ライフサイエンスコーパス: substrate recognition

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

2 ave provided valuable insights into protease substrate recognition.

3 other PRMTs may employ similar mechanism for substrate recognition.

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

5 that multiple amino acids are important for substrate recognition.

6 ts of blood-brain barrier diffusion and FAAH substrate recognition.

7 resolution provide insight into cofactor and substrate recognition.

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

9 we investigated the molecular details of its substrate recognition.

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

11 ng convergence on a common solution for tRNA substrate recognition.

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

13 providing new insight into the mechanism for substrate recognition.

14 ne headgroup is the chemical determinant for substrate recognition.

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

16 Mettl14 plays a structural role critical for substrate recognition.

17 ing enzymatic autoinhibition and enabling CN substrate recognition.

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

19 cial role of the insertion domain in MvcA in substrate recognition.

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

21 share their overall architecture and mode of substrate recognition.

22 swapping within eukaryotic thioesterases for substrate recognition.

23 superfamily based on reaction mechanism and substrate recognition.

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

25 residues essential for Cd-SrtB catalysis and substrate recognition.

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

27 to inhibit activity presumably by preventing substrate recognition.

28 s and an extracellular domain positioned for substrate recognition.

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

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

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

32 r binding site primed for aliphatic aldehyde substrate recognition.

33 l catalytic activation in addition to simple substrate recognition.

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

35 identified specific determinants involved in substrate recognition.

36 the structurally unique insertion domain in substrate recognition.

37 sted that these interactions influence pUL97 substrate recognition.

38 enzyme utilizes hydrophobic interactions for substrate recognition.

39 hat adhere to the more common N-end rule for substrate recognition.

40 ation of amines with an auxiliary domain for substrate recognition.

41 suggest a mechanism that couples H+ flux to substrate recognition.

42 uggest that SmgGDS-607 has multiple modes of substrate recognition.

43 tant role in energizing secretion events and substrate recognition.

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

45 nd leader peptide demonstrates the basis for substrate recognition across the entire class of such tr

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

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

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

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

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

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

52 n and propose structure-based mechanisms for substrate recognition and allosteric activation by low p

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

54 These enzymes can exhibit distinct modes of substrate recognition and are often fused to carbohydrat

55 Substrate recognition and binding are critical for the r

56 hat paradoxically couples its own folding to 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 The insights into substrate recognition and catalysis provided here form a

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

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

63 : controlling an adjoined enzymatic domain's substrate recognition and catalysis.

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

65 bility in the PRORP1 enzyme conformation for substrate recognition and catalysis.

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

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

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

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

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

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 sis for uncompetitive lithium inhibition and substrate recognition and define a sequence motif for me

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 ical features of m(7)G1405 methyltransferase-substrate recognition and distinguish at least two disti

80 fy a molecular mechanism that regulates ADAR substrate recognition and editing efficiency.

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

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

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

84 7 linker as a novel mechanism to control 30S substrate recognition and enzymatic turnover.

85 Substrate recognition and excision usually take place in

86 us pneumoniae IgA1 protease facilitates IgA1 substrate recognition and how this can be inhibited.

87 ounding the catalytic pocket of DspB in PNAG substrate recognition and hydrolysis using a combination

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

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

90 on of labor between two subunits in terms of substrate recognition and methylation.

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

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

93 radixin, and moesin) domain, responsible for substrate recognition and plasma membrane association, a

94 ty, use similar structural elements for rRNA substrate recognition and positioning is not known.

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

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

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

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

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

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

101 Our findings reveal insights into substrate recognition and specificity by SOCS2, and prov

102 e, and the proposed structural basis for the substrate recognition and specificity in CYP2J2 varies w

103 structural and mechanistic insights into the substrate recognition and specificity of PPEP-1 from the

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

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

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

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

108 d FAD in different states yield insight into substrate recognition and the FAD recycling mechanism of

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

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

111 role for this loop in a common mechanism for substrate recognition and translocation by SLC6 transpor

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

113 se studies identified residues important for substrate recognition and transport activity in AtABCC2,

114 structure provides mechanistic insight into substrate recognition and transport by MlaFEDB.

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

116 basis for a more integrated understanding of substrate recognition and transport mechanism in the SLC

117 te on caspase-6 that is critical for protein substrate recognition and turnover and therefore highly

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

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

120 gase San1 often involves Ssa1/Ssa2, but San1 substrate recognition and ubiquitination can proceed wit

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

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

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

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

125 igomerization, conformational changes to aid substrate recognition, and the metal cofactor at the act

126 sights to the factors determining stability, substrate recognition, and the structural mechanism of h

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

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

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

130 shows that the residues, which contribute to substrate recognition, are entirely conserved, further s

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

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

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

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

135 The differences in substrate recognition between these closely related PLpr

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

137 For signaling enzymes, substrate recognition, binding, and product release are

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

139 pression; whereas, mutant OGG1 with impaired substrate recognition/binding was not.

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

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

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

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

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

145 esults provide insight into the mechanism of substrate recognition by DspB and suggest a method to im

146 nd consensus sequences required for accurate substrate recognition by endoribonuclease toxins, defini

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

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

149 The mechanism of substrate recognition by GH138, however, remains unclear

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

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

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

153 Here, we report the structural basis for substrate recognition by MAGE ubiquitin ligases.

154 Mutation of the SBC disrupted substrate recognition by MAGEs and blocked MAGE-A11 onco

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

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

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

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

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

160 a built-in mechanism that enables selective substrate recognition by SHP2.

161 We propose a general mechanism for substrate recognition by structure-specific enzymes driv

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

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

164 t a structure-guided functional study of 30S substrate recognition by the aminoglycoside resistance-a

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

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

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

168 Here we show that substrate recognition by TtsA depends on a discrete doma

169 ex and the ATPase in the regulation of early substrates recognition by the T3SS.

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

171 ge by arterivirus nsp4 and describes a novel substrate recognition characteristic of EAV nsp4.

172 site features a high degree of precision in substrate recognition combined with the flexibility requ

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

174 l that EftM employs molecular strategies for substrate recognition common among both class I (Rossman

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

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

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

178 ecent work has shown that FBOX E3 ligases, a substrate recognition component of the ubiquitin proteas

179 lizing F-box only protein 44 (FBXO44) as the substrate recognition component.

180 at domain-containing 7alpha (FBW7alpha), the substrate-recognition component of the SCF(FBW7) multipr

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

199 n energy, can help characterize a protease's substrate recognition, giving insights for the potential

200 dies provide insights into the mechanisms of substrate recognition, glutamylation, and glutamate elim

201 omal degradation, yet the molecular basis of substrate recognition has remained elusive.

202 potential exploitation of unique aspects of substrate recognition in future therapeutic strategies.

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

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

205 s indicate a novel and complex mechanism for substrate recognition involving spatially remote motifs,

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

207 of the Drosophila CTLH complex suggests that substrate recognition is different than orthologous comp

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

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

210 Substrate recognition is one of the hallmarks of enzyme

211 ey regulate the Hsp70 cycle and how specific substrate recognition is performed remains unknown.

212 1 substrates are known, and its mechanism of substrate recognition is poorly understood.

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

214 eins, but the molecular mechanism of nascent substrate recognition is unknown.

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

216 vations of electrostatic interactions in PKA substrate recognition mechanism and nucleus localization

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 FN induction, EAV nsp4 adopts a more complex substrate recognition mechanism to target NEMO.

221 ds by MhsT prompted the investigation of the substrate recognition mechanism.

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

223 A and DNMT3B, we here report a multi-layered substrate-recognition mechanism underpinning their diver

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

225 The structures reveal the substrate recognition model and confirm an inverting man

226 dence that pyridine synthases use a two-site substrate recognition model to engage and process their

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

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

229 to key questions regarding these enzymes and substrate recognition more generally.

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

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

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

233 Substrate recognition of BchC was investigated using six

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

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

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

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

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

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

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

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

242 31, but little is known about the structure, substrate recognition, or catalysis by family members.

243 ing prenyltransferase and its unique mode of substrate recognition, our findings call for a revision

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

245 done in the absence of ATP to delineate the substrate recognition pattern of PriA before its ATP-cat

246 first time how a mostly hydrophobic L-shaped substrate recognition pocket selects for the (S)-cis con

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

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

249 chlamydial SBP, OppA3 (Ct) , possessed dual substrate recognition properties and is capable of trans

250 We exploited intrinsic substrate-recognition properties of elastase to specific

251 d are fundamental to processes as diverse as substrate recognition, protein folding and enzyme cataly

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

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

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

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

256 ties such as the prevention of aggregates or substrate recognition seems to be conserved between bact

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

258 oth approaches can provide information about substrate recognition signals, degrons, and conditional

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

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

261 TatB improves the formation of a proficient substrate recognition site of TatC.

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

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

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

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

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

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

268 ssor of cytokine signaling 2 (SOCS2) acts as substrate recognition subunit of a Cullin5 E3 ubiquitin

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

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

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

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

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

274 FBXW7, a classic tumor suppressor, is a substrate recognition subunit of the Skp1-cullin-F-box (

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

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

280 ubiquitin ligase complexes that included as substrate recognition subunits the F-box proteins Fbxl1

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

282 uitination and ultimately degradation of the substrate recognition subunits.

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

284 l biology to identify a determinant for PLK1 substrate recognition that is essential for proper chrom

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 motif, a hallmark of most AMT/Mep/Rh, alter substrate recognition, transport capacities, N isotope s

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

290 Taken together, SUMO regulates ICP0 substrate recognition via multiple fine-tuned mechanisms

291 iotechnology, and for which the mechanism of substrate recognition was largely unknown.

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

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

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

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

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

297 re, the structures provide new insights into substrate recognition, which involves conformational cha

298 1, the subunit most frequently implicated in substrate recognition, which widens a central cavity of

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

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