ライフサイエンスコーパス: Pro residue

1 substrates are kinked at the conserved P(3) Pro residue.

2 domain of the fusion toxin, was changed to a Pro residue.

3 -MS(3) via zn* can confirm the presence of a Pro residue.

4 e peptide bond formation between consecutive Pro residues.

5 confirmed cleavage at the C-terminal side of Pro residues.

6 neutrophils that contains five Trp and three Pro residues.

7 o appears to be modulated by the presence of Pro residues.

8 Additionally, Spry2 is hydroxylated on Pro residues 18, 144, and 160, and substitution of these

9 domain binding region that does not contain Pro residues after phospho-Ser.

10 embrane region containing six closely spaced Pro residues and a disulfide bond.

11 BxpA is unusually rich in Gln and Pro residues and contains several different tandem repea

12 in the closed channel located among Pro-Val-Pro residues and downstream; 3), a difference in the ope

13 onal modifications, such as hydroxylation of Pro residues and glycosylation, to form mature, bioactiv

14 The Pro residues and Ile58, Tyr61, and Phe62 are essential f

15 Gid4 recognized the N-terminal proline (Pro) residue and the 5-residue-long adjacent sequence m

16 main containing the highest concentration of Pro residues, and a very highly charged C domain.

17 ed to predict the release of peptides with a Pro residue at position 2 from the N terminus.

18 dues at position -5 have a high incidence of Pro residues at positions -6 and -4, Val at position -3,

19 d-coil domain is not possible because of the Pro residues at positions 3, 7, and 11 at the N-terminus

20 ition, effective maturation of a mutant with Pro residues at positions from -6 throughout -4 proved t

21 The Pro residues at the Xaa and Yaa positions of an (Xaa-Yaa

22 ich the Nleu side chains are arrayed between Pro residues belonging to different triple-helix cross s

23 Replacement of the fully conserved Pro residues by alpha-aminoisobutyric acid leads to a la

24 f adenine or O2 of thymine suggests that the Pro residue can make hydrophobic contacts with the sugar

25 I prefers to cleave peptides with 1 or more Pro residues flanked by 2 positively charged residues.

26 n I containing a Thr144 substituted with the Pro residue found in slow skeletal troponin I resulted i

27 Mutation of two invariant Pro residues had little effect on enzyme function.

28 line conformation whereas the region without Pro residues has a beta-conformation.

29 -complexity sequence enriched with basic and Pro residues, has been identified in the N-terminal regi

30 lls yielded glycoproteins with virtually all Pro residues hydroxylated and subsequently arabinosylate

31 The presence of invariant Pro residues immediately upstream of the toxin regions a

32 I and GI, the hydroxylation of the conserved Pro residue improved their folding but impaired their ac

33 s are discussed in terms of the role of each Pro residue in maintaining the structure and function of

34 Introduction of one additional Pro residue in the center of a Q9 element within PGQ9 co

35 , these data established the importance of a Pro residue in the P3' position for efficient inhibition

36 thogens is due to the presence of a specific Pro residue in the target peptidase that disrupts intera

37 The Pro residue in this compound is replaced with arylalkyl

38 Substitution of five helix-breaking Gly or Pro residues in positions 6-10 as well as disruption of

39 All of the Pro residues in the (Ala-Pro-Ala-Pro)(n) fusion protein

40 Amino acid substitution mutations at all Pro residues in the C fragment dramatically decreased st

41 Pro residues in the loop are critical for the establishm

42 states, and this exchange may be mediated by Pro residues in the sequence.

43 ling during translation of three consecutive Pro residues in vitro, and loss of eIF5A function impair

44 ranslational hydroxylation of (2 S)-proline (Pro) residues in procollagen strands.

45 translational hydroxylation of (2S)-proline (Pro) residues in protocollagen strands.

46 e gamma-carbon atom of certain (2S)-proline (Pro) residues in tropocollagen, elastin, and other prote

47 ntroduction of proline surrogates (Psi(Me,Me)pro residues) in phakellistatin 19, which effectively in

48 However, introduction of Pro residues into the leader peptide strongly affected t

49 or, a strong interaction between the Phe and Pro residues is evident, as is a strong preference for a

50 Whereas the region containing both Pro residues is quite variable among PI-PLCs, it shows h

51 librium ratio of cis to trans isomers of the Pro residues is unaffected by the presence of carbohydra

52 purely by the presence and the positions of Pro residues (L3-9).

53 ins 3 Pro residues near its N terminus and 2 Pro residues near its C terminus.

54 The interdomain segment contains 3 Pro residues near its N terminus and 2 Pro residues near

55 contrary to the model above, the N-terminal Pro residue of c-MOS is entirely dispensable for its deg

56 Thus, the N-terminal Pro residue of c-MOS is not a recognition determinant fo

57 p residues, and carbonyl groups from Gly and Pro residues on neighboring chains.

58 enic enzymes that bear either the N-terminal Pro residue or a Pro at position 2, together with adjace

59 s, conformational restriction offered by the Pro residues (phi = -60 degrees +/- 15 degrees), the set

60 ndard SH3/peptide complexes, even though the Pro residue positions are not conserved.

61 may limit access to the active site, and two Pro residues, Pro(245) and Pro(254), are associated with

62 In contrast, 20% to 30% of Pro residues remained non-hydroxylated in the (Thr-Pro-T

63 nds or isomerization of peptide bonds around Pro residues, respectively.

64 ree classes of stalling peptides: C-terminal Pro residues, SecM-like peptides, and the novel stalling

65 ecreased flexibility by substitutions of 4-6 Pro residues, shortened the hinge by a 1-residue deletio

66 the protein backbone at the Calpha atom of a Pro residue to produce 2-hydroxyproline (2-Hyp).

67 Mutation of Pro(417), but not other Pro residues, to Ala abolished GCase activation by ANP.

68 The 5 Pro residues were each mutated to both a Gly and Ala res

69 within alpha-26 with Glu, or substitution of Pro residues with Ala, significantly reduced the efficac

70 g depended upon the codon for the C-terminal Pro residue, with CCU and CCC promoting efficient +1 fra

71 The middle Pro residue within the tripeptides was replaced with ana

72 made essential DNA contacts, whereas Gly and Pro residues within the Arg-Gly-Arg-Pro core sequence we