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1 utilizing protein expressed with an alkynyl unnatural amino acid.
2 voltage-clamp fluorometry with a fluorescent unnatural amino acid.
3 labeled enzyme are largely unaffected by the unnatural amino acid.
4 age C-H oxidation to one containing a linear unnatural amino acid.
5 ent structure (7) was replaced by natural or unnatural amino acids.
6 or efficiently designing peptides containing unnatural amino acids.
7 post-translational modifications (PTMs) and unnatural amino acids.
8 rature procedures for the syntheses of these unnatural amino acids.
9 ll molecules bearing natural or bioisosteric unnatural amino acids.
10 rocyclic peptides that contain a majority of unnatural amino acids.
11 he engineering of translation to incorporate unnatural amino acids.
12 r facilitate the expression of proteins with unnatural amino acids.
13 which are the most frequently used to encode unnatural amino acids.
14 e beta-barrel as well as the introduction of unnatural amino acids.
15 y in live cells by genetically incorporating unnatural amino acids.
16 eins, and expand the genetic code to include unnatural amino acids.
17 brary (HyCoSuL), which uses both natural and unnatural amino acids.
18 n through the site-directed incorporation of unnatural amino acids.
19 photostabilizer and biomolecular target via unnatural amino acids.
20 ish eight tripeptides, each having different unnatural amino acids.
21 nalogues in which Phe(13) was substituted by unnatural amino acids.
23 es of mutants site-specific labeled with the unnatural amino acid, [(13)C]p-methoxyphenylalanine, in
24 ne WALP24 peptide labeled with the semirigid unnatural amino acid 4-(3,3,5,5-tetra-methyl-2,6-dioxo-4
25 Two stabilized derivatives incorporating unnatural amino acids ((68)Ga-SH01078 and (68)Ga-P03034)
26 polymerase variant containing a fluorescent unnatural amino acid, (7-hydroxy-4-coumarin-yl) ethylgly
27 ease the utility of protein mutagenesis with unnatural amino acids, a recombinant expression system i
29 noacyl-tRNA synthetase pair specific for the unnatural amino acid added to the media and the protein
30 with the ease of synthesis of the necessary unnatural amino acids allows for facile synthesis of tri
31 er-peptide elements with genetically encoded unnatural amino acids (amino acids that have been artifi
33 ethodology to incorporate a photoactivatable unnatural amino acid and photochemically cleave the back
34 vancing existing protocols, we introduced an unnatural amino acid and subsequently mineral-interactin
37 fted toward site-specific modification using unnatural amino acids and engineered site-selective amin
38 n reaction was applied to the preparation of unnatural amino acids and geometrically controlled tri-
39 plants or synthetic chemistry can introduce unnatural amino acids and non-peptidic constraints that
41 e optimized this system for use with several unnatural amino acids and provide a demonstration of its
43 plied to the diastereoselective synthesis of unnatural amino acids and the late-stage derivatization
44 allows for straightforward incorporation of unnatural amino acids and the preparation of peptides ma
45 on the in vivo incorporation of fluorescent unnatural amino acids and their analysis by steady-state
47 thyl-14- O-methylmorphinans with natural and unnatural amino acids and three dipeptides at position 6
48 ing novel self-associating peptides based on unnatural amino acids, and inhibitor peptides of detrime
49 the amino acid sequence, the introduction of unnatural amino acids, and labeling with stable isotopes
50 oto-cross-linking studies with site-specific unnatural amino acids, and species-specific activity of
53 specifically incorporating multiple distinct unnatural amino acids are hampered by their low efficien
54 bility and unique conformational properties, unnatural amino acids are highly valued by pharmaceutica
58 CR1 (1-350) containing Mn(2+) chelated to an unnatural amino acid assists in the characterization of
59 efficiency incorporation of a single type of unnatural amino acid at a time, because every triplet co
60 created a neopeptide via introduction of an unnatural amino acid at the K(12) position, which could
61 eases the yield of protein, incorporating an unnatural amino acid at three sites, from unmeasurably l
62 F1, we increase the yield of protein bearing unnatural amino acids at a single site 17- to 20-fold.
63 A set of variants containing natural and unnatural amino acids at position 15, which were designe
64 , we used reconstituted 26S proteasomes with unnatural amino-acid-attached fluorophores in a series o
65 l metabolic placement of a uniquely reactive unnatural amino acid, azidohomoalanine (Aha), followed b
68 ry is applied to the gram-scale syntheses of unnatural amino acids, bioactive molecules, and chiral b
69 roperties allow them to incorporate multiple unnatural amino acids (but not natural amino acids), wou
71 r demonstrate that IQF substrates containing unnatural amino acids can be used to investigate proteas
72 his study demonstrates that incorporation of unnatural amino acids can provide a flexible, straightfo
73 128, with a range of alternative natural and unnatural amino acids, changed the EC50 (from approximat
74 it will be possible to encode more than 200 unnatural amino acid combinations using this approach.
75 improved second-generation synthesis of the unnatural amino acid components of the anticancer peptai
76 s enabled a significant increase in yield of unnatural amino acid containing proteins from tens of mi
77 i-Miyaura coupling of genetically positioned unnatural amino acids containing aryl halide side chains
81 2 substrate library, which also included the unnatural amino acid cyclohexylalanine (Cha) derivative
84 n of 3-, 4-, 5-, and 6-membered heterocyclic unnatural amino acid derivatives by exploiting facile Ma
85 sters, which may be regarded as novel hybrid unnatural amino acids, during the peptide synthesis itse
86 g selective modification of both natural and unnatural amino acids--each with merits and limitations-
88 estrict the incorporation of the fluorescent unnatural amino acid epsilonNH2-Bodipy576/589-lysine (BO
91 nt immunosensor designed by incorporating an unnatural amino acid fluorophore into the binding site o
92 h residues were substituted with natural and unnatural amino acids, focusing on the role of aromatici
93 strong polarity and high hydrophobicity, the unnatural amino acid forms specific and strong interacti
94 sical properties of three of the fluorescent unnatural amino acids from two classes were also studied
95 ledge, successful detection of a fluorescent unnatural amino acid (fUAA), Lys(BODIPYFL), incorporated
96 elanogaster) and the incorporation of useful unnatural amino acids has been aided by the development
98 ty filter region of the NaK channel with the unnatural amino acids homoserine and cysteine sulfonic a
100 ssible to genetically encode a wide array of unnatural amino acids in both prokaryotic and eukaryotic
101 highlight the utility of genetically encoded unnatural amino acids in exploring the effects of posttr
103 ally-encoded, site-specific incorporation of unnatural amino acids in regions essential for activatio
104 in P. pastoris and used to incorporate eight unnatural amino acids in response to an amber codon with
105 e to efficiently direct the incorporation of unnatural amino acids in response to quadruplet codons.
106 have been evolved to incorporate a range of unnatural amino acids in response to the amber codon in
107 o pEVOL and compared their ability to insert unnatural amino acids in response to three independent a
108 o-Q1 we direct the incorporation of distinct unnatural amino acids in response to two of the new blan
113 arnessing proximity-enabled reactivity of an unnatural amino acid incorporated in the bait toward a t
115 ent advances are enhancing the efficiency of unnatural amino acid incorporation by creating and evolv
116 nstrate that tRNA levels can be limiting for unnatural amino acid incorporation efficiency, and we de
117 ns and highlight the exceptional capacity of unnatural amino acid incorporation for increasing our un
118 don suppression and related technologies for unnatural amino acid incorporation has greatly expanded
119 n O-ribosome previously evolved for enhanced unnatural amino acid incorporation in response to amber
121 codons, to provide a substantial increase in unnatural amino acid incorporation in response to the UA
124 ress in this area: (i) the low efficiency of unnatural amino acid incorporation that limits labeling
125 of the nonsense suppression methodology for unnatural amino acid incorporation to probe drug-recepto
126 enesis and the high precision methodology of unnatural amino acid incorporation to study the gating i
127 nstituted in vitro translation, quantitative unnatural amino acid incorporation via AUG codon reassig
128 heterogeneity in GCK using a combination of unnatural amino acid incorporation, time-resolved fluore
133 ite-specific incorporation of an immunogenic unnatural amino acid into a protein of interest produces
134 ite-specific incorporation of an immunogenic unnatural amino acid into an autologous protein offers a
138 d by the introduction of an azide-containing unnatural amino acid into the coat protein for the first
139 er RNAs to encode numerous pairs of distinct unnatural amino acids into a single protein expressed in
140 n vivo incorporation of isotopically labeled unnatural amino acids into large proteins drastically re
141 However, the efficient incorporation of unnatural amino acids into proteins and the specific, fl
142 h mutually orthogonal methods of introducing unnatural amino acids into proteins as well as with chem
143 new vector, pEVOL, for the incorporation of unnatural amino acids into proteins in Escherichia coli
144 nse, rare, or 4-bp codons to incorporate >50 unnatural amino acids into proteins in Escherichia coli,
145 The efficient, site-specific introduction of unnatural amino acids into proteins in mammalian cells i
146 that enables the efficient incorporation of unnatural amino acids into proteins in mammalian cells.
147 erein we review work on the incorporation of unnatural amino acids into proteins in response to quadr
148 that specifically prevents incorporation of unnatural amino acids into proteins may provide a new st
149 n for the incorporation of multiple distinct unnatural amino acids into proteins or the synthesis and
152 sion, for the site-specific incorporation of unnatural amino acids into proteins, is currently limite
154 een used to enable the incorporation of many unnatural amino acids into recombinant proteins in vivo.
155 bles efficient, homogeneous incorporation of unnatural amino acids into target proteins in diverse ma
156 e basis for ion selectivity by incorporating unnatural amino acids into the channel, engineering chan
158 e ethynyl group of pENPhe suggests that this unnatural amino acid is a more conservative substitution
159 Escherichia coli MS methods verify that the unnatural amino acid is only incorporated at one positio
161 urements, because efficient incorporation of unnatural amino acids is limited to transient expression
162 ural changes, since the incorporation of the unnatural amino acids is not inherently limited by the s
163 anted to report the utility of an unexplored unnatural amino acid, isothiocyanyl alanine ((NCS)Ala =
164 ed have been evolved to incorporate numerous unnatural amino acids, it will be possible to encode mor
165 or labeling through genetic incorporation of unnatural amino acids, lanthanide resonance energy trans
167 ension of approaches to incorporate multiple unnatural amino acids may allow the combinatorial biosyn
169 Specifically, we create the pY protein by unnatural amino acid misincorporation, mutagenize a univ
175 nto AMPA receptors using genetically encoded unnatural amino acid mutagenesis in a mammalian cell lin
176 hotocaging of a synthetic gene network using unnatural amino acid mutagenesis in mammalian cells was
178 recision structural modifications enabled by unnatural amino acid mutagenesis on mammalian receptors
182 here we use double mutant cycle analysis and unnatural amino acid mutagenesis to probe the functional
183 oteins expressed in Escherichia coli through unnatural amino acid mutagenesis using a Cnf-specific tR
184 tives into the receptor binding pocket using unnatural amino acid mutagenesis, and evaluating the res
187 ereoselective route to a masked form of this unnatural amino acid now enabled the synthesis of two of
188 to this problem, we genetically encoded the unnatural amino acids o-nitrobenzyl-2-fluorotyrosine, -3
190 For these studies, we have incorporated the unnatural amino acid p-acetyl-L-phenylalanine for specif
195 n suppression to introduce the photoreactive unnatural amino acid p-benzoyl-l-phenylalanine (BzF) at
201 We have developed a method to incorporate an unnatural amino acid, p-acetylphenylalanine (pAcPhe) int
202 ated to a mutant alphaCD3 Fab containing the unnatural amino acid, p-acetylphenylalanine, at a define
204 C identical withN stretching vibration of an unnatural amino acid, p-cyano-phenylalanine, to directly
205 movement by incorporating tryptophan and the unnatural amino acid, p-cyanophenylalanine into Glt(Ph)
211 h nanomaterials by targeted incorporation of unnatural amino acids possessing dual affinity to differ
212 es rely mainly on traditional coupling using unnatural amino acids, postsynthetic modification of pep
214 The methodology establishes novel routes to unnatural amino acids, proline homologues, and cyclic vi
215 not be feasible to separate the full-length unnatural amino acid protein from the truncated form.
217 mination of a chiral center derived from the unnatural amino acid R-alpha-methylcysteine makes the mo
219 e first experimental evidence documenting an unnatural amino acid replacement in a GPCR expressed in
220 tural amino acids will extend the use of the unnatural amino acid replacement methodology to amino ac
221 o acids are transformed to twenty-one chiral unnatural amino acids representing seven distinct functi
222 e site specifically inserted a (13)C-labeled unnatural amino acid residue, (13)C-p-methoxyphenylalani
224 This approach provides hybrid natural and unnatural amino acid sequences, and thus we termed it th
225 llows selection to yield proteins containing unnatural amino acids should such sequences functionally
226 This Perspective highlights the diversity of unnatural amino acid structures found in hit-to-lead and
228 sized a library of 61 individual natural and unnatural amino acids substrates, chosen to cover a broa
229 achieved using peptide libraries containing unnatural amino acids such as the hybrid combinatorial s
230 ombination of self-labeling protein tags and unnatural amino acid technology permits the semisynthesi
237 otein an appropriately "tuned" electrophilic unnatural amino acid that reacts with a native nucleophi
238 eted cellular proteins with versions bearing unnatural amino acids that allow imaging or synthetic re
239 bacteria, limiting the types and numbers of unnatural amino acids that can be utilized at any one ti
240 lational, site-specific incorporation of two unnatural amino acids that can function as fluorescence
243 Ita), for the synthesis of another class of unnatural amino acids, thioureayl alanines ((TU)Ala = Tu
245 addition, SIDEpro can accommodate any PTM or unnatural amino acid, thus providing a flexible predicti
246 that binds to the hot spot, and selected an unnatural amino acid to incorporate, based on the struct
247 f covalent bond into proteins by enabling an unnatural amino acid to react with a proximal cysteine.
248 redoxins, and demonstrate the power of using unnatural amino acids to address critical chemical biolo
249 of His-66 may improve the ability of certain unnatural amino acids to be incorporated by the ribosome
250 tantially enhanced this by incorporating 102 unnatural amino acids to explore the S1-S4 pockets of hu
252 This method entails the incorporation of unnatural amino acids to site-specifically label protein
253 ta suggest not only robust methods for using unnatural amino acids to study large proteins by NMR but
257 aviolet irradiation of a photo-crosslinkable unnatural amino acid (UAA) cotranslationally incorporate
258 monstrate the application of a photoreactive unnatural amino acid (UAA) crosslinking system to captur
261 echnology to site-specifically introduce the unnatural amino acid (UAA) p-azido-l-phenylalanine (azF)
262 (AMPA)-type iGluRs using genetically encoded unnatural amino acid (UAA) photocross-linkers, p-benzoyl
264 ally introduced into proteins by enabling an unnatural amino acid (Uaa) to selectively react with a p
266 essential HIV-1 protein biosynthesis through unnatural amino acid (UAA*)-mediated suppression of geno
269 nsporter protein to encode photocrosslinking unnatural amino acids (UAAs) into 75 different positions
271 The ability to site-specifically incorporate unnatural amino acids (UAAs) into proteins is a powerful
272 rm is reported that enables incorporation of unnatural amino acids (UAAs) into specific sites on the
273 click chemistry and the genetic encoding of unnatural amino acids (UAAs) to overcome this limitation
274 has led to the addition of approximately 70 unnatural amino acids (UAAs) to the genetic codes of Esc
277 onal aaRS to distinguish between a favorable unnatural amino acid (unAA) substrate from unfavorable n
278 hydrate-binding proteins that use a reactive unnatural amino acid "warhead" and demonstrates that a "
279 ogonal tRNA-synthetase pair, the fluorescent unnatural amino acid was incorporated in the Shaker volt
281 s-linking experiments with photo-activatable unnatural amino acids, we show that full-length BACE1, i
282 Saccharomyces cerevisiae to be specific for unnatural amino acids were inserted between eukaryotic t
284 the catalytic cycle can be maintained using unnatural amino acids, which may prove useful in enzyme
285 f high yields of complex proteins containing unnatural amino acids whose expression is not practical
286 application of a peptide delivery system for unnatural amino acids will extend the use of the unnatur
287 arget protein contains a genetically encoded unnatural amino acid with bioorthogonal reactivity and t
288 ara-pentafluorosulfanyl phenylalanine, is an unnatural amino acid with extreme physicochemical proper
289 antibodies containing a genetically encoded unnatural amino acid with orthogonal chemical reactivity
291 mized system, we produce proteins containing unnatural amino acids with comparable yields to a protei
292 e access to two conformationally constrained unnatural amino acids with different dispositions of the
293 y relationship for binding using a series of unnatural amino acids with different lengths of hydropho
294 eral strategy for labelling pairs of encoded unnatural amino acids with different probes via rapid an
295 labeling of proteins at genetically encoded unnatural amino acids with distinct small molecules at p
296 Using this new methodology, we incorporated unnatural amino acids with extended side chains into the
297 site-specific incorporation of a variety of unnatural amino acids with novel chemical and biological
298 e demonstrate the use of genetically encoded unnatural amino acids with orthogonal chemical reactivit
299 s were constructed using genetically encoded unnatural amino acids with orthogonal chemical reactivit