Efficient site-specific labeling of proteins via cysteines. - Wikidata - awgldk - TriplyDB

Efficient site-specific labeling of proteins via cysteines.

Efficient site-specific labeling of proteins via cysteines.

http://www.wikidata.org/entity/Q34909537

about

Hydrogen sulfide-linked sulfhydration of NF-κB mediates its antiapoptotic actions Click chemistry in complex mixtures: bioorthogonal bioconjugation Cys34-PEGylated Human Serum Albumin for Drug Binding and Delivery Surface plasmon resonance: a versatile technique for biosensor applications Correlating Calmodulin Landscapes with Chemical Catalysis in Neuronal Nitric Oxide Synthase using Time-Resolved FRET and a 5-Deazaflavin Thermodynamic Trap Proteomic approaches to quantify cysteine reversible modifications in aging and neurodegenerative diseases.Chemical cross-linkers for protein structure studies by mass spectrometry.Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET.Optimized delivery of fluorescently labeled proteins in live bacteria using electroporation Improved production of recombinant human Fas ligand extracellular domain in Pichia pastoris: yield enhancement using disposable culture-bag and its application to site-specific chemical modifications.STARD4 Membrane Interactions and Sterol Binding.Determining serpin conformational distributions with single molecule fluorescence Selective N-terminal functionalization of native peptides and proteins.Facile and stabile linkages through tyrosine: bioconjugation strategies with the tyrosine-click reaction.Single molecule FRET reveals pore size and opening mechanism of a mechano-sensitive ion channel.A novel approach to the site-selective dual labelling of a protein via chemoselective cysteine modification.Selective chemical labeling of proteins.Designing disorder: Tales of the unexpected tails.Site-selective incorporation and ligation of protein aldehydes.Novel mechanism of gene regulation: the protein Rv1222 of Mycobacterium tuberculosis inhibits transcription by anchoring the RNA polymerase onto DNA.Peptide-Appended Permethylated β-Cyclodextrins with Hydrophilic and Hydrophobic Spacers.In vivo assembly and single-molecule characterization of the transcription machinery from Shewanella oneidensis MR-1.Nanofibrillar Peptide hydrogels for the immobilization of biocatalysts for chemical transformations.Bacillus subtilis δ Factor Functions as a Transcriptional Regulator by Facilitating the Open Complex Formation.Methylsulfonyl benzothiazole (MSBT): a selective protein thiol blocking reagent.Competition between Tropomyosin, Fimbrin, and ADF/Cofilin drives their sorting to distinct actin filament networks.Caging and Photoactivation in Single-Molecule Förster Resonance Energy Transfer Experiments.Preparation of stable maleimide-functionalized au nanoparticles and their use in counting surface ligands.Promoter Escape with Bacterial Two-component σ Factor Suggests Retention of σ Region Two in the Elongation Complex.Site-selective azide incorporation into endogenous RNase A via a "chemistry" approach.Genetic encoding of caged cysteine and caged homocysteine in bacterial and mammalian cells.Proline-directed pseudo-phosphorylation at AT8 and PHF1 epitopes induces a compaction of the paperclip folding of Tau and generates a pathological (MC-1) conformation.A quantum dot-MUC1 aptamer conjugate for targeted delivery of protoporphyrin IX and specific photokilling of cancer cells through ROS generation.Fluorescence Quenching Studies of γ-Butyrolactone-Binding Protein (CprB) from Streptomyces coelicolor A3(2).Nanobodies: Chemical Functionalization Strategies and Intracellular Applications.Convenient Access to Fluorescent Probes by Chemoselective Acylation of Hydrazinopeptides: Application to the Synthesis of the First Far-Red Ligand for Apelin Receptor Imaging.Toward intrinsically colored peptides: Synthesis and investigation of the spectral properties of methylated azatryptophans in tryptophan-cage mutants.Comparison of established and novel methods for the detection and enumeration of microparticles in canine stored erythrocyte concentrates for transfusion.Methodologies for wiring redox proteins/enzymes to electrode surfaces.The TatA component of the twin-arginine translocation system locally weakens the cytoplasmic membrane of Escherichia coli upon protein substrate binding.

P2860

Q24301813-DD4A373A-6A0D-44BA-A4BF-D1C5E0BA3BC8 Q26828895-58868D55-443F-4FEE-B03A-5447F7820867 Q27301475-830382DB-662E-47AD-9C54-C7E2C9D755EC Q28084507-40374941-C7AC-436C-8441-A97D5E4E4142 Q28829445-C6741F20-1E8D-47BF-9F22-BB5A26243978 Q30393354-D73BA2F2-D006-435F-AA23-0A069D8EA85A Q30424964-7B440ACF-51D0-4673-8CE7-C7D662C409A4 Q33762981-73B5ABB9-53BE-4336-BC6C-CFC4DDC946FF Q33813284-4354BB01-3884-4478-B53B-67A8DD0F5FC9 Q35115597-4B1270B1-0E0D-4B77-98A0-627F18521DD5 Q35923335-0B7D601A-8F17-48D7-B618-3E7A5CCB48D6 Q36058093-805E7C89-937F-4D56-A428-B1A9AA7E2DD5 Q36383973-1BA46812-B2D5-4E4E-BE63-D9E67AA95FAF Q36857353-4C122689-7651-443D-B330-5A96878E9785 Q37587497-D8BD27F3-6903-4C09-B4E1-7BBE47DB5598 Q38728279-45B8314E-0C40-442E-97FE-1B0A262F8C92 Q38759843-1448257E-6D44-4469-846C-439CD61AE8BA Q38779715-15B713D0-6CF0-4393-A138-B0C39159AB13 Q38887360-F500C702-C22A-448A-8D9A-D25011C96274 Q41128029-438227A5-F8EB-4CCF-8CC1-8B0AD74DAACD Q41450733-3E1B95E2-E8CB-4ACD-AFC8-1F508E7B5037 Q41823965-F7502983-A79A-4171-8A0B-747C40A20E74 Q41998666-5B16CDE9-E5CE-447E-9BCB-2634DC75B475 Q42212403-B37A6ED0-CF62-4906-AD50-767077AC6D4E Q42228121-212E925A-710F-452A-BD4D-BD4D12089EDA Q42290514-0A22E94F-4AD6-4C50-98BD-7EC605D32436 Q42291744-86191119-0084-41ED-B826-1EB56895A405 Q43058839-152A0604-E30B-43AD-A31D-4929C1EF5F29 Q43163185-95986956-A054-42E3-A7C6-D75D4E0F3AA9 Q44451075-7C4EBC96-9C9B-4C0C-9A5C-A8B2376E0CDD Q44874415-B029085B-1B68-466A-A484-34AFB80731D6 Q46412461-2DEC9A0F-4094-4453-BA7A-0D00DCEE55DF Q46479658-199EF6D6-DBB0-468B-94F9-9BB4A7D2ED3A Q47411058-E8124125-A0A8-41AF-A4B2-47A35124E944 Q47797367-D4E61E67-CA98-4109-9924-A4E2CD8C25E1 Q48278244-EDFD6237-D0AF-44C1-B013-265A89E86247 Q50438670-303C14E9-DCF1-4D92-B793-431354407D67 Q51020070-D2EB0CA2-7FAF-43DE-8157-C48B1025F945 Q52594680-37484387-B240-4E1B-B5E9-BEE22FFAE4EF Q54208079-3EFF0116-F41F-4650-9846-15EDFDA34B44

P2860

Efficient site-specific labeling of proteins via cysteines.

http://www.wikidata.org/entity/Q34909537

description

2008 nî lūn-bûn

@nan

2008 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

Efficient site-specific labeling of proteins via cysteines.

@ast

Efficient site-specific labeling of proteins via cysteines.

@en

Efficient site-specific labeling of proteins via cysteines.

@nl

type

label

Efficient site-specific labeling of proteins via cysteines.

@ast

Efficient site-specific labeling of proteins via cysteines.

@en

Efficient site-specific labeling of proteins via cysteines.

@nl

prefLabel

Efficient site-specific labeling of proteins via cysteines.

@ast

Efficient site-specific labeling of proteins via cysteines.

@en

Efficient site-specific labeling of proteins via cysteines.

@nl

P1433

Q34909537-D3B446AC-F099-4A19-B492-D0358E0EA690

P1476

Q34909537-0EC65F9E-7A1A-4405-A4AA-217DDBE48499

P2093

Q34909537-266376E9-5E0D-4809-B3C1-FC70408E60C8

Q34909537-3431B461-C4BB-417C-A1AF-C499407305FB

Q34909537-A18BE175-21B3-4936-ACA9-298236C46A4A

Q34909537-C168C8B5-000A-46F5-92A6-AAB3710D0402

P2860

Q34909537-1633C3DC-7905-491A-B004-20E237DEF961

Q34909537-1AD52909-9623-45B7-A6AC-C4275F93E76D

Q34909537-2264F411-EA84-4823-9A58-FA41BC440C81

Q34909537-256D568D-0A70-4E33-96F8-B6E6362A308C

Q34909537-29423C77-4E06-41E4-A0F9-4C1AE19495E8

Q34909537-29851993-280D-4348-B0F4-48177DED7308

Q34909537-2EEAB39E-D7BB-41D6-B4C3-47A5265B06C5

Q34909537-3D0D54B2-3406-4EB9-8315-FD3BB500C142

Q34909537-435EEC76-ED96-44C9-AF6E-5BDBA7412D48

Q34909537-4D199222-C403-4EAB-950E-B39545E0F9C8

P304

Q34909537-9B828A7D-4312-4572-B79B-1371979A463C

P31

Q34909537-722D00CC-CAEB-4C46-B7F4-BC7FE1432C23

P356

Q34909537-8B766F4B-7051-4208-A165-846B16ECF0D2

P433

Q34909537-1CE3AC3A-8882-4347-8CC5-A260B71C01DE

P478

Q34909537-C710D22E-C2CD-4965-83F0-FAAD5D5F8446

P50

Q34909537-059D5F29-75EE-4C7F-A4C8-A781D24243F3

Q34909537-A880EC78-7BFB-4E08-9D56-CE0B19C1B0C3

Q34909537-F274293A-9AA3-43F5-9F69-C9893415FE33

P577

Q34909537-DCF4BB1C-F310-47C4-9A6A-6C4BAA2E1C7C

P5875

Q34909537-3ECB8769-1A39-4EE0-828E-D07E67D34E4F

P698

Q34909537-EB5F70EF-901A-48DF-AB23-813930EA9C67

P932

Q34909537-479558C8-E98D-4C93-9FA8-F882F3E8B984

P356

P1433

Bioconjugate Chemistry

P1476

Efficient site-specific labeling of proteins via cysteines.

@en

P2093

Elizabeth V Landorf

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

Sam O Ho

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

You Korlann

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

Younggyu Kim

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

P2860

Initial transcription by RNA polymerase proceeds through a DNA-scrunching mechanism

Thiol-reactive dyes for fluorescence labeling of proteomic samples

An expanded eukaryotic genetic code

Mechanistic investigation of the staudinger ligation

Polyphasic taxonomy of the genus Shewanella and description of Shewanella oneidensis sp. nov.

Direct observation of abortive initiation and promoter escape within single immobilized transcription complexes.

Fluorescence-aided molecule sorting: analysis of structure and interactions by alternating-laser excitation of single molecules.

Site-specific labeling of proteins for single-molecule FRET by combining chemical and enzymatic modification

Three-color alternating-laser excitation of single molecules: monitoring multiple interactions and distances.

Structural organization of the RNA polymerase-promoter open complex.

P304

786-791

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

P31

scholarly article

P356

10.1021/BC7002499

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

P433

3

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

P478

19

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

P50

Frank R. Collart

Natalie Gassman

P577

2008-02-15T00:00:00Z

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

P5875

5577213

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

P698

18275130

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

P932

3086356

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