about
Pyrrolysyl-tRNA synthetase: an ordinary enzyme but an outstanding genetic code expansion toolAminophosphonate inhibitors of dialkylglycine decarboxylase: structural basis for slow binding inhibitionStructural basis for the recognition of para-benzoyl-L-phenylalanine by evolved aminoacyl-tRNA synthetasesA genetically encoded bidentate, metal-binding amino acidA genetically encoded diazirine photocrosslinker in Escherichia coliTowards reassigning the rare AGG codon in Escherichia coliSelecting folded proteins from a library of secondary structural elements.The genetic incorporation of thirteen novel non-canonical amino acidsA genetically encoded aldehyde for rapid protein labellingProbing the Catalytic Charge-Relay System in Alanine Racemase with Genetically Encoded Histidine Mimetics.Two rapid catalyst-free click reactions for in vivo protein labeling of genetically encoded strained alkene/alkyne functionalities.Genetically encoded unstrained olefins for live cell labeling with tetrazine dyes.Nonsense and sense suppression abilities of original and derivative Methanosarcina mazei pyrrolysyl-tRNA synthetase-tRNA(Pyl) pairs in the Escherichia coli BL21(DE3) cell strainImproving the bioactivity of rHirudin with boronophenylalanine site-specific modification.Facile Removal of Leader Peptides from Lanthipeptides by Incorporation of a Hydroxy AcidA rationally designed pyrrolysyl-tRNA synthetase mutant with a broad substrate spectrumFluorinated Aromatic Amino Acids Distinguish Cation-π Interactions from Membrane InsertionCatalyst-free and site-specific one-pot dual-labeling of a protein directed by two genetically incorporated noncanonical amino acidsGenetically encoded fluorophenylalanines enable insights into the recognition of lysine trimethylation by an epigenetic reader.Genetic incorporation of twelve meta-substituted phenylalanine derivatives using a single pyrrolysyl-tRNA synthetase mutantThe "π-Clamp" Offers a New Strategy for Site-Selective Protein Modification.A genetically encoded acrylamide functionality.Phospha-Michael Addition as a New Click Reaction for Protein Functionalization.Effects of End Group Termination on Salting-Out Constants for Triglycine.Genetic incorporation of seven ortho-substituted phenylalanine derivatives.Synthesis of proteins with defined posttranslational modifications using the genetic noncanonical amino acid incorporation approach.Role of Q52 in catalysis of decarboxylation and transamination in dialkylglycine decarboxylase.Sirtuins 1 and 2 Are Universal Histone Deacetylases.Near-cognate suppression of amber, opal and quadruplet codons competes with aminoacyl-tRNAPyl for genetic code expansion.Expanding the chemical diversity of lasso peptide MccJ25 with genetically encoded noncanonical amino acids.Genetically Encoded 2-Aryl-5-carboxytetrazoles for Site-Selective Protein Photo-Cross-Linking.A genetically encoded photocaged Nepsilon-methyl-L-lysine.Kinetic and thermodynamic analysis of the interaction of cations with dialkylglycine decarboxylase.E1-catalyzed ubiquitin C-terminal amidation for the facile synthesis of deubiquitinase substrates.Reversal of the hofmeister series: specific ion effects on peptides.A Genetically Encoded Allysine for the Synthesis of Proteins with Site-Specific Lysine Dimethylation.tRNAPyl: Structure, function, and applications.A Versatile Approach for Site-Specific Lysine Acylation in Proteins.Proteins with Site-Specific Lysine Methylation.Genetic code expansion: Synthetases pick up the PACE.
P50
Q26850882-FCA93066-C741-4A23-98CD-4B2642684739Q27639753-827B25C6-E002-4A61-AC32-5DD986A36F12Q27646662-F77F2191-1796-4D52-B34E-E72472454095Q27648487-E45302AD-ED2F-49E3-B82A-4D6A661BF32BQ27649029-C9638E32-E923-47A1-8DBF-3B4FB3C31C90Q28244340-AF054C95-90A5-469B-8CBF-24805C83F5FAQ33309329-7580A76C-FCD0-4683-A226-AAB3F86050A0Q33571583-CE393DB4-43BA-41DB-8EA2-EDDE6C883623Q33774216-7A370A32-4AB6-4958-AE66-BEC5EF75B171Q33817575-3E9B1E82-D293-425F-81D8-7F816E26BCC4Q34196992-0EA087F5-12C7-4496-9625-7B8ABD421D45Q34287968-B00A4ED6-FE98-4E92-BFF8-3BDFACFA23AFQ34631659-191F5B4E-F40F-4A31-93E8-AF1C24C608F9Q35542278-4C39A110-42CA-47F2-A92A-8065C8E60C98Q35640582-28B46397-C787-466B-A7E2-543DC986F2BFQ35784598-D7A9298A-6DFB-4112-B046-DE8CFB263492Q35905418-B0DED14B-6961-4B73-B01E-627FF3B11517Q36075683-10094FD4-4FF1-4186-A79D-0D0ADF6BE4EFQ36155490-4637BBBE-6D7C-4A0A-992A-8A9F8D7CB03BQ36614988-456D0B11-1B0B-431B-88DF-2C1745AE34F3Q37077812-A2F6DEE0-7BFD-4E95-8DE6-659D0ED0B95CQ37101354-BCC72275-B320-4A3B-BDED-C2CCCAFF5CE5Q37330789-78EED7FA-A933-4987-BB9A-68C9C3E12A64Q37503451-FCAB8279-303D-4BA4-A6F6-F14BA7F0A369Q37720490-0F6936C3-D25F-44F5-AC7A-76DFB8D8585AQ37810786-04404B99-7282-4453-AED5-D5B1D606606FQ38317833-AD983888-96FD-48CE-ACFD-994782A07EA7Q38798846-A6CE5E11-B71C-4B37-8F0A-15BBB5C367B3Q41511627-447A8258-9FC9-4BB7-A3CC-81B38233A714Q41656633-6D4E9216-797C-4FD7-8095-0449D9724275Q42282926-28D3AFF7-B65B-45AF-8BD9-C07ED428A0E2Q42936853-5FB17037-62FD-4A84-A4FB-B5184F120DF6Q44861335-AB330E3B-0154-4F2E-BA38-E3BD66279180Q45183246-14FDD9E8-FCC0-4A5A-8866-C5AEECA9A3F5Q46038267-EE276B72-5E7B-4E23-9FE9-A8C0B64A7291Q47129712-7B8E79E5-B185-4BDD-B918-36E643A7D1ADQ47911274-5E6F28B1-C48F-4480-B1CD-5F840B811F12Q48103473-4DB0D320-A7E8-4129-B46F-2289E2434709Q48148437-2B129D96-CF10-4D20-9D8F-CF620473D9E7Q48261671-FECA5569-AD94-4441-AD1B-9F1EC0EB53D9
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Wenshe R Liu
@ast
Wenshe R Liu
@en
Wenshe R Liu
@es
Wenshe R Liu
@nl
type
label
Wenshe R Liu
@ast
Wenshe R Liu
@en
Wenshe R Liu
@es
Wenshe R Liu
@nl
prefLabel
Wenshe R Liu
@ast
Wenshe R Liu
@en
Wenshe R Liu
@es
Wenshe R Liu
@nl
P106
P31
P496
0000-0002-7078-6534