer, L.W.1    Shainoff, J.R.2
  • 4
    • 14544302314 scopus 로고    scopus 로고
    • New concepts in von Willebrand disease
    • Sadler JE (2005) New concepts in von Willebrand disease. Annu Rev Med 56:173-191.
    • (2005) Annu Rev Med , vol.56 , pp. 173-191
    • Sadler, J.E.1
  • 6
    • 47249144803 scopus 로고    scopus 로고
    • Von Willebrand factor, ADAMTS13, and thrombotic thrombocytopenic purpura
    • Sadler JE (2008) Von Willebrand factor, ADAMTS13, and thrombotic thrombocytopenic purpura. Blood 112:11-18.
    • (2008) Blood , vol.112 , pp. 11-18
    • Sadler, J.E.1
  • 7
    • 67249086879 scopus 로고    scopus 로고
    • Structural specializations of A2, a force-sensing domain in the ultralarge vascular protein von Willebrand factor
    • Zhang Q, Zhou Y-F, Zhang C-Z, Springer TA (2009) Structural specializations of A2, a force-sensing domain in the ultralarge vascular protein von Willebrand factor. Proc Natl Acad Sci USA 106:9226-9231.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9226-9231
    • Zhang, Q.1    Zhou, Y.-F.2    Zhang, C.-Z.3    Springer, T.A.4
  • 8
    • 0036893186 scopus 로고    scopus 로고
    • ADAMTS-13 rapidly cleaves newly secreted ultralarge von Willebrand factor multimers on the endothelial surface under flowing conditions
    • Dong JF, et al. (2002) ADAMTS-13 rapidly cleaves newly secreted ultralarge von Willebrand factor multimers on the endothelial surface under flowing conditions. Blood 100:4033-4039.
    • (2002) Blood , vol.100 , pp. 4033-4039
    • Dong, J.F.1
  • 9
    • 66749099068 scopus 로고    scopus 로고
    • Mechanoenzymatic cleavage of the ultralarge vascular protein, von Willebrand factor
    • Zhang X, Halvorsen K, Zhang CZ, Wong WP, Springer TA (2009) Mechanoenzymatic cleavage of the ultralarge vascular protein, von Willebrand factor. Science 324:1330-1334.
    • (2009) Science , vol.324 , pp. 1330-1334
    • Zhang, X.1    Halvorsen, K.2    Zhang, C.Z.3    Wong, W.P.4    Springer, T.A.5
  • 10
    • 79955977529 scopus 로고    scopus 로고
    • A novel calcium-binding site of von Willebrand factor A2 domain regulates its cleavage by ADAMTS13
    • Zhou M, et al. (2011) A novel calcium-binding site of von Willebrand factor A2 domain regulates its cleavage by ADAMTS13. Blood 117:4623-4631.
    • (2011) Blood , vol.117 , pp. 4623-4631
    • Zhou, M.1
  • 11
    • 79960288960 scopus 로고    scopus 로고
    • Calcium modulates force sensing by the von Willebrand factor A2 domain
    • Jakobi AJ, Mashaghi A, Tans SJ, Huizinga EG (2011) Calcium modulates force sensing by the von Willebrand factor A2 domain. Nat Commun 2(385):1-9.
    • (2011) Nat Commun , vol.2 , Issue.385 , pp. 1-9
    • Jakobi, A.J.1    Mashaghi, A.2    Tans, S.J.3    Huizinga, E.G.4
  • 12
    • 0347533937 scopus 로고    scopus 로고
    • Evaluation of ADAMTS-13 activity in plasma using recombinant von Willebrand Factor A2 domain polypeptide as substrate
    • Cruz MA, Whitelock J, Dong JF (2003) Evaluation of ADAMTS-13 activity in plasma using recombinant von Willebrand factor A2 domain polypeptide as substrate. J Thromb Haemost 90(6):1204-1209. (Pubitemid 38004445)
    • (2003) Thrombosis and Haemostasis , vol.90 , Issue.6 , pp. 1204-1209
    • Cruz, M.A.1    Whitelock, J.2    Dong, J.-F.3
  • 13
    • 0026599616 scopus 로고
    • Extending CD spectra of proteins to 168 nm improves the analysis for secondary structures
    • Toumadje A, Alcorn SW, Johnson WC, Jr (1992) Extending CD spectra of proteins to 168 nm improves the analysis for secondary structures. Anal Biochem 200:321-331.
    • (1992) Anal Biochem , vol.200 , pp. 321-331
    • Toumadje, A.1    Alcorn, S.W.2    Johnson Jr., W.C.3
  • 14
    • 48749103325 scopus 로고    scopus 로고
    • Targeted rescue of a destabilized mutant of p53 by an in silico screened drug
    • Boeckler FM, et al. (2008) Targeted rescue of a destabilized mutant of p53 by an in silico screened drug. Proc Natl Acad Sci USA 105:10360-10365.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 10360-10365
    • Boeckler, F.M.1
  • 15
    • 34548819311 scopus 로고    scopus 로고
    • Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions
    • Greenfield NJ (2006) Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions. Nat Protoc 1:2527-2535.
    • (2006) Nat Protoc , vol.1 , pp. 2527-2535
    • Greenfield, N.J.1
  • 17
    • 33645004171 scopus 로고    scopus 로고
    • Intrinsic rates and activation free energies from single-molecule pulling experiments
    • Dudko OK, Hummer G, Szabo A (2006) Intrinsic rates and activation free energies from single-molecule pulling experiments. Phys Rev Lett 96:108101-108104.
    • (2006) Phys Rev Lett , vol.96 , pp. 108101-108104
    • Dudko, O.K.1    Hummer, G.2    Szabo, A.3
  • 18
    • 0031001349 scopus 로고    scopus 로고
    • Dynamic strength of molecular adhesion bonds
    • Evans E, Ritchie K (1997) Dynamic strength of molecular adhesion bonds. Biophys J 72:1541-1555. (Pubitemid 27133095)
    • (1997) Biophysical Journal , vol.72 , Issue.4 , pp. 1541-1555
    • Evans, E.1    Ritchie, K.2
  • 19
    • 0029981188 scopus 로고    scopus 로고
    • Structure of the transition state for folding of a protein derived from experiment and simulation
    • DOI 10.1006/jmbi.1996.0173
    • Daggett V, Li A, Itzhaki LS, Otzen DE, Fersht AR (1996) Structure of the transition state for folding of a protein derived from experiment and simulation. J Mol Biol 257(2):430-440. (Pubitemid 26114044)
    • (1996) Journal of Molecular Biology , vol.257 , Issue.2 , pp. 430-440
    • Daggett, V.1    Li, A.2    Itzhaki, L.S.3    Otzen, D.E.4    Fersht, A.R.5
  • 21
    • 57349124448 scopus 로고    scopus 로고
    • Theory, analysis, and interpretation of single-molecule force spectroscopy experiments
    • Dudko OK, Hummer G, Szabo A (2008) Theory, analysis, and interpretation of single-molecule force spectroscopy experiments. Proc Natl Acad Sci USA 105:15755-15760.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 15755-15760
    • Dudko, O.K.1    Hummer, G.2    Szabo, A.3
  • 22
    • 75649138819 scopus 로고    scopus 로고
    • Force-induced cleavage of single VWF A1A2A3-tridomains by ADAMTS-13
    • Wu T, Lin J, Cruz MA, Dong JF, Zhu C (2010) Force-induced cleavage of single VWF A1A2A3-tridomains by ADAMTS-13. Blood 115:370-378.
    • (2010) Blood , vol.115 , pp. 370-378
    • Wu, T.1    Lin, J.2    Cruz, M.A.3    Dong, J.F.4    Zhu, C.5
  • 23
    • 77951629169 scopus 로고    scopus 로고
    • Unfolding the A2 domain of von Willebrand factor with the optical trap
    • Ying J, Ling Y, Westfield LA, Sadler JE, Shao JY (2010) Unfolding the A2 domain of von Willebrand factor with the optical trap. Biophys J 98:1685-1693.
    • (2010) Biophys J , vol.98 , pp. 1685-1693
    • Ying, J.1    Ling, Y.2    Westfield, L.A.3    Sadler, J.E.4    Shao, J.Y.5
  • 24
    • 33645642908 scopus 로고    scopus 로고
    • ADAMTS-13 plasma level determination uncovers antigen absence in acquired thrombotic thrombocytopenic purpura and ethnic differences
    • Feys HB, et al. (2006) ADAMTS-13 plasma level determination uncovers antigen absence in acquired thrombotic thrombocytopenic purpura and ethnic differences. J Thromb Haemost 4:955-962.
    • (2006) J Thromb Haemost , vol.4 , pp. 955-962
    • Feys, H.B.1
  • 25
    • 0030024985 scopus 로고    scopus 로고
    • Overstretching B-DNA: The elastic response of individual double-stranded and single-stranded DNA molecules
    • Smith SB, Cui Y, Bustamante C (1996) Overstretching B-DNA: The elastic response of individual double-stranded and single-stranded DNA molecules. Science 271:795-799.
    • (1996) Science , vol.271 , pp. 795-799
    • Smith, S.B.1    Cui, Y.2    Bustamante, C.3
  • 26
    • 77955915209 scopus 로고    scopus 로고
    • A mechanically stabilized receptor-ligand flex-bond important in the vasculature
    • Kim J, Zhang C, Zhang X, Springer TA (2010) A mechanically stabilized receptor-ligand flex-bond important in the vasculature. Nature 466:992-995.
    • (2010) Nature , vol.466 , pp. 992-995
    • Kim, J.1    Zhang, C.2    Zhang, X.3    Springer, T.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.