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1 voltage-clamp fluorometry with a fluorescent unnatural amino acid.
2 firmed a high translational fidelity for the unnatural amino acid.
3 age C-H oxidation to one containing a linear unnatural amino acid.
4 utilizing protein expressed with an alkynyl unnatural amino acid.
5 or efficiently designing peptides containing unnatural amino acids.
6 post-translational modifications (PTMs) and unnatural amino acids.
7 rature procedures for the syntheses of these unnatural amino acids.
8 ll molecules bearing natural or bioisosteric unnatural amino acids.
9 rocyclic peptides that contain a majority of unnatural amino acids.
10 brary (HyCoSuL), which uses both natural and 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 the production of mutant proteins containing unnatural amino acids.
17 n through the site-directed incorporation of unnatural amino acids.
18 photostabilizer and biomolecular target via unnatural amino acids.
19 ish eight tripeptides, each having different unnatural amino acids.
20 nalogues in which Phe(13) was substituted by unnatural amino acids.
21 ent structure (7) was replaced by natural or 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 ease the utility of protein mutagenesis with unnatural amino acids, a recombinant expression system i
28 noacyl-tRNA synthetase pair specific for the unnatural amino acid added to the media and the protein
29 with the ease of synthesis of the necessary unnatural amino acids allows for facile synthesis of tri
30 er-peptide elements with genetically encoded unnatural amino acids (amino acids that have been artifi
32 used biosynthetic methods to incorporate the unnatural amino acid analogue 2-fluorohistidine (2-FHis)
33 ethodology to incorporate a photoactivatable unnatural amino acid and photochemically cleave the back
36 fted toward site-specific modification using unnatural amino acids and engineered site-selective amin
37 n reaction was applied to the preparation of unnatural amino acids and geometrically controlled tri-
39 e optimized this system for use with several unnatural amino acids and provide a demonstration of its
41 on the in vivo incorporation of fluorescent unnatural amino acids and their analysis by steady-state
43 ing novel self-associating peptides based on unnatural amino acids, and inhibitor peptides of detrime
44 the amino acid sequence, the introduction of unnatural amino acids, and labeling with stable isotopes
47 specifically incorporating multiple distinct unnatural amino acids are hampered by their low efficien
48 bility and unique conformational properties, unnatural amino acids are highly valued by pharmaceutica
50 CR1 (1-350) containing Mn(2+) chelated to an unnatural amino acid assists in the characterization of
51 efficiency incorporation of a single type of unnatural amino acid at a time, because every triplet co
52 created a neopeptide via introduction of an unnatural amino acid at the K(12) position, which could
53 eases the yield of protein, incorporating an unnatural amino acid at three sites, from unmeasurably l
54 F1, we increase the yield of protein bearing unnatural amino acids at a single site 17- to 20-fold.
56 A set of variants containing natural and unnatural amino acids at position 15, which were designe
57 ial expression of mutant proteins containing unnatural amino acids at specific sites designated by am
58 l metabolic placement of a uniquely reactive unnatural amino acid, azidohomoalanine (Aha), followed b
61 ry is applied to the gram-scale syntheses of unnatural amino acids, bioactive molecules, and chiral b
62 roperties allow them to incorporate multiple unnatural amino acids (but not natural amino acids), wou
63 late an amber suppressor tRNA with a desired unnatural amino acid, but no natural amino acids, in euk
66 r demonstrate that IQF substrates containing unnatural amino acids can be used to investigate proteas
67 his study demonstrates that incorporation of unnatural amino acids can provide a flexible, straightfo
68 128, with a range of alternative natural and unnatural amino acids, changed the EC50 (from approximat
69 it will be possible to encode more than 200 unnatural amino acid combinations using this approach.
70 improved second-generation synthesis of the unnatural amino acid components of the anticancer peptai
71 s enabled a significant increase in yield of unnatural amino acid containing proteins from tens of mi
72 i-Miyaura coupling of genetically positioned unnatural amino acids containing aryl halide side chains
75 2 substrate library, which also included the unnatural amino acid cyclohexylalanine (Cha) derivative
78 sters, which may be regarded as novel hybrid unnatural amino acids, during the peptide synthesis itse
79 g selective modification of both natural and unnatural amino acids--each with merits and limitations-
81 estrict the incorporation of the fluorescent unnatural amino acid epsilonNH2-Bodipy576/589-lysine (BO
84 h residues were substituted with natural and unnatural amino acids, focusing on the role of aromatici
85 ilitate new molecular studies using tailored unnatural amino acids for cell biology and neurobiology.
86 sical properties of three of the fluorescent unnatural amino acids from two classes were also studied
87 ledge, successful detection of a fluorescent unnatural amino acid (fUAA), Lys(BODIPYFL), incorporated
88 te-specifically incorporate a diverse set of unnatural amino acids (>30) into proteins and quickly ad
89 elanogaster) and the incorporation of useful unnatural amino acids has been aided by the development
91 ty filter region of the NaK channel with the unnatural amino acids homoserine and cysteine sulfonic a
93 ssible to genetically encode a wide array of unnatural amino acids in both prokaryotic and eukaryotic
94 w one to genetically encode a large array of unnatural amino acids in both prokaryotic and eukaryotic
95 ade possible the genetic encoding of diverse unnatural amino acids in different mammalian cells and p
96 highlight the utility of genetically encoded unnatural amino acids in exploring the effects of posttr
100 ally-encoded, site-specific incorporation of unnatural amino acids in regions essential for activatio
101 in P. pastoris and used to incorporate eight unnatural amino acids in response to an amber codon with
102 e to efficiently direct the incorporation of unnatural amino acids in response to quadruplet codons.
103 have been evolved to incorporate a range of unnatural amino acids in response to the amber codon in
104 o pEVOL and compared their ability to insert unnatural amino acids in response to three independent a
105 o-Q1 we direct the incorporation of distinct unnatural amino acids in response to two of the new blan
108 including the site-specific incorporation of unnatural amino acids in vivo and the directed evolution
111 arnessing proximity-enabled reactivity of an unnatural amino acid incorporated in the bait toward a t
113 ent advances are enhancing the efficiency of unnatural amino acid incorporation by creating and evolv
114 nstrate that tRNA levels can be limiting for unnatural amino acid incorporation efficiency, and we de
115 ns and highlight the exceptional capacity of unnatural amino acid incorporation for increasing our un
116 we increase the efficiency of site-specific unnatural amino acid incorporation from approximately 20
117 don suppression and related technologies for unnatural amino acid incorporation has greatly expanded
118 n O-ribosome previously evolved for enhanced unnatural amino acid incorporation in response to amber
120 codons, to provide a substantial increase in unnatural amino acid incorporation in response to the UA
123 ress in this area: (i) the low efficiency of unnatural amino acid incorporation that limits labeling
124 of the nonsense suppression methodology for unnatural amino acid incorporation to probe drug-recepto
125 f truncated proteins in experiments that use unnatural amino acid incorporation to probe protein func
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
132 en used to site-specifically incorporate the unnatural amino acid into a protein in mammalian cells i
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 t of their kind to show the incorporation of unnatural amino acids into a voltage-gated sodium channe
142 n vivo incorporation of isotopically labeled unnatural amino acids into large proteins drastically re
143 However, the efficient incorporation of unnatural amino acids into proteins and the specific, fl
144 h mutually orthogonal methods of introducing unnatural amino acids into proteins as well as with chem
145 new vector, pEVOL, for the incorporation of unnatural amino acids into proteins in Escherichia coli
146 nse, rare, or 4-bp codons to incorporate >50 unnatural amino acids into proteins in Escherichia coli,
147 The efficient, site-specific introduction of unnatural amino acids into proteins in mammalian cells i
148 that enables the efficient incorporation of unnatural amino acids into proteins in mammalian cells.
149 erein we review work on the incorporation of unnatural amino acids into proteins in response to quadr
150 to allow the site-specific incorporation of unnatural amino acids into proteins in response to the a
151 that specifically prevents incorporation of unnatural amino acids into proteins may provide a new st
152 n for the incorporation of multiple distinct unnatural amino acids into proteins or the synthesis and
155 sion, for the site-specific incorporation of unnatural amino acids into proteins, is currently limite
157 een used to enable the incorporation of many unnatural amino acids into recombinant proteins in vivo.
158 bles efficient, homogeneous incorporation of unnatural amino acids into target proteins in diverse ma
159 e basis for ion selectivity by incorporating unnatural amino acids into the channel, engineering chan
161 ction may provide a way for incorporation of unnatural amino acids into tRNA, and consequently into p
162 e ethynyl group of pENPhe suggests that this unnatural amino acid is a more conservative substitution
164 urements, because efficient incorporation of unnatural amino acids is limited to transient expression
165 ural changes, since the incorporation of the unnatural amino acids is not inherently limited by the s
166 anted to report the utility of an unexplored unnatural amino acid, isothiocyanyl alanine ((NCS)Ala =
167 ed have been evolved to incorporate numerous unnatural amino acids, it will be possible to encode mor
168 or labeling through genetic incorporation of unnatural amino acids, lanthanide resonance energy trans
170 been made to peptides, including the use of unnatural amino acids, mainchain modifications and other
171 ension of approaches to incorporate multiple unnatural amino acids may allow the combinatorial biosyn
179 nto AMPA receptors using genetically encoded unnatural amino acid mutagenesis in a mammalian cell lin
180 hotocaging of a synthetic gene network using unnatural amino acid mutagenesis in mammalian cells was
182 recision structural modifications enabled by unnatural amino acid mutagenesis on mammalian receptors
186 here we use double mutant cycle analysis and unnatural amino acid mutagenesis to probe the functional
187 The work described here on application of unnatural amino acid mutagenesis to two GPCRs, the chemo
188 oteins expressed in Escherichia coli through unnatural amino acid mutagenesis using a Cnf-specific tR
189 tives into the receptor binding pocket using unnatural amino acid mutagenesis, and evaluating the res
192 ereoselective route to a masked form of this unnatural amino acid now enabled the synthesis of two of
193 to this problem, we genetically encoded the unnatural amino acids o-nitrobenzyl-2-fluorotyrosine, -3
195 cids, the necessity for the incorporation of unnatural amino acids or chemical modification of the pr
197 For these studies, we have incorporated the unnatural amino acid p-acetyl-L-phenylalanine for specif
201 n suppression to introduce the photoreactive unnatural amino acid p-benzoyl-l-phenylalanine (BzF) at
208 We have developed a method to incorporate an unnatural amino acid, p-acetylphenylalanine (pAcPhe) int
209 ated to a mutant alphaCD3 Fab containing the unnatural amino acid, p-acetylphenylalanine, at a define
211 C identical withN stretching vibration of an unnatural amino acid, p-cyano-phenylalanine, to directly
215 h nanomaterials by targeted incorporation of unnatural amino acids possessing dual affinity to differ
216 es rely mainly on traditional coupling using unnatural amino acids, postsynthetic modification of pep
218 The methodology establishes novel routes to unnatural amino acids, proline homologues, and cyclic vi
219 not be feasible to separate the full-length unnatural amino acid protein from the truncated form.
221 mination of a chiral center derived from the unnatural amino acid R-alpha-methylcysteine makes the mo
223 e first experimental evidence documenting an unnatural amino acid replacement in a GPCR expressed in
224 tural amino acids will extend the use of the unnatural amino acid replacement methodology to amino ac
225 o acids are transformed to twenty-one chiral unnatural amino acids representing seven distinct functi
226 e site specifically inserted a (13)C-labeled unnatural amino acid residue, (13)C-p-methoxyphenylalani
228 This approach provides hybrid natural and unnatural amino acid sequences, and thus we termed it th
229 llows selection to yield proteins containing unnatural amino acids should such sequences functionally
230 This Perspective highlights the diversity of unnatural amino acid structures found in hit-to-lead and
232 sized a library of 61 individual natural and unnatural amino acids substrates, chosen to cover a broa
233 achieved using peptide libraries containing unnatural amino acids such as the hybrid combinatorial s
234 ombination of self-labeling protein tags and unnatural amino acid technology permits the semisynthesi
241 otein an appropriately "tuned" electrophilic unnatural amino acid that reacts with a native nucleophi
242 eted cellular proteins with versions bearing unnatural amino acids that allow imaging or synthetic re
243 bacteria, limiting the types and numbers of unnatural amino acids that can be utilized at any one ti
244 lational, site-specific incorporation of two unnatural amino acids that can function as fluorescence
247 Ita), for the synthesis of another class of unnatural amino acids, thioureayl alanines ((TU)Ala = Tu
249 addition, SIDEpro can accommodate any PTM or unnatural amino acid, thus providing a flexible predicti
250 that binds to the hot spot, and selected an unnatural amino acid to incorporate, based on the struct
251 f covalent bond into proteins by enabling an unnatural amino acid to react with a proximal cysteine.
252 redoxins, and demonstrate the power of using unnatural amino acids to address critical chemical biolo
253 of His-66 may improve the ability of certain unnatural amino acids to be incorporated by the ribosome
254 tantially enhanced this by incorporating 102 unnatural amino acids to explore the S1-S4 pockets of hu
255 This method entails the incorporation of unnatural amino acids to site-specifically label protein
256 ta suggest not only robust methods for using unnatural amino acids to study large proteins by NMR but
260 aviolet irradiation of a photo-crosslinkable unnatural amino acid (UAA) cotranslationally incorporate
262 ally introduced into proteins by enabling an unnatural amino acid (Uaa) to selectively react with a p
264 essential HIV-1 protein biosynthesis through unnatural amino acid (UAA*)-mediated suppression of geno
267 nsporter protein to encode photocrosslinking unnatural amino acids (UAAs) into 75 different positions
269 The ability to site-specifically incorporate unnatural amino acids (UAAs) into proteins is a powerful
271 rm is reported that enables incorporation of unnatural amino acids (UAAs) into specific sites on the
272 click chemistry and the genetic encoding of unnatural amino acids (UAAs) to overcome this limitation
273 has led to the addition of approximately 70 unnatural amino acids (UAAs) to the genetic codes of Esc
276 onal aaRS to distinguish between a favorable unnatural amino acid (unAA) substrate from unfavorable n
277 hydrate-binding proteins that use a reactive unnatural amino acid "warhead" and demonstrates that a "
278 ogonal tRNA-synthetase pair, the fluorescent unnatural amino acid was incorporated in the Shaker volt
279 s for genetically directing incorporation of unnatural amino acids, we have inserted trifluoromethyl-
280 s-linking experiments with photo-activatable unnatural amino acids, we show that full-length BACE1, i
281 Saccharomyces cerevisiae to be specific for unnatural amino acids were inserted between eukaryotic t
283 the catalytic cycle can be maintained using unnatural amino acids, which may prove useful in enzyme
284 f high yields of complex proteins containing unnatural amino acids whose expression is not practical
285 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 antibodies containing a genetically encoded unnatural amino acid with orthogonal chemical reactivity
290 mized system, we produce proteins containing unnatural amino acids with comparable yields to a protei
291 e access to two conformationally constrained unnatural amino acids with different dispositions of the
292 eral strategy for labelling pairs of encoded unnatural amino acids with different probes via rapid an
293 labeling of proteins at genetically encoded unnatural amino acids with distinct small molecules at p
294 We developed a general approach that allows unnatural amino acids with diverse physicochemical and b
295 Using this new methodology, we incorporated unnatural amino acids with extended side chains into the
296 site-specific incorporation of a variety of unnatural amino acids with novel chemical and biological
297 e demonstrate the use of genetically encoded unnatural amino acids with orthogonal chemical reactivit
298 s were constructed using genetically encoded unnatural amino acids with orthogonal chemical reactivit
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