ライフサイエンスコーパス: covalent modification

1 immobilized to the graphene surface via non-covalent modification.

2 vidence that His-50 is the main site of this covalent modification.

3 e enhanced by kinase activation or oxidative covalent modification.

4 r positive allosteric modulator activity via covalent modification.

5 loss, which is a characteristic signature of covalent modification.

6 tive stress and altering protein function by covalent modification.

7 notion that the electrophile, DMF, acts via covalent modification.

8 from screening campaigns modulate GLP-1R by covalent modification.

9 y via small molecule allosteric effectors or covalent modification.

10 equently regulated through posttranslational covalent modifications.

11 ure GFP containing the desired site-specific covalent modifications.

12 primarily by recognizing sequence motifs or covalent modifications.

13 rted interference of different unanticipated covalent modifications.

14 Upon this ROS-dependent, reversible, covalent modification, a marked decrease in its catalyti

15 omponents, structure, chromatin folding, and covalent modifications across the human cell cycle.

16 Covalent modification adding acetyl groups to the C term

17 made in recent years to understand how these covalent modifications affect cell identity and function

18 duction is predominantly involved in protein covalent modification after exposure in vivo to styrene

19 e indeed substrates for CaMKII and that this covalent modification alters the expression of cell surf

20 nyl diazirine and alkyne moieties that allow covalent modification and enrichment of kinases, respect

21 The accumulation of 2AA leads to covalent modification and inactivation of several enzyme

22 species, deregulation of Ca(2+) homeostasis, covalent modification and oxidation of proteins, lipid p

23 rooxidant activity of Abeta leads to its own covalent modification and to accelerated amyloidogenesis

24 Histone covalent modifications and 26S proteasome-mediated prote

25 nce silencing) through modulation of histone covalent modifications and association of silencing fact

26 Chromatin proteins undergo covalent modifications and form complexes that encode a

27 a fundamental tool for detecting and mapping covalent modifications and quantifying their changes.

28 failed to protect inactivation of GAPDH, its covalent modification, and translocation to the nucleus.

29 inal microvascular cells is inhibited by its covalent modifications, and this activates multiple path

30 Allostery and covalent modification are major means of fast-acting met

31 Combinations of histones carrying different covalent modifications are a major component of epigenet

32 Hydrogen-bonding promoted covalent modifications are finding useful applications i

33 While a number of covalent modifications are known to occur on histone tai

34 These stable, heritable, covalent modifications are largely associated with the r

35 losteric regulation, product inhibition, and covalent modification as well as alterations in gene tra

36 he first report that identifies H2O2-induced covalent modifications as an essential component for the

37 A, CaMKII) and postsynaptic (Ca(2+), CaMKII) covalent modifications, as well as both presynaptic and

38 ed tryptic peptides have shown evidence of a covalent modification at the N-terminus and a noncovalen

39 Covalent modification at two conserved cysteine residues

40 ferent time points during folding introduces covalent modifications at solvent accessible side chains

41 ovative technique for incorporating multiple covalent modifications at specific sites in covalently c

42 ctivation of the nucleotide that involves no covalent modification but only electrostatic polarizatio

43 lling activity of the target protein through covalent modification, but accumulating evidence points

44 The covalent modification by (2-(trimethylammonium)ethyl) me

45 lpha DNA-binding domain (DBD) as targets for covalent modification by 15d-PGJ(2).

46 and can be irreversibly inactivated through covalent modification by a mechanism-based inhibitor, wh

47 system, protein substrates are degraded via covalent modification by a polyubiquitin chain.

48 erall activity or function but allows direct covalent modification by a small-molecule probe containi

49 Owing to their covalent modification by cholesterol and palmitate, Hedg

50 and several nucleophilic side chains undergo covalent modification by ethyl diazoacetate (EDA).

51 a) accessibility of substituted cysteines to covalent modification by methanesulfonate reagent depend

52 One potential mechanism involves covalent modification by reactive carbonyls of apolipopr

53 ed to activate IKs channels depends on their covalent modification by small ubiquitin-like modifier (

54 Covalent modification by small ubiquitin-related modifie

55 Pro-1 is the sole site of covalent modification by the ( R) and ( S) enantiomers.

56 was identified as the residue that undergoes covalent modification by the 12,13-epoxide group of trip

57 pectrometry identified Cys475 as the site of covalent modification by the active metabolite.

58 bitory flavonoids to alpha-synuclein and the covalent modification by the flavonoid quinone led to th

59 rate, protected L393C, I397C, and T400C from covalent modification by the MTS reagents.

60 eic acid, and the structural consequences of covalent modification by these two inhibitors are fundam

61 Post-translational covalent modification by ubiquitin and ubiquitin-like pr

62 Recognition of histone covalent modifications by chromatin-binding protein modu

63 UV-activated aromatic azide, mapping of the covalent modifications by liquid chromatography-tandem m

64 ation by one tail shock involves presynaptic covalent modifications by protein kinase A (PKA) and Cam

65 and/or multiple sites of post-translational covalent modification can be modeled using reaction rule

66 The kinetics of covalent modification can be monitored spectroscopically

67 ved complex, which is a prerequisite for the covalent modification chemistry to occur.

68 n of methionine residues is reversible, this covalent modification could also function as a mechanism

69 or one or both forms of the substrate of the covalent modification cycle affected the steady-state ou

70 by the out-of-equilibrium properties of the covalent modification cycle controlling Cdk1 activity.

71 esult in subsensitive responses, even if the covalent modification cycle displays significant ultrase

72 ream target on the signaling properties of a covalent modification cycle, an example of retroactivity

73 roperties of an upstream signal transduction covalent modification cycle.

74 Covalent modification cycles (systems in which the activ

75 Here, we analyze the properties of covalent modification cycles and ligand/receptor interac

76 Covalent modification cycles are basic units and buildin

77 nt spatial aspects of signal transduction in covalent modification cycles by starting with a basic te

78 the systematic understanding of signaling in covalent modification cycles, pathways, and networks in

79 Such covalent modification cycles, triggered by transcription

80 Among different covalent modifications found on p53 the most controversi

81 Histone tail covalent modifications have been extensively studied, bu

82 cent studies indicate that, similar to other covalent modifications, histone lysine methylation is su

83 Here we identify a distinct function of this covalent modification in controlling the later proteolyt

84 rged residues is an effective alternative to covalent modification in increasing factor VIII (VIIIa)

85 The biologic role of this covalent modification in regulating cell function is not

86 best satisfied by including a mutation and a covalent modification in the C-terminal part, and the as

87 ylation is one of the most prevalent protein covalent modifications in eukaryotes and is mediated by

88 determined the presence of such variants and covalent modifications in seven tissue types of the anur

89 alpain-1 with iso[4]LGE2 in vitro results in covalent modification, inactivation, the formation of hi

90 l mono-acetylation at LYS-16, which is a key covalent modification, induces a significant reorganizat

91 Such covalent modifications involve extensive preparative and

92 Regulation by covalent modification is a common mechanism to transmit

93 sible inhibitor scaffold to demonstrate that covalent modification is not a requirement for activity

94 idopsisthaliana) the isothiocyanate provokes covalent modification (K4me3, K9ac) of histone H3 in the

95 However, how covalent modification leads to channel opening is not un

96 st that dynamic counterbalance by reversible covalent modification may be a general strategy for cont

97 Together, our results suggest covalent modification may be used to stabilize the GLP-1

98 ARP-1 and -2 are regulated by DNA breaks and covalent modifications, mechanisms of PARG regulation ar

99 is report improves the repertoire of peptide covalent modification methods by exploiting the syntheti

100 olvent at ambient temperatures suggests that covalent modification might be involved in the Golgi-alt

101 we use particle-based simulation to study a covalent modification network in which the activating co

102 to CXCL12, indicates the importance of this covalent modification not only in marking receptors for

103 The apparent covalent modifications occurred in the cytoplasm within

104 Covalent modification of 8A11 with amine-reactive deriva

105 ective inhibitor of the Ag85 complex through covalent modification of a cysteine residue proximal to

106 ctive metabolite (AM) of clopidogrel and the covalent modification of a cysteinyl residue of human cy

107 Covalent modification of a drug with a peptide moiety ha

108 Postsynthetic covalent modification of a metal-organic framework (MOF)

109 s of NO are mediated by S-nitrosylation, the covalent modification of a protein cysteine thiol by an

110 Catalyzing the covalent modification of aliphatic amino groups, such as

111 n-ortho-quinone adducts showed that although covalent modification of alpha-syn occurs, this does not

112 ases AR transcriptional activity through the covalent modification of an AR-specific coregulatory pro

113 Thus, covalent modification of beta-1,6-GlcNAc by N-deacetylat

114 these findings, it can be proposed that the covalent modification of beta-lactoglobulin functions as

115 iarylphosphines has been employed for direct covalent modification of biomolecules with probes in the

116 Reversible inactivating covalent modification of BiP is believed to contribute t

117 Acute hyperglycaemia causes covalent modification of CaMKII by O-linked N-acetylgluc

118 Thus, SUMOylation is a covalent modification of caveolins that influence the re

119 The E114Q mutant slows covalent modification of Cg10062 but does not prevent it

120 CIATED NEDD8-DISSOCIATED1 participate in the covalent modification of CULLIN1 by RELATED TO UBIQUITIN

121 Covalent modification of cullins by the ubiquitin-like p

122 Likewise, the covalent modification of Cys residues at selected positi

123 group acts as inhibitor of catBoNT/A through covalent modification of Cys(165).

124 ast in part, by inhibiting NF-kappaB through covalent modification of Cys(62) of the p50 subunit of N

125 cket of the p50 were constructed through the covalent modification of Cys(62); the models reveal that

126 We conclude by demonstrating that covalent modification of Cys118 on Ras leads to a novel

127 Conclusive evidence for the covalent modification of Cys181 is provided from enzyme

128 2-oxo-clopidogrel inactivates CYP2B6 through covalent modification of Cys475.

129 Through covalent modification of cysteine and lysine residues, T

130 ctivate both insect and vertebrate TRPA1 via covalent modification of cysteine residues in the amino-

131 bit the protein-protein interactions through covalent modification of cysteine residues within the RG

132 hat 15d-PGJ(2) can block ERalpha function by covalent modification of cysteine residues within the vu

133 d by a variety of reactive irritants via the covalent modification of cysteine residues.

134 These exogenous compounds activate TRPA1 by covalent modification of cysteine residues.

135 Activation of hPLCbeta3 by U73122 required covalent modification of cysteines as evidenced by the o

136 has been demonstrated to be mediated through covalent modification of cytoplasmic cysteines located i

137 hilic agents activate these channels through covalent modification of cytosolic cysteine residues, th

138 The turnover process utilizes covalent modification of D244, requiring two transition-

139 Covalent modification of DNA and histones, also termed e

140 Cytosine methylation is the most common covalent modification of DNA in eukaryotes.

141 as been demonstrated that DNA methylation, a covalent modification of DNA that can regulate gene expr

142 tional modifications of nuclear proteins and covalent modification of DNA, result in potent regulatio

143 city is believed to occur mainly through its covalent modification of DNA, resulting in the formation

144 visible light, which induces ligand loss and covalent modification of DNA.

145 -MS) is the method of choice for analysis of covalent modification of DNA.

146 were evaluated for each of the proteins: (1) covalent modification of electron-rich amino acids (asse

147 a robust mechanism tuning TRPV1 activity via covalent modification of evolutionarily conserved cystei

148 Flurazepam and zolpidem significantly slowed covalent modification of gamma(2)R197C, whereas DMCM, GA

149 Covalent modification of graphene by organic diazonium s

150 imicrobial effector genes, also required the covalent modification of histone H3 at gene promoters.

151 Covalent modification of histones by protein arginine me

152 Covalent modification of histones by ubiquitylation is a

153 Covalent modification of histones is a fundamental mecha

154 Covalent modification of histones on chromatin is a dyna

155 a may produce certain of its effects through covalent modification of host proteins.

156 chimeras and the assessment of the effect of covalent modification of introduced Cys at the domain-do

157 ust have two distinct binding sites, because covalent modification of its free cysteines with N-ethyl

158 Mutagenesis studies showed that covalent modification of just Cys81 is sufficient to inh

159 l products that modify Keap1 does not detect covalent modification of Keap1 by some highly reversible

160 es that decrease NRF2-ubiquitination through covalent modification of KEAP1 cysteine residues, but su

161 DNA methylation, the only known covalent modification of mammalian DNA, occurs primarily

162 Cytosine methylation is the major covalent modification of mammalian genomic DNA and plays

163 Postsynthetic covalent modification of metal-organic frameworks (MOFs)

164 xposure irreversibly inhibits respiration by covalent modification of mitochondrial cytochrome oxidas

165 Covalent modification of nucleosomal histones is an impo

166 genome by altering the epigenome, including covalent modification of nucleosomal histones.

167 y elements and germline transcription in the covalent modification of nucleosomes at Ag receptor loci

168 ion of ATP hydrolysis is irreversible due to covalent modification of P-gp.

169 We identify covalent modification of p300 by the dicarbonyl metaboli

170 that 3-HPAA inactivation did not result from covalent modification of PGHS-2 or damage to the heme mo

171 PUVA increases the order of lipid phases by covalent modification of phospholipids, thereby inhibiti

172 soluble precursors, products and lipids, and covalent modification of phosphorylation, while in vivo

173 Covalent modification of primary amine groups in multipl

174 periment with Cg10062 does not result in the covalent modification of Pro-1.

175 nactivated after one turnover because of the covalent modification of Pro-1.

176 Covalent modification of protein by drugs may disrupt se

177 The covalent modification of protein substrates by ubiquitin

178 However, the questions of whether covalent modification of proteins by IsoLGs are subject

179 hr phosphorylation is the primary reversible covalent modification of proteins in eukaryotes.

180 nsduction mechanisms: protein binding, and a covalent modification of proteins termed protein pyropho

181 ed ROS generation, site-specific, reversible covalent modification of proteins, particularly oxidatio

182 rylhydrazone approach for the chemoselective covalent modification of QDs that is compatible with neu

183 When bound to Rab1, LidA interfered with the covalent modification of Rab1 by phosphocholination or A

184 analogues were potent inhibitors, effecting covalent modification of recombinant Cal1 catalytic doma

185 lts suggest the feasibility of DNA-catalyzed covalent modification of side chains of large protein su

186 ROS are modulated in large part through the covalent modification of specific cysteine residues foun

187 vatize the triazine with an electrophile for covalent modification of target proteins, an alkyne as a

188 ences indicate that distal damage occurs via covalent modification of the 5'-adjacent dG, but there i

189 fomycin, which specifically inhibits MurA by covalent modification of the active site residue Cys-115

190 active-site directed manner consistent with covalent modification of the active site.

191 ment of NHS from NHS esters with concomitant covalent modification of the arginine residue.

192 suicide substrate for MIF, resulting in the covalent modification of the catalytically active NH(2)-

193 ty of this ubiquitin ligase is regulated via covalent modification of the Cullin-1 subunit by the ubi

194 Covalent modification of the Cys residues with a structu

195 a mutated human alphaB-crystallin (K90C) by covalent modification of the cysteine residue with N-(2-

196 Reversible covalent modification of the DNA via N3 of adenine occur

197 d coronavirus 3CLpro inhibitors that act via covalent modification of the enzyme, 16-(R) is a noncova

198 n turn acts as a suicide inhibitor of SPT by covalent modification of the essential catalytic lysine.

199 resulting in partial oxidation, reduction or covalent modification of the graphene sheets.

200 In 3, covalent modification of the interacting proteins procee

201 S inactivation of reduced 2-KPCC occurs with covalent modification of the interchange thiol (Cys(82))

202 Covalent modification of the membranes was achieved by r

203 Covalent modification of the metastable helicates preven

204 Third, covalent modification of the nanowire device surfaces wi

205 In this paradigm, covalent modification of the NP with cell-targeting moti

206 potency through a reversible or irreversible covalent modification of the nucleophile Ser241 in the u

207 Covalent modification of the pi-electron basal planes of

208 ne quinone, dilution-independent, suggesting covalent modification of the protein by the catecholamin

209 e subunit of bistramide A is responsible for covalent modification of the protein in vitro and in A54

210 Covalent modification of the proteome by SUMO is critica

211 Covalent modification of the specific cysteine residue(s

212 n-mediated signaling events, which involve a covalent modification of the substrate protein by a sing

213 crease in fluorescence quantum yield and not covalent modification of the SWCNT or scavenging of reac

214 Limitations with these systems include covalent modification of the target complement to the ar

215 th tritylium tetrafluoroborate resulted in a covalent modification of the terminal O-atom, and cleava

216 e was uncoupled from membrane binding by the covalent modification of the undecapeptide cysteine thio

217 The covalent modification of therapeutic biomolecules has be

218 osides in clinical bacterial isolates is the covalent modification of these antibiotics by enzymes pr

219 Mutation and covalent modification of these residues have charge-depe

220 f the acetylenic group of 9EP and subsequent covalent modification of Thr 302.

221 To characterize the effect of covalent modification of Thr302, tBPA-modified P450 2B4

222 subject to irreversible photodamage through covalent modification of tryptophans (Trps) and other UV

223 In summary, covalent modification of TSC2 by iNOS-derived NO is asso

224 CCG-4986 inhibits RGS4 function through the covalent modification of two spatially distinct cysteine

225 ersensitivity reactions that can result from covalent modification of unintended targets.

226 tryptic peptide anions is consistent with a covalent modification of unprotonated primary amines (i.

227 We have investigated the potential use of covalent modification of VSV with polyethylene glycol (P

228 nhibitor of eukaryotic transcription through covalent modification of XPB, a subunit of the general t

229 Epigenetic information encoded in covalent modifications of DNA and histone proteins regul

230 The epigenetic mechanisms involve covalent modifications of DNA and histones, which affect

231 etazoan gene expression includes coordinated covalent modifications of DNA and its associated histone

232 cused on the regulatory relationship between covalent modifications of histone H3 lysine 9 (H3K9) and

233 Covalent modifications of histone proteins have profound

234 DNA methylation and covalent modifications of histone tails contribute to ch

235 Covalent modifications of histones have an established r

236 Covalent modifications of histones integrate intracellul

237 ey determine the use of histone variants and covalent modifications of histones, can be among those t

238 Covalent modifications of histones, such as acetylation,

239 epigenetic regulation by DNA methylation and covalent modifications of histones.

240 Covalent modifications of intracellular proteins, such a

241 In vivo positioning and covalent modifications of nucleosomes play an important

242 g RNAs that form ribonucleoproteins to guide covalent modifications of ribosomal and small nuclear RN

243 The epigenome includes covalent modifications of the DNA and its associated pro

244 Covalent modifications of the histone (H) code consisted

245 Diverse covalent modifications of the lipid A moiety may occur d

246 n structure that include DNA methylation and covalent modifications of the proteins that bind DNA.

247 g process of SV40 Vp1 by stimulating certain covalent modifications of Vp1 or by recruiting certain c

248 at least partly achieved through changes in covalent modifications on DNA and histones.

249 The structure explains how covalent modifications on H4K16 and H3K79 regulate forma

250 ructure through ATP-dependent remodeling and covalent modifications on histones play important roles

251 Covalent modifications on therapeutic proteins are tradi

252 sting change in receptor molecules, either a covalent modification or conformation that enhances thei

253 altering contacts at this A1-C2 junction by covalent modification or increasing hydrophobicity incre

254 suggest that H3 cleavage may be regulated by covalent modifications present on the histone tail itsel

255 Covalent modification provides a mechanism for modulatin

256 This covalent modification redirects the de-excitation pathwa

257 For autoantigens, covalent modifications represent a mechanism to sidestep

258 Thr(328)) in the activation loop is the only covalent modification required for kinase activation in

259 for a better understanding of the underlying covalent modifications responsible for the charge differ

260 Overall, examining the spatial dimension of covalent modification reveals that 1), there are importa

261 uding regulation of cotranslational folding, covalent modifications, secretion, and expression level.

262 order structure is affected well beyond the covalent modification site.

263 function at spindle poles by extending from covalent modification sites on PARP-5a and NuMA and bind

264 display many of the attributes of reversible covalent modifications such as protein phosphorylation o

265 Covalent modifications, such as methylation and demethyl

266 can bind either ligand in the absence of any covalent modifications, such as oxidation.

267 rotein SidD that hydrolytically reverses the covalent modification, suggesting a tight spatial and te

268 etely protect the beta2M286C suflhydryl from covalent modification, suggesting close steric interacti

269 This contrasts with the well-mixed covalent modification system studied by Goldbeter and Ko

270 sphorylation, ubiquitylation is a reversible covalent modification that regulates the stability, acti

271 onsequences of phosphorylating serine 381, a covalent modification that turns off F-actin bundling ac

272 on-channel signaling to epigenetic chromatin covalent modifications that affect gene expression patte

273 uding UV shadowing and heat annealing, cause covalent modifications that alter folding behavior.

274 eome consists of reversible and irreversible covalent modifications that link redox metabolism to bio

275 In contrast, covalent modifications that may regulate its action afte

276 Control is achieved through several covalent modifications that occur both on DNA and chroma

277 Activation of Nrf2 by covalent modifications that release it from its inhibito

278 small nuclear RNAs (snRNAs) undergo multiple covalent modifications that require guide RNAs to direct

279 The adaptation helices undergo reversible covalent modifications that tune the stimulus-responsive

280 of sequestering reactive metabolites through covalent modification, thereby limiting their exposure t

281 te drugs in this and other systems by simple covalent modification to form lipophilic analogs that re

282 d add quantitation of protein expression and covalent modification to the arsenal of techniques for c

283 lorimetry, and NMR titrations indicated that covalent modifications to a carrier protein modulate dom

284 can differ from its neighbors as a result of covalent modifications to both the DNA and the histone p

285 Covalent modifications to histones play important roles

286 These changes include covalent modifications to the DNA and histones as well a

287 Such information exists in the form of covalent modifications to the histone proteins that comp

288 The relevance of these covalent modifications to the several functions ascribed

289 es revealed that LRAT undergoes spontaneous, covalent modification upon incubation with a variety of

290 These QDs are amenable to covalent modification via simple carbodiimide coupling c

291 These data demonstrated that our non-covalent modification was able to alter Ad's interaction

292 The covalent modification was characterized, and we establis

293 The site of covalent modification was mapped to a cysteine residue l

294 Covalent modification was surprising because the accumul

295 e receptor is a conformational change and/or covalent modification, which then sets in motion a signa

296 findings provide a physiological role for a covalent modification widespread in nature and suggest p

297 The disruption of the sarcin/ricin domain by covalent modification with either sarcin or pokeweed ant

298 Toward these objectives, covalent modification with poly(ethylene glycol) (PEG) h

299 ated with unintegrated DNAs become marked by covalent modifications, with a delay relative to the tim

300 Our results indicate that covalent modifications within this pocket may alter inte