ライフサイエンスコーパス: proline residue

1 ition of a single oxygen atom to a conserved proline residue.

2 inal lysine residues following the conserved proline residue.

3 tes in the linker region are followed by the proline residue.

4 turn or touch-turn that is anchored by a cis-proline residue.

5 ,4S)-fluoroproline relative to the canonical proline residue.

6 nical fusion tripeptide along with a central proline residue.

7 sponding position is occupied by a conserved proline residue.

8 half is induced to kink outward by a central proline residue.

9 de whose helical structure is disrupted by a proline residue.

10 bstantial differences in the vicinity of the proline residue.

11 verage about four residues N-terminal to the proline residue.

12 has been associated with the presence of the proline residue.

13 n and an unusual preference for a C-terminal proline residue.

14 H2 orthologs through the Drosophila sp. to a proline residue.

15 e was the highest of all propensities of non-proline residues.

16 ix more than unfavorable ring puckers of the proline residues.

17 a conserved beta-hinge region containing two proline residues.

18 traordinary high concentration (over 25%) of proline residues.

19 the hydroxyl group installed on C(gamma) of proline residues.

20 onverting conformers that often contain many proline residues.

21 ne residues on the basis of their spacing to proline residues.

22 changes including cis/trans isomerization of proline residues.

23 cts are observed consistent with cleavage at proline residues.

24 residues, three tryptophan residues, and two proline residues.

25 ization of one or both of the N-terminal cis proline residues.

26 embrane helix kinks, which commonly occur at proline residues.

27 at CyP40 interacts with tau at sites rich in proline residues.

28 peptide bond trans/cis ratio of substituted proline residues.

29 w for connecting triple-helical collagen via proline residues.

30 Celiac Disease (CD) is their high content in proline residues.

31 requires posttranslational hydroxylation of proline residues.

32 ight amino acids and contains four invariant proline residues.

33 ith a proline knot motif defined by only two proline residues.

34 with PHD2 and PHD3 and is hydroxylated at 2 proline residues.

35 inations of cis and trans forms of the three proline residues.

36 of peptides with stereospecifically modified proline residues.

37 post-translational hydroxylation of peptidyl proline residues.

38 Cep192 is hydroxylated by PHD1 on proline residue 1717.

39 ical amino acids were subsequently mapped to proline residues 184 and 188 within a conserved PXXXP mo

40 ells and catalyzes hydroxylation of actin at proline residues 307 and 322.

41 dues in length) in the database that contain proline residues, 57% show multiple resolved features in

42 SFMBT1 hydroxylation on Proline residue 651 by EglN1 mediated its ubiquitination

43 Mutation of proline residues abolished cyclin D1 binding and also di

44 Mutation of this proline residue abrogated co-immunoprecipitation of CD14

45 riking feature is the alignment of conserved proline residues across the dimer interface.

46 We hypothesize that these proline residues act to partially restore virus budding

47 were clustered adjacent to an oxygen-sensing proline residue, affecting HIF2alpha interaction with th

48 alpha-helix, an increased number of internal proline residues along the transmembrane helices, and a

49 he present results indicate that penultimate proline residues also are an important means of increasi

50 at either L230 or L230, L233, and Y236 with proline residues also decreases the level of binding, in

51 These data indicate that an intact proline residue and an intact G(14)XXXG(18) motif within

52 ned no 3Hyp at any site, despite a candidate proline residue and recognizable A1 sequence motif.

53 In normoxia, hydroxylation of two proline residues and acetylation of a lysine residue at

54 Prolyl peptidases cleave proteins at proline residues and are of importance for cancer, neuro

55 aves oligopeptides at the C-terminal side of proline residues and constitutes an important pharmaceut

56 The rat 20-29 sequence contains three proline residues and does not form amyloid, while the hu

57 ding hydroxylation of polypeptide lysine and proline residues and dopamine that are required for coll

58 The optimal linker contains two proline residues and enhances compound affinity.

59 ters of the proteins e.g. number of charges, proline residues and extended strand.

60 y disrupting polyQ chains with insertions of proline residues and find that their mechanical extensib

61 xylase domain proteins hydroxylate substrate proline residues and have been linked to fuel switching.

62 ral region of both Las17 and WASP is rich in proline residues and is generally considered to bind to

63 striking ones between the presence of nearby proline residues and lethal mutations, and the presence

64 ine assemblies containing 16, 17, 18, and 19 proline residues and ordered arrays of a Ru(II)-bipyridy

65 lyze the post-translational hydroxylation of proline residues and play a role in collagen production,

66 ylated serine residues in the absence of any proline residues and suggest a novel mechanism whereby a

67 rally slower than that around amide bonds to proline residues and takes place on the NMR inversion-ma

68 avage at the amide bond on the N-terminal of proline residues and the consequently low relative abund

69 To further elucidate the role of these proline residues and to simplify the folding mechanism,

70 pseudosubstrate motif centered on a critical proline residue, and that this regulation occurs indepen

71 c pairs, in parallel stacked pairs involving proline residues, and in parallel offset arrangements fo

72 nces contained fewer tyrosine residues, more proline residues, and more hydrophobic residues (p<0.001

73 ophobic residues, the conserved and variable proline residues, and the conserved lysine residues to t

74 he puckering of the pyrrolidine rings of the proline residues, and the secondary structural motifs.

75 etitive domain that is rich in glutamine and proline residues, and three C-terminal domains with eigh

76 mutants were identified as proline, and both proline residues are adjacent to cysteine residues invol

77 eptide database that illustrates penultimate proline residues are frequently found in neuropeptides.

78 These 4-tyrosine and 5-proline residues are highly conserved in herpesvirus sca

79 rgeted for proteasomal degradation after two proline residues are hydroxylated by a family of prolyl

80 The proline residues are not apparently conserved for functi

81 s can participate in this reaction, and that proline residues are particularly reactive.

82 Proline residues are relatively common in transmembrane

83 refolding phase of a construct in which all proline residues are replaced remains slow.

84 g heterogeneity persists even when all seven proline residues are replaced.

85 Mutational analysis reveals that proline residues are required for this nucleation activi

86 spectra of peptides containing more than 30% proline residues are simpler and easier to interpret tha

87 Proline residues are uniformly distributed along the pol

88 conservative substitution of a leucine for a proline residue at a structurally important site in neo-

89 We found that adding a single proline residue at Kabat position 243, immediately adjac

90 Replacement of the proline residue at position 1 of the protease dimer inte

91 ong protein kinases due to the presence of a proline residue at position 123 that precludes the forma

92 ensitivity toward W84, and it seems that the proline residue at position 179 in M5 (corresponding to

93 The replacement of this proline residue at position 180 (P180) by either threoni

94 ") that expressed a mutant DSPP in which the proline residue at position 19 was replaced by a leucine

95 To advance studies of DsbA2, a cis-proline residue at position 198 was replaced with threon

96 no acid mutagenesis, that replacement of the proline residue at position 28 of the insulin B-chain (P

97 ed by a pivotal cis-trans isomerization of a proline residue at position 32 in the polypeptide, with

98 of the C-terminal domain is compromised by a proline residue at position 572 or 550.

99 ncers, we have identified a highly conserved proline residue at position 830 (Pro(830)) that is criti

100 ttributed to isomerization of the native cis-proline residue at position 93.

101 ave a basic residue at the +2 position and a proline residue at the -2 position, respectively, the ma

102 mutant eIF5A proteins contain mutations in a proline residue at the junction between the two eIF5A do

103 ues (Asp or Glu) at the S/T-2 position and a proline residue at the S/T+1 position.

104 ealed that tryptic peptide ions containing a proline residue at the second position from the N-termin

105 P, suggesting an incompatibility between the proline residue at this position and the presence of KK

106 states, and favored cleavages N-terminal to proline residues at high charge states.

107 ammalian counterparts by the substitution of proline residues at several key dynamic locations in fir

108 Thus, domain interaction and a cis-proline residue between the two domains are ruled out as

109 ding by increasing the rate of transition of proline residues between the cis and trans states.

110 ation decreased by 125-fold with three added proline residues between tyrosine and the oxidant.

111 le residues, but also short sequences of non-proline residues can adopt the P(II) conformation.

112 e go on to show that mutation of a conserved proline residue centrally located within the C-terminal

113 Protonation site, proline residue conformation, and side chain orientation

114 s in adjoining membranes, mainly mediated by proline residues conserved in AQP0s from different speci

115 sting that cis- trans isomerization of these proline residues contributes to the slow association rat

116 We hypothesized that this proline residue could affect the size and orientation of

117 f collagens, particularly 4-hydroxylation of proline residues, could be one of the modalities by whic

118 gion or due simply to the fact that multiple proline residues destabilize amyloid fibrils.

119 that a subset of free peptides enriched with proline residues directly bind to the target.

120 observed in a mutant in a membrane-embedded proline residue elsewhere in the Tet(L) protein (P175C)

121 ant virus occurred rapidly, resulting in new proline residues elsewhere in the M protein.

122 Proline residues favor bending of alpha-helices, and sub

123 ch is initiated by hydroxylation of specific proline residues followed by binding of von Hippel-Linda

124 the MS2-derived protein cage with N-terminal proline residues followed by three variable positions.

125 2, replacement of serine 104 (S104) with the proline residue found in murine DAF eliminated virus bin

126 Removal of the proline residue from the Trx active site yields a CGC ac

127 ix geometry, it is reasonable to expect that proline residues generate these kinks.

128 te that the incorporation of the substituted proline residues had a dramatic effect upon the self-ass

129 Our results suggest that (1) the proline residue has a role in both specificity and phosp

130 plete backbone assignments (>93%) of all non-proline residues have been obtained, with the majority o

131 Functionalized proline residues have diverse applications.

132 amma-amino acid being flanked by two d- or l-proline residues, have been synthesized and tested as or

133 ells produced a fusion glycoprotein with all proline residues hydroxylated and substituted with an ar

134 A proline residue immediately follows 7 of the 11 unambigu

135 edral angles of the guest amino acid and the proline residue immediately preceding it; and 2), a nonl

136 ntrast, the strictly conserved histidine and proline residues immediately upstream of the asparagine

137 se data provide a high-resolution mapping of proline residues important for CyPA binding and identify

138 s important for structural stability and two proline residues important for Fc epsilon RI binding.

139 This SNP, which converts a conserved proline residue in FAAH to threonine (P129T), suggests a

140 mers, enhanced permeation is due to a single proline residue in GluK5 that alters the dynamics of the

141 the absence of cyclosporine via a regulatory proline residue in Itk.

142 Experiments with the P20G variant show the proline residue in pHLIP reduces the alpha-helix content

143 erase activity is largely abolished when the proline residue in position 2 or the lysine residue in p

144 mutant phenotype to a missense mutation of a proline residue in position 80 to a leucine residue in a

145 enzyme responsible for hydroxylation of the proline residue in precrocapeptin.

146 oints to an important role of this conserved proline residue in stabilizing the Fe-S cluster.

147 n of one or two fluorine atoms into a single proline residue in the 99 amino acid long protein--modul

148 Mutation of one proline residue in the activation domain to an alanine (

149 are responsible for anchoring the invariant proline residue in the active site of this postproline-c

150 Prolyl 3-hydroxylase 1 modifies a single proline residue in the alpha chains of type I, II, and I

151 o-trans conversion upon hydroxylation of the proline residue in the dipeptide.

152 ous study of the effect of deleting a single proline residue in the FP of a demyelinating MHV strain,

153 ulge away from the ATP-binding pocket, and a proline residue in the hinge removes a conserved main ch

154 X-3 has two important structural features: a proline residue in the hydrophobic core that discourages

155 tutions for the five lysine residues and the proline residue in the MCD peptide (1) sequence.

156 Post-translational hydroxylation of a proline residue in the oxygen-dependent degradation (ODD

157 n that the Ahp-heterocycle originates from a proline residue in the precursor molecule precrocapeptin

158 Furthermore, mutation of a single proline residue in the protease prodomain suppressed the

159 alysis revealed that Ssu72 requires that the proline residue in the substrate's SP motif is in the ci

160 cid substitutions for a completely conserved proline residue in this region not only impair fusion an

161 This is dependent on a singular proline residue in trialysin and is inhibited by the cyc

162 Replacing proline residues in (ProProGly)(7) collagen strands with

163 to discriminate against the conformation of proline residues in a manner that diminishes product inh

164 t regio- and stereospecifically hydroxylates proline residues in a peptide chain into R-4-hydroxyprol

165 se for the analogous secondary amide bond to proline residues in acyclic peptides.

166 The large number of proline residues in ADAMTS13 is consistent with the impo

167 Careful positioning of proline residues in AMP sequences is required to enable

168 intermediates that then couple to N-terminal proline residues in high yield.

169 oxygen-dependent hydroxylation of conserved proline residues in its alpha-subunit, carried out by pr

170 We systematically characterized all proline residues in NS5A domain II, low-complexity seque

171 ence of NaDC1 contains a number of conserved proline residues in predicted transmembrane helices (TMs

172 to catalyze the 3-hydroxylation of specific proline residues in procollagen I in vitro.

173 hiamin, Coenzyme A, and the hydroxylation of proline residues in proteins.

174 We find that mutations to highly conserved proline residues in repeats 2 and 3 of the microtubule b

175 arate as substrates to hydroxylate conserved proline residues in target proteins.

176 usually resistant peptide bonds adjacent to proline residues in the 33-mer peptide.

177 ffers from that in humans by substitution of proline residues in the amyloidogenic sequence so that t

178 CyPA binds to proline residues in the C-terminal half of NS5A, in a di

179 mall repressor protein is weak, however, and proline residues in the dimer interface suggest that fol

180 Proline residues in the helical segments of soluble and

181 strategy is reported for the modification of proline residues in the N-terminal positions of proteins

182 roach, we identified several surface-exposed proline residues in the nucleotide binding domain and li

183 eptide backbone despite the presence of many proline residues in the peptide that are unable to parti

184 The role of proline residues in the photocycle of bacteriorhodopsin

185 Finally, surface-exposed proline residues in the proteolytically resistant ligand

186 and Leu205 play a key role in the binding of proline residues in the S2 pocket of cathepsin K and are

187 ), due to posttranslational modifications of proline residues in the substrate.

188 5, whereas the minor, active isomer has both proline residues in their trans configuration.

189 on of proline residues, since there are five proline residues in this domain.

190 Four conserved proline residues in TMs 7 and 10 of rabbit NaDC1 were re

191 ervation of disulfide bonds, location of all proline residues in turns and loops, and conservation of

192 reports show minimal 3-hydroxylation of key proline residues in type I collagen as a result of CRTAP

193 nd capped by the use of two sequential trans-proline residues in V lambda domains.

194 A proline residue (in place of a glycine in PGI) may also

195 orm pores, and introduction of the analogous proline residue into another CDC, pneumolysin, significa

196 is mutation, which changes a fully conserved proline residue into leucine at position 20 (P20L), resu

197 To examine this, we introduced proline residues into regions of the N-terminal domain t

198 secretory reporter domain or introduction of proline residues into TM3 changed the TM2 cross-linking

199 for correct anchoring, although a preceding proline residue is dispensable.

200 A functionally important proline residue is highly conserved in the cytosolic Tol

201 The position of proline residues is critical to the toxicity of cereal p

202 The orientation of proline residues is regulated by cis/trans peptidyl-prol

203 mmonly proposed that the role of penultimate proline residues is to protect peptides from enzymatic d

204 teristics, particularly the presence of >10% proline residues, it forms the characteristic alphabetaa

205 We find that mutation of a proline residue located at a turn within this loop profo

206 A proline residue located at the central FP region has oft

207 rtion is maintained primarily by a conserved proline residue located in the proximal heme pocket.

208 Converting a single proline residue located in this region of GATA-4 to its

209 Third, proline residues located pseudo-symmetrically around the

210 The results suggest that proline residues may be conserved at domain-domain bound

211 cotinic acetylcholine receptor (nAChR) has a proline residue near the middle of the beta9 strand.

212 a critical role for the non-hydroxylation of proline residues near the collagenase cleavage site.

213 e 47 polymorphic variant, which replaces the proline residue necessary for recognition by proline-dir

214 The results of this analysis show that proline residues occur with a significant concentration

215 Hydroxylation of proline residue occurs in specific peptides and proteins

216 Posttranslational hydroxylation of proline residues occurs in DPYSP(OH)S motifs, which are

217 However, the proline residue of DYRK1 targeted by hydroxylation and t

218 which covered all of the remaining 18 trans proline residues of alphaTS, was constructed to obtain s

219 corresponding carbamate, as well as the four proline residues of an Src homology 3 domain protein.

220 hat, under normoxia, selectively hydroxylate proline residues of HIF, initiating proteosomal degradat

221 The proline residues of ubiquitin are passive spectators in

222 Proline residues often form important kinks in alpha-hel

223 Thus, the substitution of a proline residue on C-4 affects the trans/cis ratio by al

224 terminal residues on peptides and N-terminal proline residues on proteins.

225 The effect of sterically demanding groups at proline residues on the conformational stability of the

226 terminus, the inclusion of a helix-breaking proline residue or using D-amino acids as building block

227 human peptide in this segment but with three proline residues outside this region.

228 Substituting the proline residue P475 in the S6 of the Shaker channel by

229 shc) mutant containing substitutions for the proline residues (P47A/P48A/P50A) resulted in enhanced S

230 Mutating a conserved proline residue (P63A) in the HUalpha subunit, deleting

231 With more than 15% of all proline residues participating in N-H...N H-bonds, we su

232 (Q) peptides flanked on the C terminus by 11 proline residues (poly(Q)-poly(P)), as occurs in the hun

233 erplay between the anchoring residue and the proline residue preceding it.

234 Substitution of the proline residues Pro-424 and Pro-427 by alanines results

235 role group due to close interaction with the proline residue (Pro(346)) immediately following the hem

236 al analyses of C21 revealed that a conserved proline residue (Pro-221) is central to degron activity,

237 Here, the role of the three proline residues (Pro(2), Pro(3), and Pro(7)) in establi

238 tail, because point mutations in C-terminal proline residues (Pro-187 and Pro-190) completely preven

239 Mutation of proline residues (Pro2) in the amino-terminal region of

240 at the putative dynamic hinge created by the proline residue provides a structural basis for the inte

241 The proline residue provides the enhanced activity because i

242 Mutation of this proline residue reduced binding of CD147-derived peptide

243 of the zipper domain by the introduction of proline residues reduces the ability of EBNA 3C to inhib

244 rationale for the previous observation that proline residues represent favored HAT sites in the reac

245 Insertion of two proline residues resulted in soluble, nonfibrillar aggre

246 OD1-dependent hydroxylation of a neighboring proline residue resulting in 40S ribosomal subunits that

247 epitope (uTIINE) peptide, a 45-mer with 5 HO-proline residues resulting from MMP-13-catalyzed degrada

248 ere, we report that deletion of one of these proline residues, resulting in RSA59 (P), significantly

249 An analysis of H-bond-forming proline residues reveals that more than 30% of the proli

250 hinge region sequence, ER-PXPX, with its two proline residues separated by a non-conserved residue, b

251 s finding strongly supports a model in which proline residues serve as molecular hinges or swivels, e

252 c phases were attributed to isomerization of proline residues, since there are five proline residues

253 Collagen contains a large number of proline residues, so the cis/trans isomerization of prol

254 the H(gamma)(3) ring position of the second proline residue stabilizes these triple helices.

255 oints of stabilization throughout gp140, 149 proline residue substitutions at every residue of the gp

256 Positioning of proline residues such that they do not interfere with ba

257 In normoxia, PHD hydroxylates a specific proline residue that directs the degradation of constitu

258 abilization of the conserved kink, whether a proline residue that divides the helix into segments is

259 ng is mediated by the non-hydroxylation of a proline residue that is N-terminal to the cleavage site

260 harbors an unusual beta-methyl-delta-hydroxy-proline residue that may increase conformational rigidit

261 in GluK2/GluK5 heteromers results from a key proline residue that produces architectural changes in t

262 hough the membrane anchor contains a central proline residue that reaches the periplasm, its position

263 on of HIF-1alpha containing mutations in the proline residues that are hydroxylated by PHD2 induces d

264 Collagens contain a large number of proline residues that are post-translationally modified

265 of transient interactions frequently include proline residues that favor an extended conformation for

266 ns a repetitive segment rich in arginine and proline residues that is dispensable for its effects on

267 e enhanced presence of somatically generated proline residues that preclude hydrogen bond ladder form

268 rdered proteins, like tau, are enriched with proline residues that regulate both secondary structure

269 A THIK2 mutant containing a proline residue (THIK2-A155P) in its second inner helix

270 formations can be achieved in the absence of proline residues, thus raising the question of the mecha

271 hat trans 4-hydroxylation "preorganizes" the proline residue to adopt the C(4)-exo conformation, via

272 Mutation of the single proline residue to glycine (P52G) did not substantially

273 is incorporated at the gamma-carbon of the D-proline residue to mimic the charge distribution of the

274 utation (385C-->A) that converts a conserved proline residue to threonine (Pro129-->Thr), producing a

275 of the tether by mutating several conserved proline residues to alanines did not produce a discernib

276 esidue peptide, BS30, which incorporates two proline residues to induce reverse turns, was designed t

277 ab protein is dimethylated at the N-terminal proline residue, trimethylated at Lys-3 by Rkm2, and mon

278 ed (P728IeNOS) or incorporated (I958PnNOS) a proline residue unique to the eNOS hinge.

279 taining acidic side-chains and N-terminal to proline residues; UVPD did not exhibit preferential clea

280 In contrast, no 3-hydroxylation of this proline residue was found in P3H1 null mice.

281 The proline residue was found to be critically important for

282 strong NLS (844RVVKLRIAP852) with basic and proline residues was identified.

283 onstrate that this preference for C-terminal proline residues was observed in Hendra virus-derived pe

284 tasidotin, with the radiolabel in the second proline residue, was hydrolyzed intracellularly, with fo

285 d by WIP(C) and the high occurrence (25%) of proline residues, we employed 5D-NMR(13)C-detected NMR e

286 arged amino acids and the positioning of the proline residues were also investigated.

287 d on two model peptides in which penultimate proline residues were known to be important for biologic

288 Substitutions introducing proline residues were recovered at 53 % of all positions

289 Proline residues were replaced with alanine, both singly

290 Six proline residues were substituted with alanine individua

291 4070A), an isoleucine replaced the wild-type proline residue, whereas a threonine residue was found i

292 te, in general, are not determinative of the proline residues whose isomerization reactions can limit

293 e disease and substitutes a highly conserved proline residue with leucine (p.P72L) that, based on the

294 nAChR is facilitated by the presence of the proline residue within the beta9 strand.

295 linkers 1 and 2 were individually changed to proline residues within an alpha(T)/alpha(i1) chimera (d

296 carbonyl carbon atom linked to the N atom of proline residues within di- and tripeptides.

297 to its mediation of cis-trans conversion of proline residues within histone tails.

298 After examining the location of proline residues within the amino acid sequences of TM h

299 These enzymes convert proline residues within the repeat regions of collagen p

300 Therefore, all proline residues within the transmembrane helices of the