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1 e SERA5 gene, or replace Ser596 with a bulky Arg residue.
2 except near a conserved, positively charged Arg residue.
3 terminus, causing release of the C-terminal Arg residue.
4 eaks indicates that they arise from a single Arg residue.
5 nts from cleavage at the C terminus of the L-Arg residue.
6 nd with the side chain of the C-terminal Lys/Arg residue.
7 short amino acids motifs enriched in Lys and Arg residues.
8 est by a high degree of alignment of Lys and Arg residues.
9 omains, which together in bull P1 contain 19 Arg residues.
10 intermediates that contain C-terminal Lys or Arg residues.
11 al aromatic residues with positively charged Arg residues.
12 mide substrates with N-terminal Leu, Met and Arg residues.
13 yzed substrates with N-terminal Leu, Met and Arg residues.
14 which resides in a stretch of Lys, His, and Arg residues.
15 enzyme is specific for COOH-terminal Lys or Arg residues.
16 r access pathway for the transport of the S4 Arg residues.
17 llination of proteins via the deimination of Arg residues.
18 xyl terminus, to include an area rich in Ser-Arg residues.
19 lation and asymmetric dimethylation at three Arg residues.
20 riants were detected, with 6 (19%) involving Arg residues.
21 ightly held charge of a protonated arginine (Arg) residue.
22 channel blocked by the hydrocarbon chains of Arg+ residues.
23 IgG reduced this binding significantly, the Arg residues (162-163) of the C1q-A chain, which are tho
24 ve scanned the sequence -Gln-Ala-His-Ser-Asn-Arg- (residues 30-35 of [DPhe12,Nle21,38]Ac-hCRF4-41) wi
26 were separately replaced with Ala, Ser, and Arg residues; all six mutants displayed no detectable ca
28 ned the relative impact of mutation of these Arg residues alone and in combination on the above react
29 -triphosphatase identified the motif Cys and Arg residues and an upstream Asp as required for activit
30 ariety of new fluorogenic peptides with a P3 Arg residue, and we demonstrated their superiority compa
38 ractions individually with two transmembrane Arg residues (Arg-183(5.39) and Arg-258(7.35)) to create
39 SK1/PKARIalpha association requires all four Arg residues (Arg-93-96) in the pseudosubstrate site of
40 VIII) occurs through proteolysis at three P1 Arg residues: Arg(372) and Arg(740) in the FVIII heavy c
41 tatic/H-bonding interactions involving three Arg residues (Arg48, Arg51, and Arg53) projecting from t
43 endent on the presence of the highly charged Arg residue at 3056, and viruses with this phenotype and
48 between the beta4 and beta5 strands, and an Arg residue at the beginning of the catalytic domain.
49 showed that mutation of a positively charged Arg residue at the beta-dimer interface and high NaCl co
50 sidue donated by the rasGAP protein, and the Arg residue at the core of the GTP or GDP sensing switch
51 th a Bowman-Birk inhibitor reported here, an Arg residue at the P1 position of the inhibitor is bound
53 OmpT cleave peptides with three consecutive Arg residues at different sites, a difference in specifi
56 sidues to Ala, we demonstrated that only the Arg residues at positions 331 and 332 were required for
59 e results indicate that the highly conserved Arg residues at positions 365 and 375 may play a role in
60 On the basis of exon sequences, there are no Arg residues at the predicted C-terminus of the mature g
62 utation of an absolutely conserved arginine (Arg) residue at position 50 to alanine (R50A) of the sim
63 Single mutations of the Asp (or Glu) and Arg residues blocked kinase function both in yeast cells
64 antigen possessed a P7-Leu instead of the P7-Arg residue, but nevertheless was accommodated within th
67 s of the hD4R are substituted with arginine (Arg) residues, cellular hD4R protein levels increase.
69 contrast, mutation of lysines 66-68 to basic Arg residues did not decrease (and in some cases enhance
70 close to the PtdIns(3)P-binding pocket or an Arg residue directly involved in PtdIns(3)P binding abro
71 This catalytic cation is analogous to the Arg residue donated by the rasGAP protein, and the Arg r
72 m-phosphate complexation, where the cationic Arg residues drag the anionic phosphate groups along as
73 lix alpha2 in recognizing a constellation of Arg residues embedded in a hydrophobic patch on the surf
76 utagenesis was used to investigate the seven Arg residues for activity (74, 75, 160, 162, 266, 306 an
82 1 was extended at the C-terminus by a single Arg residue giving rise to analog 90 (BMS-200261) which
83 D4 to catalyze the deimination of methylated Arg residues has also been evaluated, and the results in
92 f ISD with MALDI FTICR, the influence of the Arg residue in ISD fragmentation is less straightforward
94 me high binding affinity, confirmed that the Arg residue in position 7, which is known to be crucial
98 n has a short cytoplasmic tail and a charged Arg residue in the transmembrane region that, by analogy
100 talyze the post-translational methylation of Arg residues in a variety of different proteins involved
101 tic enzymes that catalyze the methylation of Arg residues in a variety of proteins (e.g., histones H3
102 s, Drp1-x01 required oligomeric assembly and Arg residues in alternative exon 3 for microtubule targe
104 position, a strong nonpreference for Lys and Arg residues in any position, and the first evidence tha
105 mutagenesis was applied to the corresponding Arg residues in both the small and large subunits of mai
107 These results indicate a role for V(H)CDR3 Arg residues in chromatin specificity of lupus-derived a
108 Because of the reported role of V(H)CDR3 Arg residues in dsDNA binding and the near identity of t
111 second finger-like structure and a number of Arg residues in L1 that form a positively charged, shelf
113 role of high alpha-defensin Arg content, all Arg residues in mouse Paneth cell alpha-defensin cryptdi
114 mblies and cellular dispositions, homologous Arg residues in neuroligin-3 (Arg-451), in butyrylcholin
116 ionic interactions between Asp-19 (P(6)) and Arg residues in plasmin (Arg-644, Arg-719, and Arg-767),
117 P. gingivalis among bacteria, which converts Arg residues in polypeptide chains into citrulline.
118 Taken together, our results demonstrate that Arg residues in S1-S4 voltage-sensing domains reside in
119 d the important functional roles of internal Arg residues in situations where a charge is needed in t
123 y neurotransmitter receptors often relies on Arg residues in the binding site, leading to the assumpt
124 series of melanotropin analogues with His or Arg residues in the core pharmacophores of MTII, SHU9119
125 resent study, we show that altering specific Arg residues in the H chain of a human pathogenic beta2G
126 The single substitution of any of the four Arg residues in the helical segments did not affect impo
127 e within the phosphate-binding loop, and two Arg residues in the LID domain are proposed as substitut
128 eas substitutions for the individual Lys and Arg residues in the N-terminal region were tolerated.
130 cking Arg-NLS-Gln ING4 mutant, which has all Arg residues in the NLS mutated to Gln, loses its affini
131 channels are controlled by several conserved Arg residues in the S4 helix of the voltage-sensing doma
132 these results demonstrate that the conserved Arg residues in the SRH of both D1 and D2 play critical
135 structure mapping identified several Lys and Arg residues in this region that form salt bridges with
137 C:G base pairs H-bond with conserved His or Arg residues in ZnF8, ZnF9, and ZnF11, and the consensus
138 first time the replacement of all arginine (Arg) residues in a protein with canavanine (Can), a toxi
142 eta 2GPI was achieved by the introduction of Arg residues into the 3H9 H chain variable region at pos
143 analyses of Sdh1 implicate C-terminal region Arg residues involvement in covalent flavinylation and S
145 the invariant Lys residue as well as the two Arg residues, its phosphate-binding loop is examined and
147 demonstrate that citrullination of selected Arg residues leads to progressive disruption of HSP90 te
148 ement, in the Pro3 analogue, with additional Arg residues led to analogues with improved kappa affini
150 in-tyrosine kinases contain a catalytic loop Arg residue located either two or four positions downstr
151 ively spliced AT-hook indicated that Lys and Arg residues made essential DNA contacts, whereas Gly an
153 586A/R588A/R591A (all three of the indicated Arg residues mutated to Ala), had wild-type activity and
156 eport that alterations in the 0-layer Gln or Arg residues of Vam7p or Nyv1p, respectively, strongly i
158 We have demonstrated that a highly conserved Arg residue on loop 1 of RHBDL2 plays a critical role in
159 open conformation, two of the four conserved Arg residues on S4 are on a lipid-facing surface and two
163 and demonstrated that its positively charged Arg residues, particularly Arg6 and Arg7, were crucial f
165 In this pathway for peptide translocation, Arg residues play a fundamental role not only in the bin
166 than for binding, while Arg-65 and two other Arg residues play a greater role in binding than in resi
167 d concentration-dependent manner, suggesting Arg residues play an important role in the catalytic act
170 Within these domains, a strictly conserved Arg residue present in both activating cofactors, but no
171 In this arrangement, the highly conserved Arg residue present in either cofactor comes into close
172 d a key epitope corresponding to an internal Arg residue (R502 [HSP90beta]/R510 [HSP90alpha]) that is
174 with a neutral (Met, Gln, or Ala) or basic (Arg) residue results in an approximately 10(4)- or 250-f
176 d included those having the alpha-subunit 96(Arg) residue substituted by Gln, Leu, or Ala, the alpha-
177 N9PP orthologs share a stringently conserved Arg residue that forms a salt bridge with the substrate
178 a much longer surface loop, and the critical Arg residue that is required for ascorbate binding in AP
179 on of Trp-222 in the loading AT domain to an Arg residue that is universally conserved in all extende
180 hydrophobic pocket near a cluster of Asp and Arg residues that are essential for catalysis, with the
181 HORMA structure reveals a pair of conserved Arg residues that constitute a putative phosphate sensor
183 ced affinity for hydrolysis after Lys versus Arg residues; therefore, the ability to autolytically ac
184 els, suggesting that movements of protonated Arg residues through the membrane will be prohibited.
190 sical basis behind the remarkable ability of Arg residues to remain protonated in environments otherw
191 experiments, surface accessibility maps for Arg residues were compared for the free fPollambda versu
193 (HNP1) and several HNP1 analogs where three Arg residues were replaced by each of the following six
195 nhibitor is principally determined by the P1 Arg residue, whereas exosites outside the loop which are
196 re active than KSHV-GPCR, suggesting that an Arg residue, which is constrained outside the bundle by
197 ss-II myosins begins with a highly conserved Arg residue (whose mutation in human beta-cardiac myosin
198 The interaction of these positively charged Arg residues with the lipid membrane has been of intense
199 jacent C residues of the CCA sequence and an Arg residue within a highly conserved sequence motif in
203 which contained Arg-->Ala mutations at four Arg residues within the effector binding region (EF) or
206 minimal 9-mer peptide, R6A-1, do not contain Arg residues yet retain high affinity (K(D) = 60 and 200
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