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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

57 Pro-peptide has two distinct functions in guiding protei

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

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

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

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

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

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

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

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

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

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

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

69 The pro peptide of proHNP1 also interacts specifically with

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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