ライフサイエンスコーパス: kringle domain

1 nuclei through a mechanism that requires its kringle domain.

2 in nucleolin through a region containing the kringle domain.

3 points toward a novel functional role for a kringle domain.

4 HGF containing the N-terminal and the first kringle domain.

5 omposed of only the amino terminus and first kringle domain.

6 the HGF/SF amino-terminal sequence and first kringle domain.

7 scope of potential biological functions for kringle domains.

8 ormation of Pg through interactions with the kringle domains.

9 of SK x Pg*, and this process is governed by kringle domains.

10 om release of both the variable and constant kringle domains.

11 pecific for plasminogen and conserved in its kringle domains.

12 ructural makeup from a composite of multiple kringle domains.

13 ns a major lysine binding site in one of its kringle domains.

14 ed the native conformations adopted by these kringle domains.

15 pigment epithelium-derived factor (PEDF) or Kringle domains 1-3 of angiostatin (K1K3) in reducing ab

16 g ulcers to a number of fragments, including kringle domains 1-3, an angiostatin-related protein.

17 d to angiostatin, which contains plasminogen kringle domains 1-3.

18 ring human isoform consisting of plasminogen kringle domains 1-4 and most of kringle domain 5, dose d

19 uence 467-476 of prepro-plasminogen, between kringle domain 4 and 5.

20 omains comes from its binding to plasminogen kringle domain 4 and to miniplasminogen (kringle domain

21 with the lysine-binding sites in plasminogen kringle domain 4 because a deletion mutant of plasminoge

22 gen kringle domain 4 and to miniplasminogen (kringle domain 5 plus the protease domain) with apparent

23 plasminogen kringle domains 1-4 and most of kringle domain 5, dose dependently reduces cell number d

24 ed HGF/NK2, which extends through the second kringle domain and behaves as a competitive HGF/SF antag

25 stability of the native conformation of this kringle domain and perhaps to maintenance of local confo

26 rably to plasminogen, which consists of five kringle domains and a serine protease domain, and to ang

27 cifically bound to alphavbeta(3) through the kringle domains and induced migration of endothelial cel

28 meric cDNAs with the propeptide/Gla domains, kringle domain, and serine protease domain exchanged bet

29 o-terminal segment with a hairpin loop, four kringle domains, and a serine protease-like region.

30 cluding an amino-terminal hairpin loop, four kringle domains, and a serine protease-like region.

31 Here, we show that cleavage of the kringle domain at Lys317/Thr318 switches its function to

32 HGF/SF comprised of the N-terminal and first Kringle domains) by titration with either heparin or DS

33 bility of rFII to that of hFII, and the rFII kringle domain changed the stability of hFII to that of

34 The presence of the hFII kringle domain changed the stability of rFII to that of

35 Additional evidence for NG2 interaction with kringle domains comes from its binding to plasminogen kr

36 proteoglycan NG2 with human plasminogen and kringle domain-containing plasminogen fragments have bee

37 ), which are located within each of its five kringle domains, except kringle 3.

38 ver, the lysine-binding sites in plasminogen kringle domains facilitate the C4BP-plasminogen interact

39 of four homologous triple-disulfide bridged kringle domains, has previously been shown to exhibit pr

40 CA), indicating the requirement for a lysine-kringle domain interaction.

41 lar analysis revealed that the extracellular Kringle domain is required for ROR1/ROR2 heterooligomeri

42 Functional divergence among kringle domains is discussed on the basis of their surfa

43 asminogen fragment containing 3-4 N-terminal kringle domains, is a potent inhibitor of tumor-induced

44 verified specific interaction of recMoPrP to kringle domains (K(1+2+3)) with higher binding by recMoP

45 mation of a circular exon encoding the first kringle domain (K1) of the human tissue plasminogen acti

46 xpressed the N-terminal (N) domain, the four kringle domains (K1 to K4) and the serine proteinase hom

47 Three kringle domains (K1, K2 and K4) displayed agonistic acti

48 s composed of an alpha-chain containing four Kringle domains (K1-K4) and a serine protease domain-lik

49 actions between the N- domain and the second kringle domain (K2).

50 hil activation through interactions with its kringle domain (KD).

51 uPA receptor binding growth factor domain or kringle domain (kringle) from full-length single chain u

52 Our data suggest that different kringle domains may contribute to the overall anti-angio

53 The N-terminal and first Kringle domains (NK1) of HGF comprise a naturally occurr

54 in containing an N-terminal segment and four kringle domains (NK4) antagonize HGF activity.

55 Here we report the NMR structure of its kringle domain, NT/K.

56 ichiometry in which the N-terminal and first kringle domain of HGF/SF contact the face of the seven-b

57 ary aim of our study was to characterize the kringle domains of angiostatin for their inhibitory acti

58 and the first kringle (K1) or the first two kringle domains of HGF.

59 ation was dependent on an interaction of the kringle domains of plasmin with alpha(9)beta(1) as well

60 Angiostatin, representing the kringle domains of plasmin, alone did not induce the mig

61 ting the Gla, aromatic amino acid stack, and kringle domains of prothrombin, has the signal peptide a

62 rotease (E2-fXa) as well as the Gla and both kringle domains of the substrate (prethrombin-2) had bee

63 to fragment 1.2 (containing Gla and the two kringle domains only) and to fragment 2 but not to throm

64 Deletion of the various kringle domains or the amino-terminal hairpin loop had v

65 otease SK x Pg*, and we examined whether the kringle domains regulate this process.

66 ease domain, interactions between SK and the kringle domain(s) play a key role in Pg activation.

67 s much slower in Glu-Pg, which contains five kringle domains, than in Pg forms containing one kringle

68 n inhibitor of angiogenesis, contains 3 to 4 kringle domains that are derived from proteolytic cleava

69 t the SK alpha domain binds avidly to the Pg kringle domains that maintain Glu-Pg in a tightly folded

70 The kringle domain therefore is critical in determining the

71 ragment lacking the Gla domain and the first kringle domain), to fragment 1.2 (containing Gla and the

72 The structure also shows that Pg kringle domains undergo significant structural rearrange

73 ids in the heparin binding site (HBS) in the kringle domain were mutated to alanines behaved like Del

74 binding affinity and binding specificity of kringle domains with various ligands.