ライフサイエンスコーパス: substrate recognition

1 ion) (dmin = 1.8 A) revealed key features of substrate recognition.

2 ead group of PG as the main determinants for substrate recognition.

3 share their overall architecture and mode of substrate recognition.

4 swapping within eukaryotic thioesterases for substrate recognition.

5 inding site in TRiC and uncover the basis of substrate recognition.

6 iquitin-charged E2 and a separate domain for substrate recognition.

7 to inhibit activity presumably by preventing substrate recognition.

8 s and an extracellular domain positioned for substrate recognition.

9 Cdk12/CycK and analyse its requirements for substrate recognition.

10 eptides, and reveals the mechanism of primed substrate recognition.

11 ociation with PKA and causes a switch in PKA substrate recognition.

12 other PRMTs may employ similar mechanism for substrate recognition.

13 l catalytic activation in addition to simple substrate recognition.

14 entifies hot-spot residues for catalysis and substrate recognition.

15 actions with intracellular proteins prior to substrate recognition.

16 n of ADAM17 involved in its dimerization and substrate recognition.

17 a potential site involved in glutamine-donor substrate recognition.

18 istent with a central role of this region in substrate recognition.

19 eper" mutations in enabling major changes in substrate recognition.

20 e that is required for efficient carboxylate substrate recognition.

21 role of the exosite in the spacer domain in substrate recognition.

22 rved molecular interface that defines enzyme/substrate recognition.

23 5, and delineates the structural elements of substrate recognition.

24 assay to evaluate the role of this region in substrate recognition.

25 necessary for specific acetylation-dependent substrate recognition.

26 an IP(5) 2-K, which shed light on aspects of substrate recognition.

27 olecular determinants for Ac-CoA and tubulin substrate recognition.

28 indicating a common catalytic mechanism and substrate recognition.

29 gated BPH inner pore loop may be involved in substrate recognition.

30 hat conformational selection plays a role in substrate recognition.

31 tion regarding conformational plasticity and substrate recognition.

32 that multiple amino acids are important for substrate recognition.

33 resolution provide insight into cofactor and substrate recognition.

34 eptide repeats of OGT that are essential for substrate recognition.

35 hat the isoprenyl moiety is not required for substrate recognition.

36 s lead to the detailed understanding of VioA substrate recognition.

37 suggesting a role for AR C-terminus in E2/E3 substrate recognition.

38 providing new insight into the mechanism for substrate recognition.

39 ne headgroup is the chemical determinant for substrate recognition.

40 the extrinsic mechanisms that control APC/C-substrate recognition.

41 Mettl14 plays a structural role critical for substrate recognition.

42 ing enzymatic autoinhibition and enabling CN substrate recognition.

43 ht have adopted a unique set of residues for substrates recognition.

44 ides a molecular understanding of how kinase-substrate recognition acts as a gatekeeper to regulate a

45 Cdt2 is the substrate recognition adaptor of CRL4(Cdt2) E3 ubiquitin

46 A model of QueF substrate recognition and a catalytic pathway for the en

47 In contrast to a conserved mode of substrate recognition and a conserved active site, regul

48 ses a catalytic domain sufficient for primed substrate recognition and a multivalent recruitment modu

49 tional selection is an integral component of substrate recognition and access, but direct evidence of

50 However, the molecular basis of Eco1 substrate recognition and acetylation in cohesion is not

51 imulates activity through membrane-dependent substrate recognition and allosteric effects.

52 or membranes and might also be implicated in substrate recognition and allosteric regulation.

53 Each CCT subunit may have distinct substrate recognition and ATP hydrolysis properties.

54 Substrate recognition and binding are critical for the r

55 hat paradoxically couples its own folding to substrate recognition and binding.

56 CipA scaffoldin that may aid in cellulosome substrate recognition and binding.

57 we precisely mapped key residues involved in substrate recognition and catalysis by PI3Kalpha.

58 ur studies illuminate general mechanisms for substrate recognition and catalysis in the UbiA superfam

59 BIA biosynthesis, but the molecular basis of substrate recognition and catalysis is not known for NMT

60 ver, the mechanistic understandings of their substrate recognition and catalysis remain elusive.

61 f the conformational changes associated with substrate recognition and catalysis remain poorly unders

62 mmodate the spatial requirements of pre-mRNA substrate recognition and catalysis.

63 and have identified the residues involved in substrate recognition and catalysis.

64 reby organizing the nuclease active site for substrate recognition and catalysis.

65 nown about regulatory mechanisms, leading to substrate recognition and catalytic activation.

66 tudies provide a deeper understanding of the substrate recognition and catalytic mechanism of Tps2 an

67 ring robustly mediate efficient and accurate substrate recognition and catalytic selectivity.

68 enhancement to uncouple and investigate the substrate recognition and catalytic steps of Fen1 and Fe

69 ch/spacer domains are principal modifiers of substrate recognition and cleavage by both ADAMTS5 and A

70 ins less stringent sequence requirements for substrate recognition and cleavage by matriptase than by

71 main of Drosophila Dicer-2 (dmDcr-2) governs substrate recognition and cleavage efficiency, and that

72 interactions and how coevolution may restore substrate recognition and cleavage in the presence of pr

73 lope, likely enabling coevolution to sustain substrate recognition and cleavage in the presence of PR

74 d forms of RNase P have distinct modules for substrate recognition and cleavage, an unanticipated par

75 solution is required to explain the onset of substrate recognition and collagenolysis.

76 complex for degradation, but the underlying substrate recognition and delivery mechanisms are curren

77 and ClpF form a binary adaptor for selective substrate recognition and delivery to ClpC, reflecting a

78 und structures of BcsA provide the basis for substrate recognition and demonstrate the stepwise elong

79 ty of the Tim23 channel is a key feature for substrate recognition and efficient protein import.

80 complete mechanistic understanding of their substrate recognition and enzymatic activities.

81 es for PARG reveals the minimal features for substrate recognition and enzymatic cleavage.

82 7 linker as a novel mechanism to control 30S substrate recognition and enzymatic turnover.

83 Substrate recognition and excision usually take place in

84 R residues potentially playing dual roles in substrate recognition and in polySia chain polymerizatio

85 ty of repeat domain proteins as scaffolds in substrate recognition and lays the foundation for future

86 g many other SUMO E3s, and are implicated in substrate recognition and ligase activity.

87 stage for future mechanistic studies of TlyA substrate recognition and modification that underpin Mtb

88 that the N-terminus of CARM1 is involved in substrate recognition and nearly indispensable for subst

89 ound in bacterial UGMs yet are important for substrate recognition and oligomerization.

90 ein confer the observed differences in dsRNA substrate recognition and processing behavior of Dicer-d

91 esent general properties of the mechanism of substrate recognition and processing by SENPs and other

92 To comprehend the mechanisms of substrate recognition and processing, we have constructe

93 er, the mechanisms for non-canonical caspase substrate recognition and proteolysis, and the direct ro

94 osure motif complexes, but its mechanisms of substrate recognition and remodeling are unknown.

95 However, critically testing the mechanism of substrate recognition and remodeling by Hsp90 has been c

96 Our results uncover major differences in substrate recognition and S-acylation by these zDHHC enz

97 2*, demonstrating that chaperones can aid in substrate recognition and San1p-dependent protein degrad

98 nctional studies, the mechanisms involved in substrate recognition and selective ubiquitination of it

99 ositol 5-phosphate, which sheds light on the substrate recognition and specificity of PTPMT1.

100 tly cleaved by proteases gives insights into substrate recognition and specificity, guides developmen

101 ycle of these GSTs, including stereospecific substrate recognition and stereoselective formation of b

102 These structures provide insight into substrate recognition and structural changes observed up

103 ST polybasic region plays a critical role in substrate recognition and suggest that different combina

104 periments reveal a new role for Edc3 in mRNA substrate recognition and suggest that this activity is

105 ral insight into the diverse nature of SMYD2 substrate recognition and suggests that the broad specif

106 The structural data provide new insight into substrate recognition and the catalytic mechanism and th

107 main bound to DNA, shedding light on 5mC-DNA substrate recognition and the catalytic mechanism of 5mC

108 es those residues important in catalysis and substrate recognition and the in vivo phenotypes of thes

109 These findings support the idea that both substrate recognition and the intrinsic catalytic activi

110 the WW domain at Ser16 by PKA abrogates both substrate recognition and the nonspecific interactions w

111 estigate how the combination of conventional substrate recognition and the unique topological factors

112 stinct Tom40 conformations playing a role in substrate recognition and therefore in transport functio

113 The structural basis for substrate recognition and translocation is unknown.

114 Key residues that are important for substrate recognition and transport are identified and r

115 t of MdtM may be important for antimicrobial substrate recognition and transport by the protein.

116 on of APC/C subunits and on the mechanism of substrate recognition and Ub chain initiation and extens

117 tained quality control factor that comprises substrate recognition and ubiquitin transfer activities

118 es of both human Miro1 and Miro2 that reveal substrate recognition and ubiquitin transfer to be speci

119 hexaphosphate suggests a molecular basis of substrate recognition, and an entropically driven allost

120 C2 symmetry of this class of organocatalyst, substrate recognition, and asymmetric induction in both

121 ovide insights toward viral protein mimicry, substrate recognition, and key interactive domains contr

122 sphotyrosine substrate, affords insight into substrate recognition, and provides a testable substrate

123 expected role for the ubiquitin E2 enzyme in substrate recognition, and provides insight into how the

124 portant, the underlying rules governing ADAR substrate recognition are not well understood.

125 ases and the details of their regulation and substrate recognition are poorly understood.

126 ed, suggesting either that multiple modes of substrate recognition are possible or that our definitio

127 interactions with residues not essential for substrate recognition, are less likely to be susceptible

128 retain the interactions used for tryptophan substrate recognition as causes for the 1000-fold weaker

129 proximal ATPase domain and a membrane-distal substrate-recognition assembly.

130 roteasomes is a multi-step process involving substrate recognition, ATP-dependent unfolding, transloc

131 rs mimic protease substrates, differences in substrate recognition between proteases may affect their

132 The differences in substrate recognition between these closely related PLpr

133 s that play important roles in antimicrobial substrate recognition, binding and transport by Escheric

134 mall RNA-binding pocket, which may influence substrate recognition/binding and functional specificity

135 ugh a series of subtle changes that maintain substrate recognition but no longer permit inhibitor bin

136 MalF-P2 is thus not only responsible for substrate recognition, but also directly involved in act

137 ent is a composite docking site that confers substrate recognition by both calcineurin and MAPK.

138 We delineate defined rules governing substrate recognition by C5, which reveal specificity th

139 ate-binding surface that explains structured substrate recognition by capturing two adjacent single-s

140 ded proteins can actively and directly alter substrate recognition by cellular proteases.

141 ating a bimodal interaction, we propose that substrate recognition by chaperones and targeting to the

142 or that antagonizes both kinase activity and substrate recognition by Cln1/2-Cdk complexes.

143 , CSA, and A238L all prevent "LxVP"-mediated substrate recognition by CN, highlighting the importance

144 understanding of the molecular mechanism of substrate recognition by CRL4(Cdt2) and how this E3 liga

145 The molecular determinants for substrate recognition by DASS remain obscure, largely ow

146 nistic basis for the observed specificity in substrate recognition by FAP, but not by DPPIV or PREP.

147 ovide insights into metal ion activation and substrate recognition by Fur that suggest pathways to en

148 nobserved mechanism for high-fidelity kinase-substrate recognition by in vitro kinase assays, examina

149 They provide experimental insights into substrate recognition by KPC-2 and its unique cephalospo

150 rystal structure also provides insights into substrate recognition by lantibiotic dehydratases.

151 multiple features of HLA-DR are involved in substrate recognition by MARCH8.

152 tween OCT3 and OCT1 and to the mechanisms of substrate recognition by OCTs in general.

153 use in elucidating the mechanisms of Pup and substrate recognition by PafA.

154 and amino acid sequence might be involved in substrate recognition by POPs.

155 wever, the molecular mechanism of nucleosome substrate recognition by PRC1 or other chromatin enzymes

156 Here the authors give insights into OGA substrate recognition by presenting four human OGA struc

157 Our findings underscore the complexity of substrate recognition by RNA modification enzymes and th

158 ities, understanding the structural basis of substrate recognition by SBPs has remained very challeng

159 tures are located at strategic positions for substrate recognition by shape and coordination of the c

160 It is widely believed that substrate recognition by such enzymes involves a series

161 ilities of their methylation helices prevent substrate recognition by the adaptation enzymes.

162 oligomerization of the complex and prevents substrate recognition by the catalyst.

163 We therefore conclude that substrate recognition by the FXIa exosite(s) requires di

164 ructural elements required for catalysis and substrate recognition by the HPP family of enzymes withi

165 ates assembled by the APC/C strongly enhance substrate recognition by the proteasome, thereby driving

166 required for translocation, the mechanism of substrate recognition by the T3SS is unknown.

167 Factors mediating substrate recognition by the type VI secretion system (T

168 oducts distinguish these LTs with respect to substrate recognition, catalytic activity, and relative

169 Overall, this work provides an insight into substrate recognition, catalytic mechanism for acetyl tr

170 solution, we propose a mechanistic model for substrate recognition, commitment, deubiquitylation, and

171 catalytic site are a key feature of several substrate recognition complexes.

172 tivation of the SCF-type E3 ubiquitin ligase substrate recognition component Fbw7 induces pancreatic

173 n as Fbxw7, hCdc4 and Sel-10) functions as a substrate recognition component of a SCF-type E3 ubiquit

174 Here, we show that beta-TrCP, the substrate recognition component of an E3 ubiquitin ligas

175 in 1 (SKP1), suggesting that LEF-7 acts as a substrate recognition component of SKP1/Cullin/F-box (SC

176 t, Ras-regulated complex with beta-TrCP, the substrate recognition component of the SCF(beta-TrCP) ub

177 Fbw7 is the substrate recognition component of the Skp1-Cullin-F-box

178 de structural insights into the mechanism of substrate recognition coupled enzymatic activation withi

179 IF and collagen PHDs reveals conservation in substrate recognition despite diverse biological roles a

180 thway via a series of tightly coupled steps: substrate recognition, dislocation, and ubiquitin-depend

181 The mechanism of substrate recognition displayed by the enzyme, however,

182 Thus, this work has uncovered a conserved substrate recognition domain in DNA repair enzymes that

183 Here we describe a substrate recognition domain within ZRANB3 that is neede

184 t divergent missense mutations affecting the substrate-recognition domain of the ubiquitin ligase ada

185 We instead targeted the substrate-recognition domain of TNKS, as it is unique am

186 PCH-2 possesses a substrate-recognition domain related to those of the pro

187 VHZ also lacks substrate recognition domains and other domains typicall

188 Thus, substrate recognition domains are a common feature of fo

189 monstrate that the leucine-rich repeat (LRR) substrate recognition domains of different IpaH enzymes

190 We present here crystal structures of the substrate recognition domains of Mib1, both in isolation

191 ays, show that Mib1 contains two independent substrate recognition domains that engage two distinct e

192 neral structural feature used by kinases for substrate recognition during signaling.

193 d use of folded and intrinsically disordered substrate recognition elements as the molecular basis fo

194 of the pump and have provided insights into substrate recognition, energy coupling and the transduct

195 s the importance of the N-terminal domain in substrate recognition, explains the activity restoration

196 ER-associated E3 ligases, which coordinate substrate recognition, export, and proteasome targeting,

197 wnregulation of the ubiquitin ligase complex substrate recognition factors SOCS5/6.

198 ng protein chaperones, peptidases, and their substrate recognition factors.

199 IBM, and this interaction, in turn, provides substrate recognition for c-IAP1 mediated ubiquitylation

200 th tRNAPhe revealed the structural basis for substrate recognition, identified the active site locati

201 plastic region in TAT has been implicated in substrate recognition in other GCN5 superfamily acetyltr

202 interactions play a larger role than enzyme-substrate recognition in the evolution or design of cata

203 hexanoyl-CoA, reveal the molecular basis for substrate recognition, inspiring the development of meth

204 rporate homodimerization, Cul3 assembly, and substrate recognition into a single multidomain protein,

205 This supports a model in which substrate recognition is associated with the open-to-clo

206 ing the molecular mechanisms underlying OCT3 substrate recognition is critical for the rational desig

207 ctions and sequence alignments suggests that substrate recognition is exquisitely conserved among euk

208 We also provide evidence that Parkin substrate recognition is functionally separate from subs

209 The SSB-ribosome cycle and substrate recognition is modulated by its ribosome-bound

210 However, the structural basis of its substrate recognition is not well understood.

211 sical secretion signals and the mechanism of substrate recognition is not well understood.

212 Substrate recognition is one of the hallmarks of enzyme

213 1 substrates are known, and its mechanism of substrate recognition is poorly understood.

214 orters are available, a structural basis for substrate recognition is still lacking.

215 g of its ATP-dependent folding mechanism and substrate recognition is therefore of great importance.

216 influence the more than 12 000-times weaker substrate recognition (KM = 34.5 +/- 1.6 muM).

217 Together, our study demonstrated the substrate recognition mechanism by the Hat1p/Hat2p compl

218 We discuss implications of this substrate recognition mechanism for the biogenesis and q

219 sults identified a new phosphorylation-based substrate recognition mechanism of PTPN12 by CDK2, which

220 ll kinase activity and the variations in the substrate recognition mechanism.

221 se results demonstrate that the CBM-mediated substrate-recognition mechanism is evolutionarily conser

222 ClpS1 function, substrates, and substrate recognition mechanisms are discussed.

223 coveries of novel classes of E3s and diverse substrate recognition mechanisms.

224 e the overall architecture, characterize the substrate recognition model, identify critical residues,

225 inate the juxtaposition of the catalytic and substrate-recognition modules.

226 We demonstrate that a prominent substrate recognition motif consists of a pair of argini

227 led us to propose PK/RTXS/T/V/NGKX2K/R as a substrate recognition motif.

228 Substrate recognition of A-PGS versus L-PGS was investig

229 Substrate recognition of BchC was investigated using six

230 To probe substrate recognition of DPA, we developed a general and

231 Tsr-RNA interaction in which the coordinated substrate recognition of each Tsr structural domain is a

232 sites is critical for the autoinhibition and substrate recognition of the eight Src family kinases (S

233 offered a template to model the mechanism of substrate recognition of the enzyme.

234 he ESX-1 system, which allowed us to compare substrate recognition of these two T7S systems.

235 ts shed light on the catalytic mechanism and substrate recognition of zgammaGH and other gamma-glutam

236 s has identified EcRppH residues crucial for substrate recognition or catalysis.

237 ture-based mutations that disrupt bifurcated substrate recognition or oligomerization both compromise

238 nations for these associations in regards to substrate recognition or physical environment.

239 ate in either undecaprenyl phosphate-l-Ara4N substrate recognition or transfer of l-Ara4N to the LPS.

240 The structural comparison of substrate recognition pattern between these complexes al

241 the biosynthetic process involves a complex substrate recognition pattern by the enzyme and interpla

242 es in the carbohydrate-binding module form a substrate recognition "pinch point" that we propose aids

243 enzyme inhibition at the highly conservative substrate-recognition pocket.

244 gous expression systems to establish a broad substrate recognition profile of SbMATE, showing the pro

245 s, the unique side chain-independent mode of substrate recognition provides a clear explanation for D

246 imics have provided additional insights into substrate recognition, providing the basis for further e

247 lded an SB transposon version with optimized substrate recognition (pT4).

248 The substrate recognition regions of the two proteins are ra

249 omplex has been determined, the mechanism of substrate recognition remains elusive.

250 e catalytic mechanism and molecular basis of substrate recognition remains poorly understood.

251 The RP coordinates substrate recognition, removal of substrate polyubiquiti

252 he substrate binding features locate the key substrate recognition residues not only around the heme

253 ion and that separate control of induced-fit substrate recognition sets up the catalytic selectivity

254 d with a Thr498 --> Ser498 substitution in a substrate recognition site (SRS).

255 ckbone to occupy additional sites within the substrate recognition site of BRD4(1).

256 The substrate recognition site of Pin1 performs specific and

257 titively inhibits CN by occupying a critical substrate recognition site, while leaving the catalytic

258 close contacts to the B-B' loop of CYP3A4, a substrate recognition site.

259 ro and revealed a greater flexibility in its substrate recognition site.

260 t address previously untargeted areas of the substrate recognition site.

261 cts with misfolded proteins through distinct substrate recognition sites and conjugates these protein

262 and simultaneous utilization of two distinct substrate recognition sites on Lon, an HspQ binding site

263 and high sequence conservation that serve as substrate-recognition sites San1 uses to target its diff

264 Pases that serve different functions such as substrate recognition, substrate unfolding, and assembly

265 box (ASB) family of proteins function as the substrate recognition subunit in a subset of Elongin-Cul

266 ed that mutation of fbxw7, which encodes the substrate recognition subunit of a SCF ubiquitin ligase

267 ing the von Hippel-Lindau protein (VHL), the substrate recognition subunit of an E3 ligase, and an im

268 We identified the F-box protein cyclin F, a substrate recognition subunit of an SCF (Skp1-Cul1-F-box

269 tability by limiting the binding of the cdh1-substrate recognition subunit of APC/C ubiquitin ligase

270 beta-TrCP, the substrate recognition subunit of SCF-type ubiquitin liga

271 large numbers of F-box proteins (FBPs), the substrate recognition subunit of SKP1-CULLIN-F-box (SCF)

272 PPFR-1 interacted with MEL-26, the substrate recognition subunit of the CUL-3 RING E3 ligas

273 Kbtbd2 encodes a BTB-Kelch family substrate recognition subunit of the Cullin-3-based E3 u

274 AUF1 is a target of beta-TrCP, the substrate recognition subunit of the E3 ubiquitin ligase

275 The von Hippel-Lindau protein (pVHL) is the substrate recognition subunit of the VHL E3 ligase that

276 nanomolar potency, led to degradation of the substrate recognition subunit Skp2 in cells, and reduced

277 uires the Cul4-Roc1-DDB1 E3 ubiquitin ligase substrate recognition subunit VprBP.

278 tein Vpu binds to both BST-2 and betaTrCP, a substrate-recognition subunit for the SCF (Skip1-Cullin1

279 As a substrate-recognition subunit in the Elongin BC-containi

280 E1 by repressing the expression of FBXW7, a substrate-recognition subunit of the SCF E3 ubiquitin li

281 t upon expression of the E3 ubiquitin ligase substrate-recognition subunit ZIF-1, proteins tagged wit

282 complexes can engage variant ubiquitination substrate recognition subunits, and we found the F-box p

283 uitination and ultimately degradation of the substrate recognition subunits.

284 ligases containing FBXW11 and beta-TRCP1 as substrate recognition subunits.

285 que but overlapping sets of PBR residues for substrate recognition, that the NCAM-recognizing PBR sit

286 ously provide a mechanism to directly couple substrate recognition to activity.

287 , suggesting that Swc5 is required to couple substrate recognition to ATPase activation.

288 The VHL gene product, pVHL, is the substrate recognition unit of an ubiquitin ligase that t

289 To examine the mechanism of Dis3l2 substrate recognition we determined the structure of mou

290 To investigate CN substrate recognition we used X-ray crystallography, bio

291 in consensus structures/sequences needed for substrate recognition, we demonstrate that RPP21*RPP29 a

292 To elucidate the mechanism of substrate recognition, we determined the crystal structu

293 atures of the APN pharmacophore required for substrate recognition were elucidated by x-ray crystallo

294 In particular, this includes substrate recognition, what properties render a given su

295 gesting that Arg(82) plays a general role in substrate recognition, whereas Arg(93) specifically func

296 might have evolved to support flexibility in substrate recognition while catalyzing efficient, high-f

297 only for understanding the mechanism of the substrate recognition with PRNTase but also for designin

298 roper control of mitosis that connects APC/C substrate recognition with the SAC.

299 vestigated the molecular determinants of FIH substrate recognition, with a focus on differences betwe

300 n an effort to identify residues involved in substrate recognition, X-ray crystal structures of a C-t