000 01680 a2200469 4500
005 20250515121822.0
264 0 _c20080930
008 200809s 0 0 eng d
022 _a1528-0020
024 7 _a10.1182/blood-2008-04-148759
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aGao, Weiqiang
245 0 0 _aExtensive contacts between ADAMTS13 exosites and von Willebrand factor domain A2 contribute to substrate specificity.
_h[electronic resource]
260 _bBlood
_cSep 2008
300 _a1713-9 p.
_bdigital
500 _aPublication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
650 0 4 _aADAM Proteins
_xchemistry
650 0 4 _aADAMTS13 Protein
650 0 4 _aAmino Acid Sequence
650 0 4 _aBase Sequence
650 0 4 _aBinding Sites
650 0 4 _aBiomarkers, Tumor
_xchemistry
650 0 4 _aCalcium-Binding Proteins
650 0 4 _aDNA Primers
_xgenetics
650 0 4 _aHumans
650 0 4 _aIn Vitro Techniques
650 0 4 _aKinetics
650 0 4 _aModels, Molecular
650 0 4 _aMolecular Sequence Data
650 0 4 _aMutagenesis, Site-Directed
650 0 4 _aPeptide Fragments
_xchemistry
650 0 4 _aProtein Interaction Domains and Motifs
650 0 4 _aProtein Structure, Tertiary
650 0 4 _aRecombinant Fusion Proteins
_xchemistry
650 0 4 _aSequence Deletion
650 0 4 _aSubstrate Specificity
650 0 4 _aTranscription Factors
_xchemistry
700 1 _aAnderson, Patricia J
700 1 _aSadler, J Evan
773 0 _tBlood
_gvol. 112
_gno. 5
_gp. 1713-9
856 4 0 _uhttps://doi.org/10.1182/blood-2008-04-148759
_zAvailable from publisher's website
999 _c17987047
_d17987047