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1  to a missense mutation in an evolutionarily conserved amino acid.
2     All three variants change evolutionarily conserved amino acids.
3 family-specific missense mutations at highly conserved amino acids.
4 yme is inactivated by mutation of two highly conserved amino acids.
5                 Both mutations affect highly conserved amino acids.
6 domain of TGBp2, which contains a stretch of conserved amino acids.
7 l roles are assigned to this latter class of conserved amino acids.
8  and nearly monoclonal CDR3 containing novel conserved amino acids.
9 xon 11 that results in deletion of 30 highly conserved amino acids.
10 ed mutations and/or (for coding DNA) encoded conserved amino acids.
11 is targeted to lipid droplets, requiring the conserved amino acid 22-28 sequence and amino acid 71-10
12 inant viruses containing HA with exchange of conserved amino acids adjacent to acylation sites or wit
13 rchanging the first four coding exons or the conserved amino acids adjacent to the RGD of DMP1 with c
14                        Among the six non-Sox conserved amino acids, amino acids 16 and 45 are likely
15 eteen missense mutations occur in absolutely conserved amino acids among the vertebrate homologs.
16 tution, arginine 321 to histidine, at a well-conserved amino acid and behaves genetically as a domina
17       The missense mutation affects a highly conserved amino acid and is predicted to severely impair
18                 These mutations alter highly conserved amino acids and are absent among control chrom
19 OL4A1(R538G)) found only in patients changed conserved amino acids and impaired COL4A1 secretion much
20 inase domain contains several alterations in conserved amino acids and is catalytically inactive.
21                      The mechanism relies on conserved amino acids and may therefore underlie GPCR/G
22         Mapping the specific location of the conserved amino acids and sites of constitutively active
23 The C-terminal subdomain displays a patch of conserved amino acids and we show that this patch define
24 the phenotype in these families, affect well-conserved amino acids, and are predicted to be damaging
25 The replication-defective mutations affected conserved amino acids, and similar phenotypes were obser
26       The four QARS mutations altered highly conserved amino acids, and the aminoacylation activity o
27                 We hypothesized that certain conserved amino acids are critical for ethanol modulatio
28 though mutational analyses demonstrated that conserved amino acids are essential for the function of
29 inding domains (motif III) demonstrated that conserved amino acids are often not essential for functi
30 icient substrate for POMGNT2 when two of the conserved amino acids are replaced.
31 lso, in most of these integrases, all of the conserved amino acids are required for integration.
32                 Both missense changes affect conserved amino acids, are predicted to be damaging by m
33              We demonstrate that each of the conserved amino acids Arg146, Arg221, Tyr230, Gly266, an
34 e-structural relationships; (iv) identifying conserved amino acids as fingerprints of the Dbl and Rho
35              In the crystal structure highly conserved amino acids Asn(335) and Ser(338) of the thumb
36                         The integrity of the conserved amino acids Asn-615 and Asn-619 in helix 7 is
37 n in cardiac troponin T (cTnT) of two highly conserved amino acids (Asn-100 and Glu-101) was found in
38              Here, we mutated three of these conserved amino acids, Asn(82) in the predicted transmem
39 tic model in which O(2) and NO movements and conserved amino acids at the E11, G8, E2, E7, B10, and F
40  of the CENPC-k motif and by mutating single conserved amino acids, but can be restored by insertion
41 nhibitors (TCIs) are designed to bind poorly conserved amino acids by means of reactive groups, the s
42                                 A stretch of conserved amino acids called the GP(Y/F) domain has been
43 he resulting EF-Tu variants contained highly conserved amino acid changes within members of the libra
44 ntified two natural variant toxins with four conserved amino acid changes, including a switch of E to
45  had COI mutations, the latter altering less conserved amino acids (conservation index=71%).
46                       Our results identify a conserved amino acid critical for NST1/SND1 function, an
47                                              Conserved amino acids critical to catalysis in this fami
48 can be partially ascribed to ancient, highly conserved amino acid differences in the N-terminal regio
49 or enhanced DSP-PP(240) cleavage; 2) certain conserved amino acids distant from the cleavage site wer
50  Yip1A was blocked by alteration of a single conserved amino acid (E95K) in its N-terminal cytoplasmi
51 ed a predicted missense mutation in a highly conserved amino acid encoded by thiamine biosynthesis2 (
52 , highlighting the importance of these three conserved amino acids for GA 3-oxidase activity.
53  in the CHRNA5 gene (D398N), which changes a conserved amino acid from aspartic acid to asparagine.
54               At last, proximity between two conserved amino acids from transmembrane helices 3 and 7
55 wer this question, we mutated evolutionarily conserved amino acids, generated eight mutants in the HE
56      The structure shows that three strictly conserved amino acids, Glu198, Tyr109, and Tyr23, are in
57                         We identify a highly conserved amino acid, Gly449, that is necessary for Src
58 mutation in the PUS1 gene affecting a highly conserved amino acid has been associated with mitochondr
59  RHAG that lead to substitutions of 2 highly conserved amino acids (Ile61Arg, Phe65Ser).
60                            Changing a highly conserved amino acid in motif A of any of the four yeast
61 rrga1-d) that is caused by substitution of a conserved amino acid in the C-terminal domain of a DELLA
62 hat the two populations differed by a single conserved amino acid in the CDR3beta motif.
63 ning reveals a missense mutation of a highly conserved amino acid in the low density lipoprotein rece
64      The Thr518Met mutation altered a highly conserved amino acid in the MYRF protein and three of fo
65          The 12848T mutation alters a highly conserved amino acid in the ND5 complex I gene, is not f
66 sidues Arg283, Arg285, and Ile287 are highly conserved amino acids in bovine viral diarrhea virus RNA
67                             To find critical conserved amino acids in dengue viruses, 120 complete ge
68                                          Two conserved amino acids in FeoC were found to be necessary
69                               The respective conserved amino acids in NP may thus be critical for the
70 volves pattern matching to a small number of conserved amino acids in precursor proteins, and thus al
71                                        Three conserved amino acids in region 2.3 of sigma32 were foun
72                                For 21 highly conserved amino acids in RP1, mutation of 15 of these re
73 ed mutations based on sequence alignment and conserved amino acids in selected domains.
74                                   We changed conserved amino acids in SpoIID to alanine to determine
75 cofactor suggested a possible role for three conserved amino acids in substrate binding or catalysis:
76                          Further analysis of conserved amino acids in the amino-terminal conserved do
77                     However, substitution of conserved amino acids in the ATP-binding site did not af
78    Our studies are the first to identify key conserved amino acids in the C terminus of alpha-catenin
79           They further suggest that five non-conserved amino acids in the C-terminal region flanking
80 on protein (PrP) molecules with deletions of conserved amino acids in the central region.
81                         However, mutation of conserved amino acids in the core domain, which may be i
82 common rearrangement in the packing of three conserved amino acids in the core of the muOR, and molec
83  splice-site, and three missense variants at conserved amino acids in the CUL4B gene on Xq24 in 8 of
84                                  In general, conserved amino acids in the GTP-binding pocket were, ho
85                    In contrast, mutations of conserved amino acids in the inner loop of CD82 or of pa
86                                  Mutation of conserved amino acids in the Nbs1 binding domain of Mdm2
87 uggest that pTRS1 inhibits PKR by binding to conserved amino acids in the PKR eIF2alpha binding site
88 ing revealed substitutions of several highly conserved amino acids in the PtD14b protein including a
89 ver, we found that changing three of the six conserved amino acids in the signature, one of which was
90                             Mutation of five conserved amino acids in the Tcf1 HDAC domain diminishes
91                                   Relatively conserved amino acids in the TCR complementarity-determi
92                        We have identified 11 conserved amino acids in the tunnel that are critical fo
93                                  Exchange of conserved amino acids in the vicinity of an acylation si
94 rable or interdependent by substituting many conserved amino acids in this region with alanine to ide
95                           Mutation of highly conserved amino acids in YbeY, allowed the identificatio
96 d a homozygous missense mutation, changing a conserved amino acid, in ATG5 in two siblings with conge
97 ly spliced micro-exon encoding six perfectly conserved amino acids incorporated postnatally into TBC1
98 plants and RNA editing events, which restore conserved amino acids, indicates that matR encodes a fun
99 t points (such as amino acids 4 and 29), and conserved amino acids interacting with other proteins su
100  recognition domains, each displaying 6 of 8 conserved amino acids involved in galactoside-binding ac
101 evealed that WKS1 phosphorylates PsbO at two conserved amino acids involved in physical interactions
102 -specific recognition of the flanking DNA by conserved amino acids is revealed, defining a new role f
103                              In each center, conserved amino acids known to be involved in sulfur and
104 of these 10 amino acids or mutation of three conserved amino acids (L(385), F(389), and T(390)) in th
105 histidyl tRNA synthetase HARS2 at two highly conserved amino acids, L200V and V368L.
106                Mutations of two other highly conserved amino acids (L588A and P589A) reduced but did
107 h ATP, and x-ray structures, show a triad of conserved amino acids lining the nucleotide site that fo
108             Both substitutions affect highly conserved amino acids located in the regulatory GAF-B do
109       It is altered in certain of the highly conserved amino acids making contacts to this antibiotic
110             These features, formed by highly conserved amino acids, match well to the chemical proper
111 patients harbored COI mutations that altered conserved amino acids (mean conservation index=83%), whe
112  from covalently linked side chains of three conserved amino acids (Met-255, Tyr-229, and Trp-107, My
113 ne expression requires box B, a short highly conserved amino acid motif characteristic of BTG2/TOB fa
114           Here we describe an evolutionarily conserved amino acid motif within APLF that is required
115 and a C-terminal region termed REKLES (for a conserved amino acid motif).
116 f these two HhH motifs in conjunction with a conserved amino acid motif, VNINTA.
117                  We have identified a highly conserved amino acid motif, WDXNWD, located within the u
118 f their alpha-helical transmembrane domain a conserved amino acid motif.
119                             We leveraged the conserved amino acid motifs in Cys(2)His(2) zinc fingers
120 tein, and their binding sites are defined by conserved amino acid motifs, forming the structural basi
121             First, even though CLC-ck2 lacks conserved amino acids near the Cl(-)-binding sites that
122 l coupling analysis approach to characterize conserved amino acid networks important for biochemical
123 analyzed it to identify and characterize the conserved amino acid-nucleotide interactions that determ
124 le through public databases, which changes a conserved amino acid of cadherin 2 protein and is suppor
125 quencing to identify a mutation (A280V) in a conserved amino acid of the glycerol-3-phosphate dehydro
126 tivity, an alanine substitution (P365A) in a conserved amino acid of the GP(Y/F) domain did not signi
127               Here we queried the role of 14 conserved amino acids of Escherichia coli LigA by alanin
128                   We identified mutations at conserved amino acids of loops L1 and L3 in the DNA-bind
129  generate 74 viruses possessing mutations at conserved amino acids of NP.
130 o structure-function studies to identify the conserved amino acids of the C2 domain that regulate the
131                                       Highly conserved amino acids of the duplex RNA-binding domain a
132  alleles all contain transversions in highly conserved amino acids of the extracellular domains, sugg
133 vity was not reduced by substitutions in two conserved amino acids of the GP(Y/F) domain, G364A and P
134            Its function was dependent on the conserved amino acids of the hA3A active site, consisten
135 upon protonation of His-121 and Glu-122, two conserved amino acids of the receptor.
136  consistent with the effects of mutations of conserved amino acids on Dio3 activity.
137         Here we show that phosphorylation of conserved amino acids on the membrane-distal surface of
138 A22 c.G328C, results in a change of a highly conserved amino acid (p.G110R) and was not present in co
139                    Carbonyl groups of highly conserved amino acids point toward the lumen to act as s
140 gous variant c.3562C > T located at a highly conserved amino acid position (p.R1188W) in the low dens
141 5 transposases (Tnp's) with mutations at the conserved amino acid position W450, which was structural
142 translocated across membranes facilitated by conserved amino acids positioned on the exoplasmic, cyto
143 ous OPA1 missense mutations affecting highly conserved amino acid positions (p.G488R, p.A495V) in the
144   Using the CRISPR-Cas9 system to target six conserved amino acid positions in Caenorhabditis elegans
145 Finally we have identified conserved and non-conserved amino acid positions within the rim loops that
146 ey share main anchor positions, evidenced by conserved amino acid preferences across the four HLA-E m
147 describing the clearly observable and highly conserved amino acid preferences at individual sites is
148                  Mutations of the contiguous conserved amino acids Pro-148 and Leu-149 in the GHSR1a
149 ropeptide Y type 2 receptors that the highly conserved amino acids, proline and alanine, naturally oc
150                     Furthermore, mutation of conserved amino acids R1097A, W1103A, Y1120A, Y1138A and
151  is composed of one cysteine residue and one conserved amino acid region.
152 rithms to identify oligonucleotide probes in conserved amino acid regions and untranslated sequences.
153              Mutagenesis studies reveal that conserved amino acid regions in the hydrophilic domains
154          These domains were used to identify conserved amino acid regions in the recovered consensus
155 calponin-homology domain of CLAMP to contain conserved amino acids required for actin binding.
156 oss a shallow intersubunit channel formed by conserved amino acids required for RNA-stimulated ATP hy
157 ng mutation, c.567 G > A, affecting a highly conserved amino acid residue (p.Gly189Arg) of the MRM2 p
158 he transcript, including bases that encode a conserved amino acid residue considered critical for ACC
159               Mutagenesis further revealed a conserved amino acid residue implicated in reprotonation
160                     The mutation at the same conserved amino acid residue in IRF-7 drastically reduce
161 R-1 is linked to the replacement of a highly conserved amino acid residue in the activation loop.
162                The mutation affects a highly conserved amino acid residue in the Tubby domain and is
163     The identified mutation affects a highly conserved amino acid residue in the zinc finger domain o
164 so provide structure-function insight into a conserved amino acid residue of transportins in brain de
165                  Substitution of this highly conserved amino acid residue renders PK inactive and thu
166 ation of AMPAR can also be modified by a non-conserved amino acid residue substitution within the spl
167 ward genetic screen in planta, we identify a conserved amino acid residue that determines product spe
168 e disease in the pedigree, affected a highly conserved amino acid residue, and was predicted to be de
169 s, we demonstrated that the phylogenetically conserved amino acid residue, F439, was critical for bot
170  transporter to study the impact of a highly conserved amino acid residue, Thr(101), in transmembrane
171  effector domains and characterized by three conserved amino acid residues (Cys-1865, His-1955, and A
172                                      Several conserved amino acid residues (His228, His11, His333, Cy
173                               An analysis of conserved amino acid residues among members of the SLC4
174 cess, we substituted alanines for each of 19 conserved amino acid residues and assessed the in vivo r
175 responsible for substrate specificity, while conserved amino acid residues and divalent cations are r
176        Both of these mutations affect highly conserved amino acid residues and impair key catalytic f
177 racterize eight BRCA2 VUS that affect highly conserved amino acid residues and map to the N-terminal
178        Both the mutations occurred at highly conserved amino acid residues and were absent in the nor
179                                We found that conserved amino acid residues are located within the hol
180  CD4 suggested a critical role of the highly conserved amino acid residues at positions 423 and 432.
181  introduced a single or a double mutation in conserved amino acid residues contained within this doma
182 n that resembles a Cu-Zn SOD with all of the conserved amino acid residues for binding copper and zin
183                   Maize MIK protein contains conserved amino acid residues found in pfkB carbohydrate
184 ate shuffling to introduce 62 differentially conserved amino acid residues from type I SUTs into OsSU
185                                Lastly, three conserved amino acid residues identified by sequence ali
186  binding interface utilizes many of the same conserved amino acid residues implicated in the binding
187  that these plant-specific proteins lack key conserved amino acid residues important for GTP binding
188 ference in interaction between antimycin and conserved amino acid residues in bovine and bacterial bc
189                      To evaluate the role of conserved amino acid residues in DsbDbeta in the electro
190  the mechanisms of this coupling, we mutated conserved amino acid residues in membrane helices H and
191 ed to act as an affinity ligand for specific conserved amino acid residues in the antibody.
192                                       Highly conserved amino acid residues in the C subunits of the g
193            This was achieved by mutating two conserved amino acid residues in the catalytic domain of
194         All mutations caused substitution of conserved amino acid residues in the kinase domain and i
195 e G(-2)A(-1) cleavage site and several other conserved amino acid residues in the leader peptide were
196                                          The conserved amino acid residues in the loop interacting wi
197                                  The role of conserved amino acid residues in the polymerase domain o
198  kappaM-, and psi-conotoxins revealed highly conserved amino acid residues in the precursor sequences
199                    Importantly, mutations of conserved amino acid residues in the putative DPA(2,6)-b
200       These mutations, heb1 and heb3, change conserved amino acid residues in the regulatory H-NOX do
201 that IrvR is a "LexA-like" protein with four conserved amino acid residues likely required for IrvR a
202                                   Two highly conserved amino acid residues near the C-terminus within
203                  Therefore, mutations in six conserved amino acid residues of H. pylori Fur were cons
204                               To analyze the conserved amino acid residues of HmuR that may be involv
205       Site-directed mutagenesis of 12 highly conserved amino acid residues of the C-terminal domain o
206 s of the cysteine residues of Tvc as well as conserved amino acid residues of the IgV Tvc domain comp
207                       Two additional, highly conserved amino acid residues on an adjacent beta-sheet
208 Furthermore, we identified additional highly conserved amino acid residues or motifs within the DDE/D
209  Based on this structural similarity several conserved amino acid residues present in all velvet doma
210 ition, we have examined the roles of several conserved amino acid residues surrounding the phosphoryl
211 e electrostatic effects of non-conserved and conserved amino acid residues surrounding the rhodopsin
212  proteins containing substitutions of highly conserved amino acid residues that contact the triphosph
213  the DeoR/GlpR family have identified highly conserved amino acid residues that function in DNA-bindi
214             In addition, a cluster of highly conserved amino acid residues was identified which repre
215 ve site of myosin contains a group of highly conserved amino acid residues whose roles in nucleotide
216                               Replacement of conserved amino acid residues with leucine blocked virus
217                                              Conserved amino acid residues within IscS, IscU, and Isc
218 m, we and others recently identified several conserved amino acid residues within L protein domain VI
219 entified distinct mutations affecting highly conserved amino acid residues within NS4B, which mediate
220                                   Two highly conserved amino acid residues, an arginine and a glutami
221  in the public databases, both affect highly conserved amino acid residues, and both are predicted to
222 and c.772C>T (p.Arg258Trp) mutations involve conserved amino acid residues, are located within the co
223 ps (kappa, lambda, and sigma isotypes) using conserved amino acid residues, recombination signal sequ
224 led that both of the mutations affect highly conserved amino acid residues, which are predicted to be
225 itivity of different point mutants of highly conserved amino acid residues.
226 rare, predicted to be damaging, and occur at conserved amino acid residues.
227 GS in 11 unrelated families and alter highly conserved amino acid residues.
228 strate binding by alanine substitution of 36 conserved amino acid residues.
229 ons involved 4 of the 5 exons, all at highly conserved amino acid residues.
230 and were more likely to alter evolutionarily conserved amino acid residues.
231 NA editing to codons encoding evolutionarily conserved amino acid residues.
232                               Mutagenesis of conserved amino acids revealed that S253, H257, D258 and
233                            An evolutionarily conserved amino acid segment within Vps35 is required fo
234                          The gene has highly conserved amino acid sequence and is universally express
235 utilizing Block Maker identified a region of conserved amino acid sequence in a large domain between
236 uires that biochemical functions, defined by conserved amino acid sequence motifs, be embedded into a
237 t the bacterial kingdom and contains several conserved amino acid sequence motifs.
238 ow that Spa40 is cleaved within the strictly conserved amino acid sequence NPTH and substitution of t
239          We also show that the normally well-conserved amino acid sequence of the autoproteolytic cle
240                                We identify a conserved amino acid sequence, KVHPSST, in the C-terminu
241 ment of the substrate protein and contains a conserved amino acid sequence.
242  for de novo gene creation within a strongly conserved amino-acid sequence.
243 HIV-1 Vif proteins, we identified two highly conserved amino acid sequences, (81)LGxGxSIEW(89) and (1
244 rther insights into their genetic diversity, conserved amino acid sequences, and plausible catalytic
245 ly the interspersed segments of variable and conserved amino acid sequences, generate recurring patte
246                                              Conserved amino acid sequences, structure-function data
247 es found in the mature toxins are flanked by conserved amino acid sequences.
248 airs were first designed based on the highly conserved amino-acid sequences of several selected yeast
249                                            A conserved amino acid, Ser-37, is required for activity.
250 as a number of direct hydrogen bonds between conserved amino acid side chains and bases.
251                                              Conserved amino acid side chains in Ire1 that face into
252 rve ciliate-specific modifications of widely conserved amino acid sites in DNA polymerases as one pot
253               PTOX and AOX contain 20 highly conserved amino acids, six of which are Fe-binding ligan
254 4%, respectively), while HPV45 E1 was highly conserved (amino acid substitution rate was 0.77%).
255 n MCLs and ICLs could be attributed to three conserved amino acid substitutions in the active site, s
256 n, tissue culture-adapted (TC) PoSaV has two conserved amino acid substitutions in the RNA-dependent
257             Protein modeling of the 4 highly conserved amino acid substitutions, residing in both hea
258 are distinguishable from eIF4E1a by a set of conserved amino acid substitutions, several of which are
259 e conserved, with mole-rats lacking uniquely conserved amino acid substitutions.
260 s of homologous proteins are relatively well conserved, amino acid substitutions lead to significant
261                        We identified several conserved amino acids surrounding the conserved DB that
262   We identified 66Y (N1 numbering), a highly conserved amino acid that was critical for the stability
263 ne the following: (i) identified a number of conserved amino acids that are crucial for GerBC functio
264 s in all ref4 alleles cause substitutions in conserved amino acids that are located adjacent to predi
265                                 Although the conserved amino acids that are required for mediating D4
266 nd we show that it is controlled by a set of conserved amino acids that couple RNA and ATP binding to
267 e-rich region of each family member contains conserved amino acids that include a PPGY consensus bind
268 TnDOT (IntDOT) carries the C-terminal set of conserved amino acids that is characteristic of the tyro
269                                      Several conserved amino acids that map to cytoplasmic portions o
270                       We identify patches of conserved amino acids that overlap the antibody epitope
271 ic strain Beaudette C (BC), we mutated three conserved amino acids thought to be part of the binding/
272 e function of the SBP2-ribosome interaction, conserved amino acids throughout the SBP2 L7Ae RNA bindi
273 tal structure data and the information about conserved amino acids to perform semiempirical PM3 calcu
274        Site-directed mutagenesis of a highly conserved amino acid tryptophan within this motif recapi
275 ive site of CYP72C1 does not contain several conserved amino acids typically needed for substrate hyd
276                                Stat3 has two conserved amino-acid (Tyr705 and Ser727) residues, which
277 d, surprisingly, that pre-phosphorylation or conserved amino acid variation at the 7-position in the
278 of the chromodomain or point mutation of the conserved amino acids, W64A or W67A, of SUV39H1 impaired
279               The variation affects a highly conserved amino acid, was absent in 800 controls, and wa
280                                      Fifteen conserved amino acids were essential for enzyme activity
281                                      Several conserved amino acids were identified that create a hydr
282 x and as they replaced evolutionarily highly conserved amino acids with a SIFT score < 0.005, they ar
283 ins shares a common geometry and identity of conserved amino acids with the active site of response r
284         This missense change alters a highly conserved amino acid within CEP120 (p.Ala199Pro).
285 lts in the substitution of an evolutionarily conserved amino acid within the beta-propeller domain, w
286     The R658C mutation in PPP1R15B affects a conserved amino acid within the domain important for pro
287                              Mutation in one conserved amino acid within this region reduced the abil
288  site of interaction on FBF-2, we identified conserved amino acids within C. elegans PUF proteins.
289                                              Conserved amino acids within each specific receptor clas
290 within its domain III, which contains highly conserved amino acids within motifs designated A and C.
291 of deleterious mutations that disrupt highly conserved amino acids within protein-coding sequences, w
292 ctroscopic methods, we examined the roles of conserved amino acids within the bilin-binding domain of
293             We introduced point mutations of conserved amino acids within the C loop, a region of the
294 g revealed that the 3 variants affect highly conserved amino acids within the GTPase domain of the pr
295 ct missense mutations affecting three highly conserved amino acids within the HCFC1 kelch domain.
296                           Point mutations to conserved amino acids within the human CHD7 SLIDE domain
297 he MEEVD domain of Hsp90, as well as several conserved amino acids within the tetratricopeptide repea
298 f the putative UL28 metal-binding domain and conserved amino acids within the UL15 nuclease domain ar
299 itro and in planta mutagenesis revealed that conserved amino acids within this domain can be altered
300                                        Three conserved amino acids (Y658, T780, and S808) and two non

 
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