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1 -MS(3) via zn* can confirm the presence of a Pro residue.
2  substrates are kinked at the conserved P(3) Pro residue.
3 domain of the fusion toxin, was changed to a Pro residue.
4 e peptide bond formation between consecutive Pro residues.
5 neutrophils that contains five Trp and three Pro residues.
6 o appears to be modulated by the presence of Pro residues.
7 confirmed cleavage at the C-terminal side of Pro residues.
8 tein folding, amplified for proteins rich in Pro residues.
9       Additionally, Spry2 is hydroxylated on Pro residues 18, 144, and 160, and substitution of these
10  domain binding region that does not contain Pro residues after phospho-Ser.
11 embrane region containing six closely spaced Pro residues and a disulfide bond.
12            BxpA is unusually rich in Gln and Pro residues and contains several different tandem repea
13  in the closed channel located among Pro-Val-Pro residues and downstream; 3), a difference in the ope
14 onal modifications, such as hydroxylation of Pro residues and glycosylation, to form mature, bioactiv
15                                          The Pro residues and Ile58, Tyr61, and Phe62 are essential f
16 trinsically disordered protein (IDP) rich in Pro residues and is involved in hydroxyapatite mineraliz
17      Gid4 recognized the N-terminal proline (Pro) residue and the 5-residue-long adjacent sequence mo
18 main containing the highest concentration of Pro residues, and a very highly charged C domain.
19 ed to predict the release of peptides with a Pro residue at position 2 from the N terminus.
20 dues at position -5 have a high incidence of Pro residues at positions -6 and -4, Val at position -3,
21 d-coil domain is not possible because of the Pro residues at positions 3, 7, and 11 at the N-terminus
22 ition, effective maturation of a mutant with Pro residues at positions from -6 throughout -4 proved t
23                                          The Pro residues at the Xaa and Yaa positions of an (Xaa-Yaa
24 ich the Nleu side chains are arrayed between Pro residues belonging to different triple-helix cross s
25           Replacement of the fully conserved Pro residues by alpha-aminoisobutyric acid leads to a la
26 f adenine or O2 of thymine suggests that the Pro residue can make hydrophobic contacts with the sugar
27  I prefers to cleave peptides with 1 or more Pro residues flanked by 2 positively charged residues.
28 n I containing a Thr144 substituted with the Pro residue found in slow skeletal troponin I resulted i
29                    Mutation of two invariant Pro residues had little effect on enzyme function.
30 line conformation whereas the region without Pro residues has a beta-conformation.
31 -complexity sequence enriched with basic and Pro residues, has been identified in the N-terminal regi
32 lls yielded glycoproteins with virtually all Pro residues hydroxylated and subsequently arabinosylate
33                    The presence of invariant Pro residues immediately upstream of the toxin regions a
34 I and GI, the hydroxylation of the conserved Pro residue improved their folding but impaired their ac
35 s are discussed in terms of the role of each Pro residue in maintaining the structure and function of
36               Introduction of one additional Pro residue in the center of a Q9 element within PGQ9 co
37 , these data established the importance of a Pro residue in the P3' position for efficient inhibition
38 thogens is due to the presence of a specific Pro residue in the target peptidase that disrupts intera
39                                          The Pro residue in this compound is replaced with arylalkyl
40   Substitution of five helix-breaking Gly or Pro residues in positions 6-10 as well as disruption of
41                                   All of the Pro residues in the (Ala-Pro-Ala-Pro)(n) fusion protein
42     Amino acid substitution mutations at all Pro residues in the C fragment dramatically decreased st
43                                              Pro residues in the loop are critical for the establishm
44 states, and this exchange may be mediated by Pro residues in the sequence.
45 ling during translation of three consecutive Pro residues in vitro, and loss of eIF5A function impair
46 ranslational hydroxylation of (2 S)-proline (Pro) residues in procollagen strands.
47 translational hydroxylation of (2S)-proline (Pro) residues in protocollagen strands.
48 e gamma-carbon atom of certain (2S)-proline (Pro) residues in tropocollagen, elastin, and other prote
49 ntroduction of proline surrogates (Psi(Me,Me)pro residues) in phakellistatin 19, which effectively in
50                     However, introduction of Pro residues into the leader peptide strongly affected t
51 or, a strong interaction between the Phe and Pro residues is evident, as is a strong preference for a
52           Whereas the region containing both Pro residues is quite variable among PI-PLCs, it shows h
53 librium ratio of cis to trans isomers of the Pro residues is unaffected by the presence of carbohydra
54  purely by the presence and the positions of Pro residues (L3-9).
55 ins 3 Pro residues near its N terminus and 2 Pro residues near its C terminus.
56           The interdomain segment contains 3 Pro residues near its N terminus and 2 Pro residues near
57  contrary to the model above, the N-terminal Pro residue of c-MOS is entirely dispensable for its deg
58                         Thus, the N-terminal Pro residue of c-MOS is not a recognition determinant fo
59 p residues, and carbonyl groups from Gly and Pro residues on neighboring chains.
60 enic enzymes that bear either the N-terminal Pro residue or a Pro at position 2, together with adjace
61 ets proteins by recognizing their N-terminal Pro residues or a Pro at position 2, in the presence of
62 s, conformational restriction offered by the Pro residues (phi = -60 degrees +/- 15 degrees), the set
63 ndard SH3/peptide complexes, even though the Pro residue positions are not conserved.
64 may limit access to the active site, and two Pro residues, Pro(245) and Pro(254), are associated with
65                            His, Lys, Arg, or Pro residues prohibit cleavage when found at the P1 posi
66                   In contrast, 20% to 30% of Pro residues remained non-hydroxylated in the (Thr-Pro-T
67 nds or isomerization of peptide bonds around Pro residues, respectively.
68  Pro-49 favors a cis configuration and three Pro residues retain an unchanged cis fraction, pointing
69                                 Whereas most Pro residues revert to trans in the oligomeric state, Pr
70 ree classes of stalling peptides: C-terminal Pro residues, SecM-like peptides, and the novel stalling
71 ecreased flexibility by substitutions of 4-6 Pro residues, shortened the hinge by a 1-residue deletio
72 protein and isomerizes the adjacent proline (Pro) residue, thereby altering folding, subcellular loca
73 the protein backbone at the Calpha atom of a Pro residue to produce 2-hydroxyproline (2-Hyp).
74          Mutation of Pro(417), but not other Pro residues, to Ala abolished GCase activation by ANP.
75 ree of order in the oligomer at the sites of Pro residues was probed by monitoring changes in cis/tra
76                                        The 5 Pro residues were each mutated to both a Gly and Ala res
77 within alpha-26 with Glu, or substitution of Pro residues with Ala, significantly reduced the efficac
78 g depended upon the codon for the C-terminal Pro residue, with CCU and CCC promoting efficient +1 fra
79                                   The middle Pro residue within the tripeptides was replaced with ana
80 made essential DNA contacts, whereas Gly and Pro residues within the Arg-Gly-Arg-Pro core sequence we