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1 le E loop, Asp-147 and Glu-149, modulate the substrate preference.
2 ave high similarities in their structure and substrate preference.
3 d not alter its intrinsic 5'-CC dinucleotide substrate preference.
4 te structures that underlie the variation in substrate preference.
5 tive site entrance also apparently influence substrate preference.
6  underlie subtle or drastic changes in pgFAR substrate preference.
7 riple mutants, suggesting their diversity in substrate preference.
8 e importance of this hydrophobic feature for substrate preference.
9 of ATP production, it can also modify energy substrate preference.
10 group of deubiquitin proteases with distinct substrate preference.
11 te lyase, suggests potential determinants of substrate preference.
12 cap domain contributes residues that enforce substrate preference.
13  differed widely with regard to activity and substrate preference.
14 dium thermocellum (CthTTM) with the opposite substrate preference.
15 cteria were characterized to determine their substrate preference.
16 eir respective orientation can contribute to substrate preference.
17 chimera was functional and displayed a novel substrate preference.
18 the functional significance of this shift in substrate preference.
19  and GlcCer transport by Dnf2, thus altering substrate preference.
20  showed that each contributed to the altered substrate preference.
21  the C-terminal lipase domain in lipoprotein substrate preference.
22 it is not sufficient to encode the change in substrate preference.
23 enesis did not affect either localization or substrate preference.
24  disease, there is a lack of consensus about substrate preference.
25  key amino acids potentially contributing to substrate preference.
26 understanding of its catalytic mechanisms or substrate preferences.
27 ts of AUM and chronophin that explains their substrate preferences.
28 hanism; however, the enzymes differ in their substrate preferences.
29 nsible for alterations in neuronal metabolic substrate preferences.
30 mes and provide valuable insights into their substrate preferences.
31 mong these enzymes based on their respective substrate preferences.
32 of GrB, demonstrating previously unknown GrB substrate preferences.
33 ies differ in their oligosaccharide acceptor-substrate preferences.
34 enzymes with regard to cleavage patterns and substrate preferences.
35 ese enzymes have both overlapping and unique substrate preferences.
36  CYP1As are orthologous enzymes with similar substrate preferences.
37 li peptidoglycan amidases may have different substrate preferences.
38 ew instances of COMT-like enzymes with novel substrate preferences.
39  MMPs previously screened, MMP-20 had unique substrate preferences.
40 ions resulted in distinct alterations in PC2 substrate preferences.
41  temperature profiles and differing relative substrate preferences.
42 istent with these biochemical activities and substrate preferences.
43 e a structural understanding of the observed substrate preferences.
44 -binding activities, whereas maintaining its substrate preferences.
45 uclease catalytic rates, directionality, and substrate preferences.
46 of OCBS and CBS, and explain their different substrate preferences.
47 oxylation activity into P450s with different substrate preferences.
48 rters surprisingly exhibit differential tRNA substrate preferences.
49  and CELA3B isoforms did not evolve distinct substrate preferences.
50 ansferase is surprisingly promiscuous in its substrate preferences.
51 hich is critical to understanding their true substrate preferences.
52  residue in the two enzymes can change their substrate preferences.
53 region of GCC and MCC explain their distinct substrate preferences.
54 protein homo- and heterodimers with distinct substrate preferences.
55                                 To elucidate substrate preferences, a panel of deletion mutations and
56                        Although ADAMs showed substrate preference (ADAM17, TGFalpha and heparin-bindi
57 mmalian orthologues revealed conservation of substrate preferences against a panel of peptide and gly
58 rovide knowledge about critical residues and substrate preference among CCRs and provide, to our know
59 ations help define the structural origins of substrate preference among Eis homologues and suggest th
60                                       sLac's substrate preference among monoaryls was also consistent
61         We further propose that the distinct substrate preferences among Cas2 proteins may be determi
62 mendments at both depths, but with different substrate preferences among lineages.
63 h identified critical residues and explained substrate preferences among PAL isozymes in sorghum and
64 rate recognition motifs determines enzymatic substrate preference and catalysis.
65                               They varied in substrate preference and catalytic activity.
66 egionella, Pseudomonas, and fungi with broad substrate preference and function in virulence.
67  and oxaloacetate, Ab-ArAT4 possesses strong substrate preference and highest activity with the aroma
68 n a molecular puzzle of mechanisms governing substrate preference and mode of action that has not yet
69 tion and divergence, gene loss, evolution of substrate preference and promiscuity.
70 and near-perfect correlation between the MMP substrate preference and sequence identity of 50-57 disc
71                   A comparison of whole-body substrate preference and skeletal muscle substrate oxida
72  with different EED isoforms exhibit similar substrate preference and specificity.
73 eatures of the human enzyme that explain its substrate preference and the mechanistic basis for catal
74 y of paralogous enzymes exhibiting divergent substrate preferences and catalytic mechanisms.
75 s of these RNA demethylases beyond different substrate preferences and cellular localization, where m
76 , and Cw24) were compared for their relative substrate preferences and cleavage kinetics using eIF4G
77 , each having however clear specificities of substrate preferences and kinetic properties.
78      Recombinant proteins displayed distinct substrate preferences and product specificities that can
79 olgi; however, the structural basis of these substrate preferences and the mechanism through which ca
80                         Based on analysis of substrate preferences and xanthophyll ester formation in
81 igh level expression, biochemical mechanism, substrate preference, and regulation.
82 t into the enzymatic properties of MarP, its substrate preference, and the importance of its transmem
83 oordinate GDP, features that define acceptor substrate preferences, and a likely mechanism for enzyme
84 m1p possess similar domains and show similar substrate preferences, and both localize to the nuclear
85 owth rates, gene expression profiles, carbon substrate preferences, and cell-cell signaling profiles.
86 structural domains to RNA product length and substrate preference are incompletely understood, due in
87 ulated transporter networks with overlapping substrate preferences are involved in sensing and signal
88  share 30% sequence identity; however, their substrate preferences are varied.
89                  OsHPLs also differ in their substrate preference as determined by in vitro enzyme as
90 membrane domains of GlcNAc6ST-2 had the same substrate preference as native GlcNAc6ST-1.
91 o liver studies, but no direct comparison of substrate preference at physiological fasting concentrat
92 proline + 4" residue within TM4 to determine substrate preference at the exit gate.
93                                The divergent substrate preference between DNMT3A and DNMT3B provides
94 ltransferases and identified a difference in substrate preference between METTL15 and its bacterial o
95 idue (Gly-553) in this pocket can change the substrate preference between short- and medium-chain acy
96  Regulatory Factor 1 (Smurf1) can switch its substrate preference between two proteins of opposing ac
97                    We confirmed the reversed substrate preference by determining the Michaelis-Menten
98             Furthermore, our results suggest substrate preference by NgTET1 to (5m)CpG and TpG dinucl
99 4,5,6-tetrakisphosphate enantiomers and that substrate preference can be manipulated by Arg(130) muta
100 gatus CYP51B, including determination of its substrate preferences, catalytic parameters, inhibition,
101 During heart failure (HF), cardiac metabolic substrate preference changes from fatty acid (FA) toward
102  heart and brown adipose tissue (BAT), where substrate preference changes in pathophysiologic states.
103 sident MyrAkt1 exhibited a markedly distinct substrate preference compared with MyrAkt1 immunoprecipi
104 tained from such in silico models, including substrate preference, consequences of gene deletions, op
105 horylation of the E3 ligase could switch its substrate preference, contributing to selective protein
106 ost of the analyzed enzymes displayed narrow substrate preferences corresponding to their predicted p
107  than ceramide based on in vitro assays with substrate preference deoxycholic acid > chenodeoxycholic
108 , A, B, and C, distinguished by their unique substrate preferences despite the fact that the structur
109 sed in E. coli, purified, and their in vitro substrate preferences determined.
110 -dependent endonuclease activity and display substrate preferences different from MspJI.
111                                          The substrate preferences displayed by these enzymes toward
112 latforms, gut fungal enzymes are unbiased in substrate preference due to a wealth of xylan-degrading
113  thought that the pathogenic mutations alter substrate preference (e.g. ATP versus ADP) thereby domin
114                We found that tissue-specific substrate preference exists in PS synthesis.
115 ically recognizes CpG dinucleotide and shows substrate preference for 5mC in a CpG context.
116 raight-chain fatty acids (SCFAs), FabH has a substrate preference for acetyl-CoA.
117 -glucosidase, a member of GH31 family, shows substrate preference for alpha(1-6) over alpha(1-4) glyc
118                The first, which demonstrated substrate preference for Ang I, was neutral endopeptidas
119   Ang-(1-7)-forming enzymes that demonstrate substrate preference for Ang II are likely to play an im
120 function is often associated with a shift in substrate preference for ATP production.
121       Mitochondrial proteases demonstrated a substrate preference for basic protein variants, which i
122                                          EET substrate preference for both COX-1 and COX-2 were estim
123 that this P450 is a omega-hydroxylase with a substrate preference for both saturated and unsaturated
124 acyl-specific phospholipid transacylase with substrate preference for cardiolipin and phosphatidylcho
125 hosphoethanolamine transferase in vitro with substrate preference for cellulosic materials.
126                   While CEK1 and CEK2 showed substrate preference for Cho over Etn, CEK3 and CEK4 had
127               MMP-13 is a collagenase with a substrate preference for collagen II over collagens I an
128                          The enzyme shows no substrate preference for dehydroepiandrosterone versus p
129    Here, we show that Orn exhibits exquisite substrate preference for diribonucleotides.
130                          However, UvrD had a substrate preference for fork structures having a nascen
131 ther, our results indicate that the acquired substrate preference for GAB1 is critical for the ERBB2
132 sion of a mutant form of Hs2st with a strong substrate preference for GlcA-containing units, suggesti
133 logs with respect to gelatinolytic activity, substrate preference for hydrophobic amino acids on both
134  or PGPH) activity and identified an overall substrate preference for hydrophobic residues at the P1
135  2-O-sulfotransferase (Hs2st) shows a strong substrate preference for IdoA over GlcA, C5-epimerizatio
136                                  A change in substrate preference for K147Q SS pyruvate lyase activit
137 a3 (At1g51440), a plastid lipase with a high substrate preference for MGDG, and is sustained by furth
138 ducts, providing a rationale for its unusual substrate preference for NaMN over NaAD.
139 terial sialidases with previously unobserved substrate preference for Neu5Gc-containing glycans.
140 encodes an acyl-ACP synthetase (AasC) with a substrate preference for palmitic compared with oleic ac
141 ipids into murine fibroblasts, with a strong substrate preference for phosphatidylserine.
142 ayed diphosphate phosphatase activity with a substrate preference for PSDP > FDP > phosphatidic acid.
143 phosphatase/phosphotransferase with distinct substrate preference for PSDP.
144 2 active site, resulting in a change in SHP2 substrate preference for Sprouty1, a known negative regu
145  Delta(10)(trans) double bond and displays a substrate preference for the trans-Delta(12), rather tha
146 range of cellular proteins, has a remarkable substrate preference for translation-related proteins (e
147                                It displays a substrate preference for two molecules of indole-3-pyruv
148 n shown that Dnmt3a and Dnmt3b have distinct substrate preferences for certain genomic loci, includin
149 s suggest that the frequent inversion of the substrate preferences for nonadiabatic photoheterolysis
150 e enzyme-peptide complex explains the marked substrate preferences for particular P4, P2 and P1 resid
151                      Here we investigate the substrate preferences for Pif1p.
152 mbers of this enzyme family show distinctive substrate preferences for short-, medium- or long-chain
153 s to explore the chemical space that defines substrate preferences for the auxin uptake carrier AUX1.
154 s an in vitro enzyme assay detected possible substrate preferences for the endopeptidase penicillin b
155                            Surprisingly, the substrate preferences for the human and mouse enzyme are
156 glycoside kinases, rationalize the different substrate preferences for these enzymes.
157  the perinatal period redirect mitochondrial substrate preference from carbohydrates to fatty acids.
158 ough highly conserved, EndoV homologs change substrate preference from DNA in bacteria to RNA in euka
159 hough in acute ischemia there is a switch in substrate preference from fatty acids to glucose, metabo
160 e dehydrogenase (ALDH) family with different substrate preferences from reported ALDH families, named
161                          Shift of myocardial substrate preference has been observed in many chronic d
162                        In support of its DNA substrate preference, helicase sequestration studies rev
163                                    The CYP51 substrate preferences imply differences in the post-squa
164  among transferases, thus further modulating substrate preference in an isoform-specific manner.
165 ns, suggesting that the Zn(2) site modulates substrate preference in mbetal L1.
166                               In this study, substrate preference in PS synthesis was determined to g
167 les in insulin-stimulated glucose uptake and substrate preference in skeletal muscle and adipose cell
168 t modulates fatty acid metabolism, regulates substrate preference in the heart.
169 19W/G301F-SbCAD4 double mutant displayed its substrate preference in the order coniferaldehyde > p-co
170 ollowed by 18:0,22:5-PC, resulting in the PC substrate preference in the order of 18:0,22:6 > 18:0,22
171           AWAT1 and AWAT2 have very distinct substrate preferences in terms of alcohol chain length a
172 combinant mTORC1 and mTORC2 exhibit distinct substrate preferences in vitro, consistent with their ro
173 itro, the enzymes have distinct glycoprotein substrate preferences in vivo.
174 w strong hydrolytic activity with a broad P1 substrate preference including basic and hydrophobic gro
175  also repair other lesions and have distinct substrate preferences, indicating that they have potenti
176 ntions have been tested clinically to target substrate preference, insulin sensitivity, and mitochond
177  and full-length proteins suggest that HDAC8 substrate preference is based on a combination of short-
178                     In B-cell lymphomas, its substrate preference is frequently altered through somat
179  exact nature of the mutations, the enzyme's substrate preference is modified.
180                          Interestingly, this substrate preference is preserved when using a released
181 rized to date, the molecular basis for their substrate preferences is unknown.
182 ynC, which was characterized with respect to substrate preference, kinetic properties, and product fo
183 mportance of the stem region with respect to substrate preference, localization, and oligomerization.
184                      Despite their different substrate preferences, many NRTKs are structurally simil
185 volutionarily related proteases with similar substrate preferences may have distinct biological roles
186 onal groups (BFGs) each distinguished by its substrate preferences, metabolic pathways and its prefer
187                            To compare kinase substrate preferences more generally, we employed a prot
188 e contains a sequence derived from known Syk substrate preference motifs linked to a cell permeable p
189 ss-talk, by which effector binding regulates substrate preference, occurs largely through R293 and Q2
190 sphopeptide chips, to determine the in vitro substrate preference of 16 members of the protein-tyrosi
191  million nucleotides that contributes to the substrate preference of a coenzyme A ligase.
192 tyrosine as free amino acid and altering the substrate preference of a prenyltransferase by mutagenes
193   Biochemical analysis demonstrates that the substrate preference of AtGH3.5 is wider than originally
194 ied Ydr109c and FGGY proteins showed a clear substrate preference of both kinases for d-ribulose over
195 te residues that appear to contribute to the substrate preference of CCMTs relative to other members
196 3 and 4 (TM3-4) of Drs2 into Dnf1 alters the substrate preference of Dnf1 from PC to PS.
197 d to the trans-Golgi network and adopted the substrate preference of GlcNAc6ST-1.
198 ion (L487A/P488A) is required to convert the substrate preference of hGS from beta-Ala to Gly.
199 reveal the molecular changes that define the substrate preference of hGS, explain the product diversi
200 s sufficient to enact a global change in the substrate preference of one MMP to that of another, indi
201 adenylation assay, we characterized the acyl substrate preference of PBS3.
202 tein coupling preferences, and the Galpha(o) substrate preference of RGS6, shape A(1)R- and M(2)R-GIR
203         Kinetic analyses suggested an AKR1A1 substrate preference of SNO-CoA > GSNO.
204 tion of kinetoplastid cells suggest that the substrate preference of TBCYP51 may reflect a novel ster
205       Biochemical analyses indicate that the substrate preference of TET2 results from the different
206             Our studies demonstrate that the substrate preference of TET2 results from the intrinsic
207                    The specific activity and substrate preference of the bacterially expressed enzyme
208                Besides shedding new light on substrate preference of the chromatin remodeler RSC, the
209 m region of GlcNAc6ST-1 affects the cellular substrate preference of the enzyme without altering its
210 on has minor effects on the structure or the substrate preference of the enzyme.
211 ure are important factors in determining the substrate preference of the EZH2 histone methyltransfera
212 ed, such as the newly uncovered bifunctional substrate preference of the key regulatory enzyme in toc
213 mino acids by mutagenesis, characterized the substrate preference of the mutants, and determined the
214                       Intrigued by the novel substrate preference of the Sicarius enzyme, we solved i
215                     To better understand the substrate preference of these toxins, we used (31)P NMR
216                               The intriguing substrate preference of this enzyme for nicked Holliday
217                           In this study, the substrate preference of this enzyme was investigated by
218                                              Substrate preferences of 14 kinases mainly from the FGGY
219 cleotides can be used to rapidly examine the substrate preferences of a given glycosylase.
220 -linking approach to probe the structure and substrate preferences of AlkB and its three human homolo
221                          We investigated the substrate preferences of bacterial aryloxyalkanoate diox
222  eIF4G, acts as a modulator for activity and substrate preferences of Ded1p, which is the RNA remodel
223   We show that the exosome exploits distinct substrate preferences of DIS3 and RRP6, its two catalyti
224 c domain distinctively influence the peptide substrate preferences of each splice variant.
225                                 The acceptor substrate preferences of FUT8 are well-characterized and
226 et of unnatural amino acids to fully map the substrate preferences of GrB, demonstrating previously u
227                 The quaternary structure and substrate preferences of MERS-CoV PLpro were determined
228 sense mutation in an ancestral ape, compared substrate preferences of mouse and human marapsins with
229             Recently, crystal structures and substrate preferences of NS2B-NS3pro from Dengue and Wes
230 s elucidate a novel mechanism for modulating substrate preferences of O-glycosyltransferases via alte
231 af and seed tissues, protein properties, and substrate preferences of plant cyclopropane synthase wer
232 nosoma cruzi, and L. infantum) suggests that substrate preferences of plant- and fungal-like protozoa
233  side of the site of hydrolysis, we profiled substrate preferences of recombinant human chymase using
234 t biological soil crusts (biocrusts) and the substrate preferences of seven biocrust isolates.
235 s from Trypanosomatidae, dramatically alters substrate preferences of TCCYP51, converting it into a m
236 al analyses provide unique insights into the substrate preferences of the distinct active sites and h
237 he reasons for the CELA3 duplication and the substrate preferences of the duplicated isoforms are unc
238     Here we report a characterization of the substrate preferences of the enzyme complex using a reco
239 s this gap in PKS engineering knowledge, the substrate preferences of the final two modules of the pi
240       Here we biochemically characterize the substrate preferences of the helix-hairpin-helix (HhH) d
241 ne ribosides and cytokinins that reflect the substrate preferences of the knocked out enzymes.
242  tri-methylation (H3K27me3) owing to altered substrate preferences of the mutant enzymes.
243 ed under various conditions to determine the substrate preferences of the OppA proteins.
244 peptide-aminomethylcoumarins to contrast the substrate preferences of the recombinant Mtb proteasome
245  the cap domain, implying differences in the substrate preferences of the two enzymes.
246  convert Ado to Ade, an understanding of the substrate preferences of these enzymes could lead to the
247                          We investigated the substrate preferences of these PPIases in vitro using ty
248 A wrap, and also suggest that the particular substrate preferences of topoisomerase IV might be dicta
249 cognition of a primary cognate sequence, the substrate preferences of two DUBs, UCH-L3 and isopeptida
250 d residue composition) lead to the different substrate preferences of VvAHGD from other ALDHs.
251 d GC adhesion, initial axonal outgrowth, and substrate preference on alternating matrix stripes and m
252                 From a protein structure and substrate preference perspective, cruzain, an essential
253 F) / feeder-free conditions and evaluated XF substrate preference, pluripotency, and karyotype.
254 ion (FAO) prevents the pathological shift of substrate preference, preserves cardiac function and ene
255 e larval swimming, or to the CNS to regulate substrate preference prior to the induction of larval se
256 l known TUTases, nucleotide specificity, RNA substrate preference, processivity, quaternary structure
257                                          The substrate preference profile of the St-IVD2 protein was
258 ors into account, our data reveal that pgFAR substrate preference provides a good explanation of how
259                   To a certain extent, their substrate preference redundancies correlate with structu
260  that originally displayed the much narrower substrate preferences required for glycogen catabolism.
261 stinguished, because they differ in acyl-CoA substrate preference, sensitivity to inhibition by dihyd
262 differences that give rise to the individual substrate preferences shown by these highly related isoe
263 otransferase exhibited specific activity and substrate preferences similar to the wild type bovine Gl
264 ects enzyme structure and dynamics, and thus substrate preference, simultaneously and sequentially.
265                                              Substrate preference studies show that nocturnin is an e
266 ian control of metabolism drives a switch in substrate preference such that the late-evening Snack Se
267 ution patterns, intracellular locations, and substrate preferences, suggesting that each isoform has
268                                         This substrate preference switch is mediated by the membrane
269    The two enzymes have differences in their substrate preferences that explain the variations observ
270  rapid in vitro assay, thereby demonstrating substrate preferences that overlapped but were clearly d
271    The two enzymes have differences in their substrates preferences that explain variations observed
272 nervous systems may alter the cardiac energy substrate preference, thereby contributing to the progre
273           There is a switch of gluconeogenic substrate preference to glycerol that quantitatively acc
274 calling for other mechanisms that coordinate substrate preference to maintain a functional TCA cycle.
275 tio of OASS:CAS activity but did not convert substrate preference to that of a CAS.
276 ' the base of each effector and communicates substrate preference to the active site by forming diffe
277                OsDGAT1-1 showed nearly equal substrate preferences to C16:0-CoA and 18:1-CoA whereas
278  variants displayed 18- to 19-fold shifts in substrate preference toward 5FC, a significant reduction
279      Importantly, vertebrate EBAX also shows substrate preference toward aberrant Robo3 implicated in
280                                   A shift of substrate preference toward glucose in the heart is cons
281 of the metabolic network to favor a shift of substrate preference toward glucose.
282               Cryptosporidium ACSs displayed substrate preference toward long-chain fatty acids.
283  albicans, and MT isoforms, reveals profound substrate preference toward obtusifoliol (turnover 5.6 m
284  showed that recombinant BAR and PAT exhibit substrate preference toward phosphinothricin over the 20
285 d by thin layer chromatography analysis with substrate preference toward unsaturated fatty acids.
286                 The enzyme exhibits a strong substrate preference toward xylooligosaccharides; hence
287 s, however, PfSET7 displays specific protein substrate preference towards nucleosomes with pre-existi
288 nal (C terminal) domain did not change lipid substrate preference (triglyceride vs. phospholipase) as
289 gest a role for adropin in regulating muscle substrate preference under various nutritional states.
290 ctivity, we analyzed Prp enzyme kinetics and substrate preference using a fluorogenic peptide cleavag
291                   To better understand these substrate preferences, we present crystal structures of
292        Residues that determine IAA versus BA substrate preference were identified.
293 erization of four new enzymes revealed their substrate preference, whereas their catalytic residues w
294 differences in expression profiles and 2-oxo substrate preferences, which account for the diversity o
295 that even closely related enzymes have clear substrate preferences with AKR7A2, AKR7A4, and AKR7A5 sh
296 igm for natural molecular rulers and imparts substrate preferences with ramifications for biological
297 ative and recombinant PjapPDE showed a clear substrate preference, with an estimated half-life in viv
298  Abs indicated divergent activity levels and substrate preferences, with the common requirement of a
299  and activation energies indicated different substrate preferences within secreted MMPs, because MMP-
300 x, providing a mechanism to evolve different substrate preferences within the family without large st

 
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