ライフサイエンスコーパス: at position

1 -linked glycosylation site at the N terminus at position 1 (equivalent to Asp-221 in the Fc of IgG1)

2 nd bearing an unnatural triazolyl nucleotide at position 1 (g1).

3 f Grignard reagents followed by N-alkylation at position 1 afforded the 1,7,7-trisubstituted hexahydr

4 presented by a lipophilic n-octyl side chain at position 1 and a positively charged azepanyl or 1,4-d

5 based on the incorporation of a [(13)C] atom at position 1 in specific amino acids.

6 , substituted with oxygen, with nitrogen, or at position 1 with aryl or methyl.

7 tion of carbo- and heterocyclic substituents at position 1', orthogonal functionalization of position

8 nt of a variety of substituents present both at positions 1 and 2; i.e., strongly electron-donating a

9 ontaining either an oxygen or a silicon atom at position 10 are reported.

10 ously identified, specifically glutamic acid at positions 10 or 11 or lysine at position 18, that pro

11 in close proximity to the amino acid cluster at positions 100, 283, and 313), which partially compens

12 g that a loss of phosphorylation site pfsSNV at position 105 in MEF2A is significantly associated wit

13 stacking interaction of an aromatic residue at position 1065 is essential for polysaccharide synthes

14 The importance of the residue at position 11 for NTS1/NTS2 selectivity was further dem

15 Ser/Asp recognition residues in the dockerin at positions 11/12 and 45/46, suggesting that a dual-bin

16 ffers from apoE3 by only a single amino acid at position 112, which is arginine in apoE4 and cysteine

17 e largely controlled by only two amino acids at positions 112 and 139, and that the same residues app

18 2, E3, E4, differing only by two amino acids at positions 112 and 158.

19 However, a different SNP, at position 1139, was identified as being specific to B.

20 -CFTR, an arginine-to-histidine substitution at position 117 of CFTR that is associated with mild for

21 e expressing human profilin1 with a mutation at position 118 (hPFN1G118V).

22 e methylation at position 2, but insensitive at position 12 of the 15-bp core sequence.

23 These methods confirm that ALT initiates at positions 120739/121012 and encodes a single splice s

24 Unexpectedly, the WoA variant with a proline at position 121 (WoA-P121) was found to have L-glutamina

25 jects with valine-to-isoleucine substitution at position 122 (Val122Ile) (n = 91) and wild-type ATTR

26 Here we identified the unique lysine residue at position 124 of the NY-ESO-1 cancer/testis antigen as

27 Here, we show that an aspartate at position 1261 is the most critical residue of the N-t

28 Escape mutations were identified at position 129, 165, or 166 in the major antigenic site

29 S protein with an arginine-to-glycine change at position 135 [liaS(R135G)]) recapitulated a carrier p

30 relatively minor change of valine to alanine at position 135 completely abolished the binding of LPS

31 We propose that the residue at position 135 of MD-2 governs the dynamics of the bind

32 Substitution of Ala for Thr at position 136 of apocarotenoid oxygenase, a site predi

33 apie is strongly influenced by polymorphisms at positions 136, 154, and 171 of a sheep's normal cellu

34 used to detect and quantitate polymorphisms at positions 136, 154, and 171 of sheep PrP(C) or PrP(Sc

35 led both a change from tyrosine to histidine at position 137 (Y137H) and elevated gene expression com

36 ucing the fluorescence donor 6-CNTrp in RRM1 at position 137, and the acceptor 4-aminobenzo[g]quinazo

37 enesis, we were able to identify amino acids at positions 147, 148, and 266 that determine the differ

38 This change at position 149 was distal to the receptor binding site

39 an insertion in the 150-loop (loop beginning at position 150) of the receptor-binding site common to

40 relation between the amino acid polymorphism at position 153 and the DHBA glycoside accumulation patt

41 regulates Mge1 by selectively reducing MetO at position 155 and restores the activity of Mge1 both i

42 Finally, C/T polymorphism of MMP-9 gene at position -1562, which upregulates MMP-9 expression, c

43 ity further increases, fragment N is cleaved at position 157.

44 genetics, we found that a single amino acid at position 158 of the hemagglutinin (HA) protein substa

45 utation introduced an N-linked glycosylation at positions 158 to 160 of the HA protein and that this

46 In this study, we identified glycosylation at positions 158 to 160 of the HA protein of two natural

47 Labeled heads resided stably at positions 16.4 nm apart, corresponding to a microtubu

48 mino acid substitution, lysine to glutamine, at position 166 (H3 numbering) in the major antigenic si

49 d substitution from aspartic acid to alanine at position 168 (D168A) reduced the potency of grazoprev

50 ed with a linear epitope at a lysine residue at position 169 (K169) in the HIV-1 envelope (Env) V2 re

51 e SDR family and oxidizes the hydroxyl group at position 17 of estradiol and 5-androstenediol using N

52 is covalently attached to a cysteine residue at position 175, which is part of an amphipathic alpha-h

53 These results indicate that residues at positions 176 and 210 are critical for the glucose tr

54 domain of HLA-A2 and -B8, including Glu/Asp at position 177, Gln/Glu at position 180, Gly/Arg at pos

55 lutamic acid at positions 10 or 11 or lysine at position 18, that produce peptides with single digit

56 a large extent by mutual exchange of Gln/Glu at position 180 or by Gly/Arg at position 239.

57 However, a negatively charged residue at position 180 was necessary to convey the CaValpha2del

58 , including Glu/Asp at position 177, Gln/Glu at position 180, Gly/Arg at position 239, and Pro/Ser at

59 This indicates that the amino acids at positions 180 and 239 determine the level of cell sur

60 analysis revealed that a valine (V) residue at position 190 in HA is responsible for efficient repli

61 me containing a 2,3-dihydroxypropyl cysteine at position 190 was identified that had significantly in

62 al bundle with two cysteine residues located at positions 191 and 192 in the juxta-transmembrane regi

63 gle substitution of a histidine-to-aspartate at position 193 in Pto, which is not near the AvrPto-spe

64 es identified, two C-terminal phosphoserines at positions 1938 and 1989 showed increased phosphorylat

65 each of four different hydrophobic residues at position 195 served as input data for mutant cycle an

66 gher transcriptional activity, substitutions at position 2 aided in tighter packing and activity, and

67 oisosteric replacement of the carbonyl group at position 2 in a series of 3,4-dihydropyrimidin-2-ones

68 e viral genome, CDK11 phosphorylated serines at position 2 in the CTD of RNAPII, which increased leve

69 ; Gid4 directly or indirectly recognized Pro at position 2 of Pck1, contributing to its targeting.

70 ituted 1-methylcyclohexyl-carboxamide groups at position 2 of the benzothiazole scaffold and endowed

71 A second arylation at position 2 was then carried out, and a library of div

72 , and efficient inversion of stereochemistry at position 2'.

73 CTCF is sensitive to cytosine methylation at position 2, but insensitive at position 12 of the 15-

74 ) N-terminal residue, particularly a residue at position 2, can affect the rate of Nt-arginylation by

75 GLP-2 analogues containing Gly substitution at position 2, norleucine in position 10, and hydrophobi

76 r either the N-terminal Pro residue or a Pro at position 2, together with adjacent sequence motifs.

77 ides with a large chemo- and stereodiversity at position 2.

78 he fourth gluconeogenic enzyme, contains Pro at position 2; Gid4 directly or indirectly recognized Pr

79 ituents (alkyl/alkyl, aryl, and alkyl/ester) at positions 2 and 3 (beta-pyrrole sites, ring A) and 13

80 Each BP lacked canonical uridines at position -2 relative to the BP adenines, with efficie

81 8 of erm(41) and 23S rRNA rrl gene mutations at position 2058 and/or 2059.

82 patients is due to amino acid substitutions at positions 206, 281, and 284 of the human STING protei

83 ates that the 3 disease-associated mutations at positions 206, 281, and 284 of the STING protein defi

84 dition, two previously undescribed variants (at positions 2083 and 2345 of the 23S rRNA gene) were al

85 ntified a PPARalpha response element located at position -2109 base pair relative to the translation

86 sion protein of D/3-13 identified a mutation at position 212 as a possible antigenic determinant resp

87 ing in an arginine to histidine substitution at position 217 (p.Arg217His).

88 IF interaction, or mutation of glutamic acid at position 22 in the catalytic nuclease domain blocked

89 In contrast, cytotoxic strains with tyrosine at position 223 of AgrC cause infections characterized b

90 ino acid substitution (tyrosine to cysteine) at position 223 of AgrC determines starkly different ST2

91 We identified mutations, including several at position 223, that reduce the apparent affinity for o

92 like the three B69 isolates, have a leucine at position 226 in the hemagglutinin (HA) receptor bindi

93 tially all vaccines since 2009, has arginine at position 226, a residue known to confer preference fo

94 irculating human H1N1 viruses, has glutamine at position 226.

95 four of these sites established that serine at position 228 (Ser(228)) on the M1 mAChR showed extrem

96 er studies showed that an avian-like glycine at position 228 at the hemagglutinin (HA) receptor bindi

97 teins that are translated from internal AUGs at positions 235 and 241 of the NS1 open reading frame.

98 of Val264 suggesting that either Ser or Cys at position 239 has similar amide-hydrogen bonding with

99 sition 177, Gln/Glu at position 180, Gly/Arg at position 239, and Pro/Ser at position 280.

100 nge of Gln/Glu at position 180 or by Gly/Arg at position 239.

101 the NS3 proteins analyzed harbored a proline at position 24 that leads to its rapid intracellular dec

102 ype protein, but a protein containing 1 both at positions 24 and 26 bound to the DNA less strongly th

103 affect mutant channels with point mutations at position 2456 that are known to exhibit slow inactiva

104 we demonstrate that the amino acid residues at positions 249, 309, and 339 of the PB2 protein from t

105 glycan emanating from the asparagine residue at position 25 (Asn-25) is located within the trans homo

106 ing in an arginine to histidine substitution at position 252.

107 Mutations located at positions 2576 and 2534 of the 23S rRNA gene were mos

108 As a result, methionine at position 258 of the heavy chain, which is located in

109 esis analyses revealed that a valine residue at position 264 in the rat p75 neurotrophin receptor is

110 bstitution from lysine (K) to methionine (M) at position 27 of histone 3 variant 3 (H3.3).

111 assays were developed to distinguish T or C at position 28 of erm(41) and 23S rRNA rrl gene mutation

112 sis, that replacement of the proline residue at position 28 of the insulin B-chain (ProB28) by (4S)-h

113 on 180, Gly/Arg at position 239, and Pro/Ser at position 280.

114 nor in the liver codon changes were detected at position 282 that cause resistance to nucleos(t)ide a

115 nalyses revealed that the lysine (K) residue at position 294 (K294) within the bZIP domain of the CRE

116 in their Fc domain at a conserved asparagine at position 297.

117 Substitution of serine with aspartate at position 3 (S3D) is widely used to mimic cofilin phos

118 t having an arginine to alanine substitution at position 3 in the N-terminal 13aa motif abolished rep

119 upled at -40 degrees C to the hydroxyl group at position 3 of glucopyranosyl acceptors to form beta-(

120 sulfur, ketone, or methylene bridging group at position 3 of the indole and with halogen or methoxy

121 conditions allowing regioselective arylation at position 3 were successfully developed.

122 oleic acid and the synthesis of regioisomers at position 3'.

123 yl or 1,4-dioxa-8-azaspiro[4.5]decane moiety at position 3.

124 re with distinct features anchoring peptides at positions 3 and 9, supported by an auxiliary anchor i

125 noleic) and regioselectivity (esterification at positions 3 vs. 3').

126 substitution, and additional hydroxyl groups at positions 3' and 4'.

127 tably protected for further chain elongation at positions 3, 4, and 6 of the terminal mannose.

128 on of the rRNA that has a perfect seed match at positions 3-8, including a single G-U base pair.

129 xpectedly, Src-S3C/S6C (containing cysteines at positions 3/6, which are palmitoylated in Fyn) exhibi

130 and a lesser conservation of nucleotide 'C' at position -3 of the 3' splice site.

131 nt harboring glutamic acid instead of valine at position 30 (V30E) failed to induce cell death and ac

132 tion, immunodepletion, and cysteine mutation at position 30.

133 ar disease, is a glutamate deletion (DeltaE) at position 302/303 of TorsinA, a AAA+ ATPase that resid

134 One sequence polymorphism at position 303 of p24 Gag (TGag303V), selected for in i

135 We found that inserting glycans at positions 306 and 314 (termed M1 and M7) markedly red

136 erved that the distances between spin labels at positions 311 and 328 in the fibril core progressivel

137 bic interactions with the tryptophan residue at position 316 and with other topologically proximal si

138 of the three amino acid variants R, W, or Q at position 325 (ZnT8RA, ZnT8WA, and ZnT8QA, respectivel

139 s, through the substitution of phenylalanine at position 327 with tryptophan (F327W).

140 An N-methyl group at position 33 blocks uncontrolled aggregation.

141 ation in GP2 and a lysine-to-serine mutation at position 33 in the stable signal peptide (SSP) subuni

142 ns, with amino acid substitutions clustering at positions 33 to 45, corresponding to the recognition

143 t limitation (extremely low expression), Cys at position 34 of the 3r germ line was replaced by Tyr r

144 nts truncated only at the C terminus, ending at positions 34, 30, and 16.

145 we found that KIR2DL2/L3 with glutamic acid at position 35 (E(35)) are functionally stronger than th

146 herichia coli tyrosine transfer RNAs (tRNAs) at position 35.

147 However, mutants with S residues exchanged at positions 365, 368, and 373 exhibited a significantly

148 a K14 variant harboring a single Cys residue at position 367.

149 ZF2 of human WT1 where the normal glutamine at position 369 is replaced by arginine (Q369R), lysine

150 the hypomodification of a guanosine residue at position 37 (G37) of mitochondrial tRNA; this hypomod

151 t(6)A) is a universal modification occurring at position 37 in nearly all tRNAs that decode A-startin

152 teraction of a proposed pore-lining cysteine at position 37 with the positively charged compound [2-(

153 and its derivatives are modifications found at position 37, 3-adjacent to the anticodon, in tRNAs re

154 the existence of a well-conserved tryptophan at position 375 (Trp 375) in HIV-2/SIVsmm.

155 A highly conserved serine located at position 375 in group M is replaced by a histidine in

156 genetic group, M, which possess a serine (S) at position 375, those from CRF01_AE strains possess a h

157 g simian immunodeficiency virus Env residues at position 375, which resides at a critical location in

158 itution of a conserved serine for a cysteine at position 379.

159 deletion of a highly conserved aspartic acid at position 385, which, for HIV-1, plays a critical role

160 titution of a conserved threonine by proline at position 387 (T387P) in hEAAT1.

161 sive CD4 alleles, which encode an asparagine at position 39 of the receptor.

162 ssense variant encoding alanine or threonine at position 391 in the zinc transporter solute carrier f

163 the replacement of the aspartic acid residue at position 398 with an asparagine (alpha5DN), has recen

164 Piperazine residues at position 4 bearing large phenylalkyl side chains prov

165 st-translationally installed hydroxyl groups at position 4 of prolyl residues.

166 inker is critical to activity, substitutions at position 4 of the benzene ring A were associated with

167 Depending on the substitution at position 4 of the pyrazolones, the new protocol allow

168 activated by deprotonation of a phenol group at position 4 of the substrate, which allows movement of

169 mutating the continuous sequence of thymines at position 4 to cytosine or guanine significantly incre

170 iven by 1,2-DHBs with different substituents at position 4 was performed.

171 ross-couplings or nucleophilic substitutions at position 4.

172 Mutation of the conserved small side chain at position 4.53 within packing cluster 2 is shown to di

173 on steps depends on the substitution pattern at positions 4 and 5 of the oxazole ring, where the aryl

174 e and with halogen or methoxy substituent(s) at positions 4-7.

175 sidues induced termination of mRNA synthesis at position +40 followed by aberrant stop-start transcri

176 rtic acid (D) to asparagine (N) substitution at position 405 (D405N) mutant was partially inhibited b

177 Interestingly, we found that the proline at position 41, a non-CDR residue in heavy chain variabl

178 ur data indicate a model where an alteration at position 420 causes a subtle change in the E2 conform

179 idue with a strong preference for tryptophan at position 420 is important, both functionally and stru

180 uced four separate mutations (F, Y, A, or R) at position 420 within the infectious HCVcc JFH-1 genome

181 xpress either an aspartic acid or an alanine at position 421, mimicking tonic phosphorylation (mHTT-S

182 served increased histone H3K9me3 methylation at positions -423 to -607 of the proximal Npc1l1 promote

183 n a phenylalanine-to-isoleucine substitution at position 427 in the fusion subunit (GP2) of the viral

184 in the NA stalk, and changing the amino acid at position 431 from Proline-to-Lysine.

185 ll mutant NA proteins that possessed proline at position 431 showed higher activities than NA protein

186 Histidine at position 435 (H435) provides for optimal Fc-IgG bindi

187 polymorphic and usually contains an arginine at position 435, which reduces its binding affinity to F

188 Some haplotypes of IgG3 have histidine at position 435.

189 doxin variant F44Y, in which a phenylalanine at position 44 is changed to a tyrosine.

190 As in wild-type Klf4 (E446), the proline at position 446 does not interact directly with either t

191 n, replacing asparagine (N) with lysine (K), at position 46 in the GlyR alpha1 subunit induced hypere

192 The change of Asn at position 460 to His, which corresponds to the natural

193 However, a glycan attached at position 476 appreciably reduced both VWF binding and

194 single substitution of cysteine for tyrosine at position 482 in the native pig CaSR provided a comple

195 utation encoding tyrosine for cysteine (Cys) at position 482 in the pig CaSR.

196 unctional (PAV: proline, alanine, and valine at positions 49, 262, and 296, respectively) or non-func

197 functional (AVI: alanine, valine, isoleucine at positions 49, 262, and 296, respectively) T2R38.

198 The conserved Glu residue at position 5 (E5) of mature (pseudo)pilins is essential

199 Aliphatic and aliphatic-aromatic variations at position 5 and 6 revealed compounds with IC50 values

200 Compounds having bulky aromatic substituents at position 5 and a tryptophan residue at position N-3 o

201 Substitution of Ala for Phe at position 5 conferred 300-fold selectivity against NaV

202 on studies, which indicated that the residue at position 5 regulates the membrane interactions of Src

203 family of stable 2,2'-bipyrroles substituted at positions 5 and 5' with thienyl, phenyl, TMS-ethynyl,

204 ions for positively charged residues located at positions 5, 7, 10 and 11 are defective in packaging

205 Furthermore, the substituents at positions 5,5' remain coplanar to the central rings.

206 ftM, with a glycine to arginine substitution at position 50 in the predicted SAM-binding domain, lack

207 s residues that were placed into the protein at positions 50 or 52.

208 utation in humans, deletion of phenylalanine at position 508 (DeltaF508), on glucose homeostasis in m

209 a single exchange of tyrosine to asparagine at position 52 in NP (in close proximity to the amino ac

210 of the universally conserved methyl-uridine at position 54 stabilizes tRNAs from thermophilic bacter

211 d identified two conserved cysteine residues at positions 54 and 56 as palmitoylation sites.

212 ts with positively charged histidine located at position 55, thereby stabilizing KIR2DL2/L3 dimer and

213 minated phosphorylation of eEF2 at threonine at position 56, resulting in increased protein synthesis

214 IP2) binding and a threonine phosphorylation at position 567.

215 sed by the combined amino acid polymorphisms at positions 58 and 92 within the D0 extracellular domai

216 nt substituents on the 2-phenyl ring (R) and at position 6 (R6), was synthesized with the main purpos

217 he interfacial hydrophobicity of amino acids at positions 6 and 7 of the complementarity-determining

218 n ATTR where tyrosine is replaced by adenine at position 60.

219 e substitution of a single threonine residue at position 61 (T61) in CD30v abrogates CD30v-mediated N

220 n FLUAV nucleocapsids but that polymorphisms at position 627 of the viral polymerase subunit PB2 modu

221 and MCT4 is mediated by a histidine residue at position 64.

222 artially restored by the other substitutions at positions 67 and 107.

223 t, in which alanine is replaced by threonine at position 673 (A673T), appears to protect against late

224 esponds to an alanine to valine substitution at position 673 in APP (A673V), or position 2 of the amy

225 Substitution of a Lys residue at position 68 with Asn in MUG not only accelerates the

226 ity of wild-type Stt7 and its Cys-Ser mutant at positions 68 and 73 in the presence of a reductant su

227 HLA-DPB1 alleles possessing a glutamic acid at position 69 of the beta-chain.

228 , we show that a highly conserved tryptophan at position 69 of the gp120 inner domain is important fo

229 the electronic character of the substituent at position 7 of the heterobicycle and on the counterion

230 y dependent on the alanine/arginine mismatch at position 7.

231 at rs117648444, which encodes a substitution at position 70 of the IFN-lambda4 protein and reduces IF

232 stitution affects hydrogen bond interactions at position 70, required for NRTI excision.

233 Mutations at positions 70 and/or 91 in the core protein of genotyp

234 eviously reported amino acid variant located at position 71, within the peptide-binding groove of HLA

235 is loop contains a functionally critical Tyr at position 71.

236 tated by palmitoylation of a single cysteine at position 739 within the large intracellular loop of N

237 d that an HLA-DR variant containing arginine at position 74 of the DRbeta1 chain (DRbeta1-Arg74) is t

238 variant, causing the substitution of leucine at position 752 to phenylalanine, in PLAA, which causes

239 single Arginine (R) to Glycine (G) mutation at position 76 in the refp17 backbone (p17R76G), as in t

240 We have previously identified a mutation at position 76 of the influenza A virus M2 protein that

241 Moreover, the only R to G mutation at position 76 was found to strongly impact on protein f

242 4 or Bw6 epitope (defined by sequence motifs at positions 77 to 83) were generated using comparative

243 ntroducing the alanine to threonine mutation at position 778 of mouse Hdac4 (corresponding to positio

244 the non-mucus-inducing strains A2 and Long, at positions 79, 191, 357, 371, and 557.

245 iant of the UL40 peptide with a modification at position 8 (P8) of the peptide (VMAPRTLVL) that uses

246 The reactions occur regioselectively at position 8 both in 7 and 9-deazapurines, leading to n

247 rate that somatic mutations occur frequently at position 83, with corresponding domain conformations

248 nce spectra of a nitroxide side chain placed at position 85 or 409 of the enzyme.

249 revealed that substitution of the D1 residue at position 87 with alanine perturbs the chloride-bindin

250 indicated that placement of a bulky residue at position 89 caused a closure of a gap at the lobby, a

251 nsferase activity, which methylates mt-tRNAs at position 9 and is vital for folding mt-tRNAs into the

252 h alpha-modified non-natural alanine analogs at position 9, as well as peptides containing only N-ter

253 y, and alteration of histidine to tryptophan at position 90 changed the electrostatic profile of the

254 glutamic acid (E)-to-glycine (G) difference at position 91 of the VP1 capsid protein shifts the prof

255 c complex, dependent on a conserved cysteine at position 94 in TAPBPR, in which TAPBPR promotes the a

256 electrostatic interactions between residues at positions a, d, e, and g of the heptad repeat.

257 Although the aspartate at position Asp-50 was indispensable for divalent cation

258 sign of specific rotation and configuration at position C(1) allows for easy determination of the ab

259 indicates a high functional group tolerance at position C(11).

260 Q from pABA requires a deamination reaction at position C4 of the benzene ring to substitute the ami

261 otective groups from oxyarene N-heterocycles at positions capable for 2-/4-O-pyridine-2-/4-pyridone t

262 reinhardtii (CrChR2) was selectively labeled at position Cys-79 at the end of the first cytoplasmic l

263 AOX1A carrying a serine residue at position CysI was activated by succinate, while corre

264 amino acids Ala, Asn, Gln, His, Ile, and Lys at positions equivalent to 782 and/or 786 in Fn-binding

265 ave any significant impact on the reactivity at positions [Formula: see text] far away from point [Fo

266 Then, MTX was introduced at positions four and 22 of [F(7),P(34)]-NPY, connected

267 er peptides that undergo sequential cleavage at positions G17/G18 and G35/A36 during export through t

268 Substitutions at position G209 in E2 have no effect on titer, but dele

269 s, we identified that calpain-1 cleaves hERG at position Gly-603 in the S5-pore linker of hERG.

270 on PPOs possess a hydrophobic isoleucine (I) at position HB2+1, group 2 PPOs exhibit a larger, positi

271 -indan-2-carboxylic acid, have been inserted at positions i and i+3 of the pentapeptide Boc-(R)-Aic(N

272 substituting the variable cysteine residues at position III in the protein.

273 For mutant P112A, insertion of K at position K127 (leading to K127KK) of NS2B rescued vir

274 recently reported that SUMOylation of the GR at position K293 in humans (K310 in mice) within the N-t

275 ists, modified with DOTA or NODAGA chelators at positions Lys(27) and Lys(40) and labeled with (68)Ga

276 Conjugation of DOTA and NODAGA chelators at positions Lys(27) and Lys(40) of Ex(9-39)NH2 resulted

277 A virus (IAV) hemagglutinin (HA), especially at position N-27, is crucial for HA folding and virus su

278 uents at position 5 and a tryptophan residue at position N-3 of the rhodanine ring were the most acti

279 While never shown, protonation of adenines at position N1 has been hypothesized to be critical for

280 en conformation, and two new masses appeared at positions near Arp2 and Arp3.

281 ative mechanism involving template switching at positions of microhomology.

282 Strikingly, mutations at positions predicted to be highly frustrated were foun

283 erface are located within the PPRs of LRPPRC at positions predicted to interact with RNA and within t

284 None occurred at positions previously reported to affect the temperatu

285 group I/II and group III involved variation at positions primarily at allosteric sites located outsi

286 ow that PRMT5 targets RUVBL1 for methylation at position R205, which facilitates TIP60-dependent mobi

287 Point mutations at position R882 have been shown to cause a dominant neg

288 osphorylation of human Rab10 and human Rab12 at positions Thr73 and Ser106, respectively, was confirm

289 y modulated by Cdk5-mediated phosphorylation at position threonine-407(mouse)/T406(rat).

290 The reinsertion at positions towards Cluster 2 reinstated the membrane p

291 yme responsible for 2'-O-methyl modification at position U1369 in the human mitochondrial 16S rRNA.

292 L1) and nucleus ambiguus motor pools located at positions where expiratory and laryngeal motor neuron

293 o predicted amino acid variations were found at positions where functional domains of the proteins we

294 taching the donor substituents to the bridge at positions where the molecular orbital coefficients ar

295 cture of the duplex and its affinity for SRA at positions where they were responsive to base flipping

296 within structured domains tend to be located at positions with high conformational flexibility.

297 Conversely, mutations at positions with low frustration were found to correlat

298 In comparing the distributions of bases at positions with respect to an mCpG, statistically sign

299 (MHV-A59) containing ExoN activity [ExoN(+)] at positions within nsp10 known to disrupt the nsp10-nsp

300 o tyrosine (NH2Y) by amber codon suppression at positions Y731 or Y730 and investigation of the NH2Y(