Enlarging the amino acid set of Escherichia coli by infiltration of the valine coding pathway. - Wikidata - awgldk - TriplyDB

Enlarging the amino acid set of Escherichia coli by infiltration of the valine coding pathway.

Enlarging the amino acid set of Escherichia coli by infiltration of the valine coding pathway.

http://www.wikidata.org/entity/Q43582952

about

An unnatural base pair for incorporating amino acid analogs into proteins Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains A single residue in leucyl-tRNA synthetase affecting amino acid specificity and tRNA aminoacylation Evolution of phage with chemically ambiguous proteomes Site-specific functionalization of proteins and their applications to therapeutic antibodies The C-Ala Domain Brings Together Editing and Aminoacylation Functions on One tRNA Sense codon emancipation for proteome-wide incorporation of noncanonical amino acids: rare isoleucine codon AUA as a target for genetic code expansion Translocation within the acceptor helix of a major tRNA identity determinant Discovery and Investigation of Natural Editing Function against Artificial Amino Acids in Protein Translation Stabilization of bzip peptides through incorporation of fluorinated aliphatic residues.A method to predict edge strands in beta-sheets from protein sequences A strategy for in vivo screening of subtilisin E reaction specificity in E. coli periplasm.Stereoselective incorporation of an unsaturated isoleucine analogue into a protein expressed in E. coli.Enzymatic aminoacylation of tRNA with unnatural amino acids.Discovery of aminoacyl-tRNA synthetase activity through cell-surface display of noncanonical amino acids Genetic code mutations: the breaking of a three billion year invariance.Nonorthologous replacement of lysyl-tRNA synthetase prevents addition of lysine analogues to the genetic code.The balance between pre- and post-transfer editing in tRNA synthetases.Blocking site-to-site translocation of a misactivated amino acid by mutation of a class I tRNA synthetase Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation.Direct charging of tRNA(CUA) with pyrrolysine in vitro and in vivo.Selection and characterization of Escherichia coli variants capable of growth on an otherwise toxic tryptophan analogue.An engineered Escherichia coli tyrosyl-tRNA synthetase for site-specific incorporation of an unnatural amino acid into proteins in eukaryotic translation and its application in a wheat germ cell-free system.Resampling and editing of mischarged tRNA prior to translation elongation.Naturally occurring aminoacyl-tRNA synthetases editing-domain mutations that cause mistranslation in Mycoplasma parasites Aminoacyl-tRNA synthetases: versatile players in the changing theater of translation.Binding of misacylated tRNAs to the ribosomal A site.Norvaline and norleucine may have been more abundant protein components during early stages of cell evolution.Mutational unmasking of a tRNA-dependent pathway for preventing genetic code ambiguity Elucidation of tRNA-dependent editing by a class II tRNA synthetase and significance for cell viability The hidden code in genomics: a tool for gene discovery.Interstice mutations that block site-to-site translocation of a misactivated amino acid bound to a class I tRNA synthetase.Artificially ambiguous genetic code confers growth yield advantage.Cysteinyl-tRNA(Cys) formation in Methanocaldococcus jannaschii: the mechanism is still unknown.Cysteinyl-tRNA formation and prolyl-tRNA synthetase.Fidelity escape by the unnatural amino acid β-hydroxynorvaline: an efficient substrate for Escherichia coli threonyl-tRNA synthetase with toxic effects on growth.Protein mistranslation protects bacteria against oxidative stress Ancestral AlaX editing enzymes for control of genetic code fidelity are not tRNA-specific.Homologous trans-editing factors with broad tRNA specificity prevent mistranslation caused by serine/threonine misactivation.Substrate specificity of bacterial prolyl-tRNA synthetase editing domain is controlled by a tunable hydrophobic pocket

P2860

Q22122123-374429B0-6E17-40D9-906D-FF9D0F14911A Q24618513-D80A335B-2439-4489-9A13-10F8271C4BAD Q24643316-EBABF33C-27E7-4749-8F85-5336652C310C Q24804563-DD6FD1E5-9EC8-424A-8DE0-BA70158BAA0E Q26830699-98D3544F-3AFE-47E3-A36B-39FE8C2CA55A Q27656913-3A93AB6D-D1A4-416D-ACDA-714E4B697690 Q28305963-935C7AA0-B9E0-414C-970F-A3A4D3D13B5C Q28348448-A943C6B6-DF53-462A-842C-203A5090A98B Q28818118-9383B689-2D36-4A9D-8B52-CAE6249F7AA0 Q30354827-3CB4AA86-9BCA-4D4F-9380-3F6A6AFFDEB3 Q30360862-A3A4A54B-320C-47DC-841A-18C0F4A5EF1B Q31051773-79003B91-762D-4CF5-AB46-C59A26DDF5FB Q33231070-CACBD7DB-3D4F-4F7E-9A27-C9D58ACDF1A7 Q33236492-730B8369-366F-4096-940F-1DC70EE4E2A2 Q33248009-2833D737-0706-4446-953A-D8EB14C07370 Q33680378-03FFF0AE-AA7F-41F5-ACB3-5BD02831BC30 Q33717093-80F486BE-3168-4BF4-BDFE-5353B8161F0C Q33810666-B285600D-3BD0-44A9-9C82-81B8D0F2E404 Q33894157-8C734112-9D1F-454F-9153-87DA208DA919 Q33896261-43365F66-6594-4C29-A19C-9C39FDF96E1B Q33980884-E8D088FF-AB0A-4EDC-B0BA-EC8E7AA94EF1 Q33996847-39881422-98F1-42FC-9159-35207B826F53 Q34075286-C568577D-CD48-4576-AED2-F8D62A678444 Q34151351-0D3E770E-BB45-4A15-B9F9-7170BF1AE0DE Q34186873-8E1FED67-5626-46B4-A058-5224E47C0994 Q34364813-F90A2E93-03E1-4C35-BC8C-57D5F68AF019 Q34366629-924733A5-7168-4837-988C-55224F00559C Q34369443-004E6C33-19C7-44A5-B44A-4C7CCCD65327 Q34410795-9BE25168-2A8C-42C8-8EAA-9790E4526622 Q34463866-EEB19164-DEB8-43CB-A3D8-1F59C2572A33 Q34464905-50873A9E-8E5E-44AD-BE48-9508D57D7FEA Q34469989-95481147-265A-44D3-B7B3-D57400DD1B25 Q34513618-7F79C91A-CD30-446A-9A7E-8764D61176CF Q34555735-D5611312-95C2-43B2-A029-DEFC6BCD4065 Q34571035-9DD47FA6-E5E5-4A43-B472-64B46631E9AD Q34714315-49EB88E5-42E8-4A13-AE9F-7441179064EE Q35089000-1748866E-C38B-4E4A-BB77-D981D9758D14 Q35451324-82A2FD6E-5646-4C9E-8EFA-32C552262B4B Q35616247-B79677F3-635B-47B6-B977-139B9A832968 Q35728198-466B74FD-4FE8-4CD7-8FF7-5FDDC009764D

P2860

Enlarging the amino acid set of Escherichia coli by infiltration of the valine coding pathway.

http://www.wikidata.org/entity/Q43582952

description

2001 nî lūn-bûn

@nan

2001年の論文

@ja

2001年学术文章

@wuu

2001年学术文章

@zh

2001年学术文章

@zh-cn

2001年学术文章

@zh-hans

2001年学术文章

@zh-my

2001年学术文章

@zh-sg

2001年學術文章

@yue

2001年學術文章

@zh-hant

name

Enlarging the amino acid set o ...... of the valine coding pathway.

@en

Enlarging the amino acid set o ...... of the valine coding pathway.

@nl

type

label

Enlarging the amino acid set o ...... of the valine coding pathway.

@en

Enlarging the amino acid set o ...... of the valine coding pathway.

@nl

prefLabel

Enlarging the amino acid set o ...... of the valine coding pathway.

@en

Enlarging the amino acid set o ...... of the valine coding pathway.

@nl

P1433

Q43582952-8A4C60F7-9EB1-4104-94A0-447377D9514F

P1476

Q43582952-D847AF3F-5780-4C58-A4EC-11576BBA516B

P2093

Q43582952-0EC2E183-BD4E-4382-B35E-C825F883ABE0

Q43582952-1F2B27A0-1CF6-409E-A963-394F486913D0

Q43582952-2E815DEB-D2D6-49B4-AD98-2055DAC2CB43

Q43582952-58B6BBB6-4EC7-4E1C-8036-3612091D607A

Q43582952-848663F9-E5A3-4AF2-B3D1-EB3C5FC6CCDB

Q43582952-B8EDFA45-5531-47AF-A7DC-73244592319A

Q43582952-BEA684AA-E3D9-463A-918C-C4035085C140

P2860

Q43582952-07553456-437A-4866-A820-E73E0AEB6F05

Q43582952-0F1DD5DE-50F3-4607-B84A-95556A5C1C7B

Q43582952-17B29EBD-8924-4DD8-A1DE-39180CD06280

Q43582952-1ED4D715-691A-49B5-9C81-D54CF42EF192

Q43582952-26E84680-2478-4D7A-B1D3-9530F4462147

Q43582952-5B1305C3-B7DD-402F-84EC-C644C583490B

Q43582952-6B3A55C9-2A4A-40E8-8EBF-E1F71B662F5F

Q43582952-81A5BE47-183B-4943-A0D6-B92EBD08539A

Q43582952-8A37C9B5-4489-4D53-A74A-5236C397552D

Q43582952-B6B84D7E-A946-4FDE-8699-473FC4766DF5

P304

Q43582952-C8E890D5-0B7A-49AC-B86C-CB054567CE25

P31

Q43582952-0F818A0E-48DB-426A-A44E-5085F9763286

P356

Q43582952-5298CA6E-587E-441C-A96A-3690097502D2

P407

Q43582952-D00AA6A2-5C21-4128-9F25-5432ACDA0285

P433

Q43582952-DD8F1293-7994-48F2-BA0F-05D57066A3C8

P478

Q43582952-6378036D-0F36-40F6-9153-A56140971DDE

P577

Q43582952-28AA2A19-44A7-4E2F-8691-BACC72E7E2EC

P698

Q43582952-86C35FDE-F118-49F4-A438-06DEDD57161E

P921

Q43582952-7B167104-0EF7-4E1F-BB12-8AD5272763BB

P356

SCIENCE.1057718

P1433

P1476

Enlarging the amino acid set o ...... of the valine coding pathway.

@en

P2093

Döring V

http://www.w3.org/2001/XMLSchema#string

Hendrickson TL

http://www.w3.org/2001/XMLSchema#string

Marlière P

http://www.w3.org/2001/XMLSchema#string

Mootz HD

http://www.w3.org/2001/XMLSchema#string

Nangle LA

http://www.w3.org/2001/XMLSchema#string

Schimmel P

http://www.w3.org/2001/XMLSchema#string

de Crécy-Lagard V

http://www.w3.org/2001/XMLSchema#string

P2860

Twenty-first aminoacyl-tRNA synthetase-suppressor tRNA pairs for possible use in site-specific incorporation of amino acid analogues into proteins in eukaryotes and in eubacteria

Enzyme structure with two catalytic sites for double-sieve selection of substrate

Aminoacyl-tRNA synthesis

Comparative physiological effects of incorporated amino acid analogs in Escherichia coli.

Functional role of cysteine-146 in Escherichia coli thymidylate synthase.

Reasons for the occurrence of the twenty coded protein amino acids.

Progress toward the evolution of an organism with an expanded genetic code.

Selenocysteine: the 21st amino acid.

Primary structure of the Escherichia coli thyA gene and its thymidylate synthase product.

Peptide transport and metabolism in bacteria.

P304

501-504

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1126/SCIENCE.1057718

http://www.w3.org/2001/XMLSchema#string

P407

P433

5516

http://www.w3.org/2001/XMLSchema#string

P478

292

http://www.w3.org/2001/XMLSchema#string

P577

2001-04-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

11313495

http://www.w3.org/2001/XMLSchema#string

P921

Escherichia coli