ライフサイエンスコーパス: pro-peptide

1 ision of their anionic N-terminal inhibitory pro peptide.

2 es non-covalently linked with the N terminal pro-peptide.

3 inflammasome by inducing the build-up of Xaa-Pro peptides.

4 as several TGF-beta inhibitory proteins and pro-peptides.

5 at prevents the autocatalytic removal of its pro-peptides.

6 held together by N-terminal swapping of the pro-peptides.

7 ), Arg(10) (polyR), Ser(10) (polyS), and (cr)pro peptide, a charge-reversing mutant of the pro peptid

8 es C-alpha hydroxylation of glycine extended pro-peptides, a critical post-translational step in pept

9 ached to beta-lactamase, indicating that the pro-peptide acts as a specific secretion enhancer for nu

10 The structures reveal that the pro-peptide acts as an assembly-promoting factor by link

11 The data suggest that the pro-peptide adopts a beta-structure when in contact with

12 leaved at residues 198 and 775 to generate a pro-peptide, amidase and glucosaminidase, respectively.

13 Surprisingly, (cr)pro peptide and (wt)pro peptide showed similar propertie

14 gs identify a dual chaperone activity of the pro peptide and may shed light on the molecular mechanis

15 ally attached the proHNP1 pro peptide or (wt)pro peptide and the following artificial pro segments to

16 A 3xHA-mCherry-AtCEP2 gene fusion including pro-peptide and KDEL targeting sequences expressed under

17 c pathway, where amino- and carboxy-terminal pro-peptides are cleaved to generate a 30-kDa mature enz

18 Proteolytic removal of part of the pro-peptide at Leu(28p) or Gly(45p), which diminishes th

19 We now demonstrate that the addition of the pro-peptide between the OmpA signal peptide and nuclease

20 ntermediate that has a 19-residue N-terminal pro-peptide between the signal peptide and nuclease A.

21 The X-Pro peptide bond (in which X represents any amino acid r

22 Here, we investigated whether the second Asp-Pro peptide bond (residues 121-122) of NOTCH3 is cleaved

23 atalyze the isomerization of the phospho-Thr-Pro peptide bond at the turn motif, thus converting thes

24 e of unfolded species which have different X-Pro peptide bond conformations.

25 the enhanced activity because its tertiary X-Pro peptide bond favors the cleavage-enhancing binding o

26 The loop containing the heterogeneous Ala-Pro peptide bond is conserved in mammals, and suggests t

27 cess which is not complicated by cis-trans X-Pro peptide bond isomerization.

28 icates that prolyl isomerization of the pThr-Pro peptide bond results from both destabilization of th

29 analyzing the conformation of the scissile X-Pro peptide bond, and by comparing the rate constants fo

30 constants for the cleavage of the tertiary X-Pro peptide bond, the tertiary X-Sar peptide bond (Sar i

31 mations via cis-trans isomerization of a Tyr-Pro peptide bond.

32 due to cis-trans isomerization about the Gly-Pro peptide bond.

33 lded species (Uvf, Uf, Um, and Us) at each X-Pro peptide bond.

34 nist-induced conformational changes at the X-Pro peptide bond.

35 sing from cis/trans isomerization of the Xaa-Pro peptide bond.

36 ubstitutions were made in the X residue of X-Pro peptide bonds (where X is the residue on the amino-t

37 ions were obtained for each of these three X-Pro peptide bonds at 15 degrees C.

38 (13)C and (15)N chemical shifts from X-Pro peptide bonds in bR are assigned from REDOR differen

39 unfolded species, labeled Uvf, has all its X-Pro peptide bonds in the native conformation.

40 to catalyze isomerization of the many pSer--Pro peptide bonds in the phosphorylated CTD.

41 rs to be determined by the fraction of cis X-Pro peptide bonds in this region.

42 that cis/trans isomerization of several Xaa-Pro peptide bonds is the source of the multiple folding

43 Whereas in two unfolded heptapeptides, X-Pro peptide bonds isomerized ca 1.6-fold faster at 1 bar

44 arise from cis-trans isomerizations at the X-Pro peptide bonds of Pro 93, 114, and 117 in the unfolde

45 rate-limiting cis-trans isomerization of Xaa-Pro peptide bonds respectively.

46 the isomerization of phosphorylated Ser/Thr-Pro peptide bonds to induce conformational changes of it

47 ion, respectively, across the Cys-Pro or Gly-Pro peptide bonds were determined by magnetization trans

48 PPEP-1 exhibits a unique specificity for Pro-Pro peptide bonds within the consensus sequence VNP PVP.

49 rol transcription by isomerizing phospho-Ser-Pro peptide bonds within the CTD repeat.

50 attributed to cis-trans isomerizations of X-Pro peptide bonds, a plausible explanation for AP, which

51 cleaved in multiple locations at labile Asp-Pro peptide bonds.

52 ering the conformation of specific pSer/pThr-Pro peptide bonds.

53 the isomerization of phosphorylated Ser/Thr-Pro peptide bonds.

54 antibodies reacting either with BDNF or its pro-peptide both stained large dense core vesicles in ex

55 ding, with PEG being the most efficient, the pro peptide catalyzed the folding of proHNPs likely thro

56 AAV-mediated expression of myostatin pro-peptide D76A mutant in adult Ldlr null mice sustaine

57 ed that AAV-mediated delivery of a myostatin pro-peptide D76A mutant in adult mice attenuates the dev

58 In addition, when added in trans, the pro-peptide does not inhibit the activity of the mature

59 In particular, the pro-peptide domain (LOX-PP) released from the secreted p

60 The presence of free BACE Pro peptide during renaturation of BACE460 but not ProBA

61 s of transcripts show that the extracellular pro-peptide-encoding gene EPIDERMAL PATTERNING FACTOR 2

62 he secreted protease CRSP, which cleaves the pro-peptide EPF2, in turn repressing stomatal developmen

63 s of cis-trans isomerization of individual X-Pro peptide groups is used to study the backbone dynamic

64 te (consisting of cis and trans isomers of X-Pro peptide groups) to the native structure in which onl

65 Pro-peptide has two distinct functions in guiding protei

66 To better understand the role of the pro peptide in the folding and functioning of alpha-defe

67 osome, and the role of the nascent TnaC-tRNA(Pro) peptide in facilitating tryptophan binding and indu

68 To understand the role of the pro-peptide in proteasome assembly, we have determined s

69 esulted in sustained expression of myostatin pro-peptide in the liver.

70 BDNF is stored with its pro-peptide in the presynaptic terminals of excitatory n

71 The existence of similar pro-peptides in Gram-positive bacterial secretory protei

72 n at the NSVD(9) sequence as occurs when the pro-peptide is in cis to the protease domain.

73 nuclease A and nuclease B indicated that the pro-peptide itself had no significant destabilizing effe

74 ytic events excise the N-terminal inhibitory pro peptide, leading to defensin maturation and storage

75 l lysine K33 to trigger cleavage of the beta pro-peptides, leading to the concerted dissociation of P

76 ently bind its ubiquitin and Pro-Thr/Ser-Ala-Pro peptide ligands.

77 to have a hydrophobic signal sequence and a pro-peptide-like sequence that is removed to generate th

78 ed by homology modeling and suggested that a pro-peptide Lys residue intrudes into the S2 pocket, whi

79 The pro peptide of proHNP1 also interacts specifically with

80 trast with the long pro-domain caspases, the pro-peptide of caspase-3 does not appear to be involved

81 The pro-peptide of type III collagen (PRO-C3) serves as a se

82 sferases, and neoepitope-specific N-terminal pro-peptide of type III collagen (Pro-C3) than placebo.

83 sferases, and neoepitope-specific N-terminal pro-peptide of type III collagen (Pro-C3) than placebo.

84 collagen (C3M), type IV collagen (C4M) and a pro-peptide of type III collagen (PRO-C3) were measured

85 otransferase, neoepitope-specific N-terminal pro-peptide of type III collagen, and liver stiffness fa

86 lar peptides with Xaa-Pro N-termini, but Xaa-Pro peptides on their own without a second danger signal

87 efensins, we chemically attached the proHNP1 pro peptide or (wt)pro peptide and the following artific

88 Procollagen type-I C-terminal pro-peptide (PICP) and collagen type-1 C-terminal telope

89 ges in serum procollagen type-III N-terminal pro-peptide (PIIINP) in participants assigned to spirono

90 binding domain (VAB) complexed with a Pro-X-Pro peptide recognition motif present in one such recept

91 For some toxins, proteolytic activation and pro-peptide removal will facilitate unfolding of the pre

92 The anionic pro peptide, required for correct sub-cellular trafficki

93 Surprisingly, (cr)pro peptide and (wt)pro peptide showed similar properties with respect to in

94 with proteolytic cleavage of the C-terminal pro-peptide that anchors assembly-incompetent UMOD precu

95 LAP is the TGF-beta pro-peptide that is cleaved intracellularly prior to sec

96 expressed as a 396-amino acid, 42.7-kDa pre-pro-peptide that is post-translationally processed into

97 e doughnut, suggesting that upon cleavage of pro-peptides, the two disk-shaped nonamers can, and have

98 hich is the conversion of a glycine-extended pro-peptide to its alpha-hydroxyglcine intermediate.

99 ich diminishes the affinity of the shortened pro-peptide to the active site, results in activated mem

100 t catalyzes conversion of a glycine-extended pro-peptide to the corresponding alpha-hydroxyglycine de

101 This enhancing effect of the pro-peptide was not as striking when it was attached to

102 The pro-peptide was processed by incubating with cell extrac

103 amined the interactions of the 28 amino acid pro-peptide when added in trans to the pro-less variant.

104 ro peptide, a charge-reversing mutant of the pro peptide where Arg/Lys residues were changed to Asp,