Crystal structure of the kringle 2 domain of tissue plasminogen activator at 2.4-A resolution

Crystal structure of the kringle 2 domain of tissue plasminogen activator at 2.4-A resolution

Item
http://www.wikidata.org/entity/Q27642053
The col-1 module of human matrix metalloproteinase-2 (MMP-2): structural/functional relatedness between gelatin-binding fibronectin type II modules and lysine-binding kringle domainsSurface-associated plasminogen binding of Cryptococcus neoformans promotes extracellular matrix invasionStructural mechanism of voltage-dependent gating in an isolated voltage-sensing domainStructure and distribution of modules in extracellular proteins.Proposed mechanisms for binding of apo[a] kringle type 9 to apo B-100 in human lipoprotein[a].A faster-acting and more potent form of tissue plasminogen activator.Molecular evolution and domain structure of plasminogen-related growth factors (HGF/SF and HGF1/MSP)The plasmin-antiplasmin system: structural and functional aspects.Identification of two functionally distinct lysine-binding sites in kringle 37 and in kringles 32-36 of human apolipoprotein(a).Anti-angiogenic activity of the recombinant kringle domain of urokinase and its specific entry into endothelial cells.The role of the lysyl binding site of tissue-type plasminogen activator in the interaction with a forming fibrin clot.An active zymogen: unravelling the mystery of tissue-type plasminogen activator.Evidence that the conformation of unliganded human plasminogen is maintained via an intramolecular interaction between the lysine-binding site of kringle 5 and the N-terminal peptide.Controlled shear affinity filtration (CSAF): a new technology for integration of cell separation and protein isolation from mammalian cell cultures.Disulfide bonds and disorder in granulin-3: An unusual handshake between structural stability and plasticity.Defensin Modulates Tissue-type Plasminogen Activator and Plasminogen Binding to Fibrin and Endothelial CellsExploring the chemical space of the lysine-binding pocket of the first kringle domain of hepatocyte growth factor/scatter factor (HGF/SF) yields a new class of inhibitors of HGF/SF-MET binding
P2860

Crystal structure of the kringle 2 domain of tissue plasminogen activator at 2.4-A resolution

Item
http://www.wikidata.org/entity/Q27642053
description
1992 nî lūn-bûn
@nan
1992 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Crystal structure of the kring ...... activator at 2.4-A resolution
@ast
Crystal structure of the kring ...... activator at 2.4-A resolution
@en
Crystal structure of the kring ...... activator at 2.4-A resolution
@nl
type
label
Crystal structure of the kring ...... activator at 2.4-A resolution
@ast
Crystal structure of the kring ...... activator at 2.4-A resolution
@en
Crystal structure of the kring ...... activator at 2.4-A resolution
@nl
prefLabel
Crystal structure of the kring ...... activator at 2.4-A resolution
@ast
Crystal structure of the kring ...... activator at 2.4-A resolution
@en
Crystal structure of the kring ...... activator at 2.4-A resolution
@nl
P1433
P1476
P2093
P304
P31
P356
P407
P433
P478
P577
P698
P921
P356
P1433
P1476
Crystal structure of the kring ...... activator at 2.4-A resolution
@en
P2093
P304
P31
P356
P407
P433
P478
P577
P698
P921