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1 in nucleolin through a region containing the kringle domain.
2 points toward a novel functional role for a kringle domain.
3 HGF containing the N-terminal and the first kringle domain.
4 omposed of only the amino terminus and first kringle domain.
5 nuclei through a mechanism that requires its kringle domain.
6 the HGF/SF amino-terminal sequence and first kringle domain.
7 pecific for plasminogen and conserved in its kringle domains.
8 scope of potential biological functions for kringle domains.
9 ormation of Pg through interactions with the kringle domains.
10 of SK x Pg*, and this process is governed by kringle domains.
11 for functional characterization of specific kringle domains.
12 om release of both the variable and constant kringle domains.
13 ructural makeup from a composite of multiple kringle domains.
14 ns a major lysine binding site in one of its kringle domains.
15 ed the native conformations adopted by these kringle domains.
16 via proteins that bind to the plasmin(ogen) kringle domains.
17 pigment epithelium-derived factor (PEDF) or Kringle domains 1-3 of angiostatin (K1K3) in reducing ab
18 g ulcers to a number of fragments, including kringle domains 1-3, an angiostatin-related protein.
20 ring human isoform consisting of plasminogen kringle domains 1-4 and most of kringle domain 5, dose d
22 omains comes from its binding to plasminogen kringle domain 4 and to miniplasminogen (kringle domain
23 with the lysine-binding sites in plasminogen kringle domain 4 because a deletion mutant of plasminoge
24 gen kringle domain 4 and to miniplasminogen (kringle domain 5 plus the protease domain) with apparent
25 plasminogen kringle domains 1-4 and most of kringle domain 5, dose dependently reduces cell number d
26 ed HGF/NK2, which extends through the second kringle domain and behaves as a competitive HGF/SF antag
27 stability of the native conformation of this kringle domain and perhaps to maintenance of local confo
28 rably to plasminogen, which consists of five kringle domains and a serine protease domain, and to ang
29 uch as lysine analogs, bind unselectively to kringle domains and are therefore unsuitable for functio
30 cifically bound to alphavbeta(3) through the kringle domains and induced migration of endothelial cel
31 meric cDNAs with the propeptide/Gla domains, kringle domain, and serine protease domain exchanged bet
34 s, the lysine binding sites on plasminogen's kringle domains, and plasmin's serine protease domain gr
36 HGF/SF comprised of the N-terminal and first Kringle domains) by titration with either heparin or DS
37 bility of rFII to that of hFII, and the rFII kringle domain changed the stability of hFII to that of
39 Additional evidence for NG2 interaction with kringle domains comes from its binding to plasminogen kr
40 proteoglycan NG2 with human plasminogen and kringle domain-containing plasminogen fragments have bee
42 ver, the lysine-binding sites in plasminogen kringle domains facilitate the C4BP-plasminogen interact
43 of four homologous triple-disulfide bridged kringle domains, has previously been shown to exhibit pr
44 al rabbit mAb in complex with the human ROR2 kringle domain (hROR2-Kr) guided affinity maturation by
47 lar analysis revealed that the extracellular Kringle domain is required for ROR1/ROR2 heterooligomeri
49 asminogen fragment containing 3-4 N-terminal kringle domains, is a potent inhibitor of tumor-induced
50 verified specific interaction of recMoPrP to kringle domains (K(1+2+3)) with higher binding by recMoP
51 mation of a circular exon encoding the first kringle domain (K1) of the human tissue plasminogen acti
52 xpressed the N-terminal (N) domain, the four kringle domains (K1 to K4) and the serine proteinase hom
54 s composed of an alpha-chain containing four Kringle domains (K1-K4) and a serine protease domain-lik
58 uPA receptor binding growth factor domain or kringle domain (kringle) from full-length single chain u
63 ichiometry in which the N-terminal and first kringle domain of HGF/SF contact the face of the seven-b
64 ary aim of our study was to characterize the kringle domains of angiostatin for their inhibitory acti
66 ation was dependent on an interaction of the kringle domains of plasmin with alpha(9)beta(1) as well
68 ting the Gla, aromatic amino acid stack, and kringle domains of prothrombin, has the signal peptide a
69 Although multivalent molecules bind to the Kringle domains of rat plasminogen and reduce plasmin ac
70 rotease (E2-fXa) as well as the Gla and both kringle domains of the substrate (prethrombin-2) had bee
71 to fragment 1.2 (containing Gla and the two kringle domains only) and to fragment 2 but not to throm
75 ectivity for KIV-10, compared with the other kringle domains tested, including plasminogen kringle 1.
76 s much slower in Glu-Pg, which contains five kringle domains, than in Pg forms containing one kringle
77 n inhibitor of angiogenesis, contains 3 to 4 kringle domains that are derived from proteolytic cleava
78 t the SK alpha domain binds avidly to the Pg kringle domains that maintain Glu-Pg in a tightly folded
80 ragment lacking the Gla domain and the first kringle domain), to fragment 1.2 (containing Gla and the
82 ids in the heparin binding site (HBS) in the kringle domain were mutated to alanines behaved like Del