Taipei Medical University

A B C D E F G H I J K L M N O P Q R S T U V W X Y Z
Chen YL
------>authors3_c=
------>paper_class1=1
------>Impact_Factor=3.056
------>paper_class3=2
------>paper_class2=1
------>vol=93
------>confirm_bywho=None
------>insert_bywho=clare
------>Jurnal_Rank=24.2
------>authors4_c=
------>comm_author=
------>patent_EDate=None
------>authors5_c=
------>publish_day=1
------>paper_class2Letter=None
------>page2=338
------>medlineContent=
------>unit=E0100
------>insert_date=20060725
------>iam=4
------>update_date=None
------>author=???
------>change_event=1
------>ISSN=
------>authors_c=
------>score=500
------>journal_name=Thromb Haemost
------>paper_name=Crotalid venom vascular endothelial growth factors has preferential affinity for VEGFR-1. Characterization of Protobothrops mucrosquamatus venom VEGF
------>confirm_date=None
------>tch_id=089142
------>pmid=15711751
------>page1=331
------>fullAbstract=Pm-VEGF, a novel member ofVEGF family from the venom gland of Taiwan habu (Protobothrops mucrosquamatu), is a disulfide-linked homodimer with 119 amino acid residues. Recombinant fusion Pm-VEGF was expressed in Escherichia coli, purified and refolded. Surface plasmon resonance was used to determine its binding kinetics toVEGF-receptors (VEGFR). Relative to human VEGF165, the binding affinity of Pm-VEGF to the VEGFR-1 was 1.7-fold higher while affinity to the VEGFR-2 was 17-fold lower. But it did not bind the VEGFR-3 or neuropilin-1. Pm-VEGF promoted the proliferation and tissue factor production of endothelial cells, the neovascularization in the chicken chorioallantoic membrane, and increased vascular permeability. It also stimulated tissue-factor production and human monocyte chemotaxis, in accord with its specificity for VEGFR-1. Structural comparison among VEGF-proteins from various viper venoms revealed that the two subfamilies of vipers (Crotalinae and Viperinae) have evolved with distinct receptor-specificities for VEGFR-1 and VEGFR-2, respectively. Discussion on structure-activity relationships of the VEGFs further provided insight into residues important for the receptor-binding and specificities.
------>tmu_sno=None
------>sno=14014
------>authors2=Tsai IH
------>authors3=Hong TM
------>authors4=Tsai SH
------>authors5=
------>authors6=
------>authors6_c=
------>authors=Chen YL
------>delete_flag=0
------>SCI_JNo=None
------>authors2_c=
------>publish_area=0
------>updateTitle=Crotalid venom vascular endothelial growth factors has preferential affinity for VEGFR-1. Characterization of Protobothrops mucrosquamatus venom VEGF.
------>language=2
------>check_flag=None
------>submit_date=None
------>country=None
------>no=2
------>patent_SDate=None
------>update_bywho=None
------>publish_year=2005
------>submit_flag=None
------>publish_month=2
A B C D E F G H I J K L M N O P Q R S T U V W X Y Z