A monovalent streptavidin with a single femtomolar biotin binding site - Wikidata - wikimedia - TriplyDB

A monovalent streptavidin with a single femtomolar biotin binding site

A monovalent streptavidin with a single femtomolar biotin binding site

http://www.wikidata.org/entity/Q24645981

about

Cholesterol loading and ultrastable protein interactions determine the level of tumor marker required for optimal isolation of cancer cells Compact biocompatible quantum dots via RAFT-mediated synthesis of imidazole-based random copolymer ligand Next-generation optical technologies for illuminating genetically targeted brain circuits The origins of femtomolar protein-ligand binding: hydrogen-bond cooperativity and desolvation energetics in the biotin-(strept)avidin binding site Monovalent, reduced-size quantum dots for imaging receptors on living cells Mapping the dynamics and nanoscale organization of synaptic adhesion proteins using monomeric streptavidin Site-specific protein modification using lipoic acid ligase and bis-aryl hydrazone formation How the biotin–streptavidin interaction was made even stronger: investigation via crystallography and a chimaeric tetramer Structural Adaptation of a Thermostable Biotin-binding Protein in a Psychrophilic Environment Plug-and-Play Pairing via Defined Divalent Streptavidins Structure-based engineering of streptavidin monomer with a reduced biotin dissociation rate Structure of active dimeric human telomerase.Kv2.1 cell surface clusters are insertion platforms for ion channel delivery to the plasma membrane Neuroligin1: a cell adhesion molecule that recruits PSD-95 and NMDA receptors by distinct mechanisms during synaptogenesis Site-specific protein labeling using PRIME and chelation-assisted click chemistry Measuring transmembrane helix interaction strengths in lipid bilayers using steric trapping.Designed auto-assembly of nanostreptabodies for rapid tissue-specific targeting in vivo.Flagellar hook flexibility is essential for bundle formation in swimming Escherichia coli cells.Photocrosslinkable pMHC monomers stain T cells specifically and cause ligand-bound TCRs to be 'preferentially' transported to the cSMAC.Plasma membrane domains enriched in cortical endoplasmic reticulum function as membrane protein trafficking hubs Phage display evolution of a peptide substrate for yeast biotin ligase and application to two-color quantum dot labeling of cell surface proteins.Bifunctional avidin with covalently modifiable ligand binding site.The heparin-binding domain of HB-EGF mediates localization to sites of cell-cell contact and prevents HB-EGF proteolytic release.Identification and characterization of alkaline serine protease from goat skin surface metagenome Single-molecule-based super-resolution images in the presence of multiple fluorophores Surface ligand effects on metal-affinity coordination to quantum dots: implications for nanoprobe self-assembly.The kinetics of two-dimensional TCR and pMHC interactions determine T-cell responsiveness.Non-covalent ligand conjugation to biotinylated DNA nanoparticles using TAT peptide genetically fused to monovalent streptavidin.Method to measure strong protein-protein interactions in lipid bilayers using a steric trap.SpyAvidin hubs enable precise and ultrastable orthogonal nanoassembly.Local clustering of transferrin receptors promotes clathrin-coated pit initiation.Redirecting lipoic acid ligase for cell surface protein labeling with small-molecule probes.Imaging LDL receptor oligomerization during endocytosis using a co-internalization assay.Design and characterization of a membrane protein unfolding platform in lipid bilayers.Monovalent Strep-Tactin for strong and site-specific tethering in nanospectroscopy.A novel approach to make homogeneous protease-stable monovalent streptavidin.The molecular architecture of human Dicer.HIT: a versatile proteomics platform for multianalyte phenotyping of cytokines, intracellular proteins and surface molecules.Structure and specificity of the RNA-guided endonuclease Cas9 during DNA interrogation, target binding and cleavage The extradomain a of fibronectin enhances the efficacy of lipopolysaccharide defective Salmonella bacterins as vaccines in mice

P2860

Q24594878-73DBDB32-9F35-43C5-8196-EDB3A6CDBE27 Q24615930-77707FEF-2691-49F8-B550-6A7191FB503B Q24649053-770B6AA3-462A-431E-9374-B6D2CBA1F4A0 Q24655859-30E8F6A0-1FA5-40DE-A1F6-F1BFE48396D1 Q24656938-6A690E45-CDE2-4A49-9EE3-17C5781A7D83 Q27330372-65A82527-3698-448F-8F1F-34F238149E68 Q27339271-3B7575F5-5E09-4986-890B-781847925F8C Q27666604-13A5AD20-462C-4EFE-964C-43349410AAC2 Q27678441-45A6B451-BC2D-4E41-88E3-FFDC7F30E364 Q27680010-C07E2B60-256D-4818-824C-96C30DCADB8E Q27684611-AAA09DE9-00E3-451D-B4F4-FD37F98675E3 Q28115347-CEF887BB-8BE8-4DFA-BB63-22AAF1313165 Q28575863-13798198-28EA-4965-B560-8DF31F0608AC Q28581737-3DA4B5F9-36A9-47C5-938B-3FC46E3208C5 Q28829219-F6ED9481-2B32-4D7D-BD28-7CF67BBD1C59 Q30357100-7AA2FB17-C02C-40B4-A784-5E80D5047B2B Q30492713-E4E46BA1-E787-4812-84CC-8E284343BE10 Q30524723-D23BDDE8-3B06-41C1-84A4-2F3C090A2F05 Q30539566-9901CE4D-BF9F-4125-996C-A613EE76BD80 Q30543827-E4156255-CAD4-4E81-9F92-370543604E5D Q33283337-167FF477-4CEC-4917-A35F-354F388196AE Q33815940-646FC83B-FD83-457B-B7E0-592A91DC9A98 Q33917661-003F4D6D-15F7-4D8F-8F5E-DCA42378D9F9 Q34015367-AEAD6E4D-2E6D-427F-91E8-C5909F4F02AA Q34049457-893EB3C0-6179-48AA-832A-5308578CEA66 Q34050648-BA8B5EB4-2246-4BE3-8792-78EE09E1CA4B Q34078621-136C3CFC-026C-4772-85E6-C2461FDE5828 Q34086269-86CABFE9-D3C0-4797-B574-A227A2268495 Q34358811-53451A10-A774-4A93-8AC8-DC2E69DD4A84 Q34433158-3F4B12C4-42CA-4D1B-8E17-BF5BD3642826 Q34439731-F8A22744-00BA-4874-9F44-9E027694F60D Q34721966-FD75E018-3BDB-491C-8E1B-AFD2FE50F3CE Q34803657-EB7BDAF8-0D1E-4B69-8A29-38B234953F11 Q35583955-71B4FED4-5382-42DA-9C25-AE9805927591 Q35803408-2032D7D8-36E7-4879-BECF-087399F1B260 Q35841372-9181AC59-D2DA-4903-A416-BDB0593C193A Q35871761-0DA8C566-C9D4-4BD1-94B2-170775CEBFF9 Q35906579-99D482F2-EF60-4754-B797-C552049973A2 Q36160691-35BCB62E-9A40-4BA3-98B3-E77679CA7CE3 Q36161454-5D59A2DC-1969-4287-8F56-010F4B6074C7

P2860

A monovalent streptavidin with a single femtomolar biotin binding site

http://www.wikidata.org/entity/Q24645981

description

2006 nî lūn-bûn

@nan

2006 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2006年の論文

@ja

2006年論文

@yue

2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

name

A monovalent streptavidin with a single femtomolar biotin binding site

@ast

A monovalent streptavidin with a single femtomolar biotin binding site

@en

A monovalent streptavidin with a single femtomolar biotin binding site

@nl

type

label

A monovalent streptavidin with a single femtomolar biotin binding site

@ast

A monovalent streptavidin with a single femtomolar biotin binding site

@en

A monovalent streptavidin with a single femtomolar biotin binding site

@nl

prefLabel

A monovalent streptavidin with a single femtomolar biotin binding site

@ast

A monovalent streptavidin with a single femtomolar biotin binding site

@en

A monovalent streptavidin with a single femtomolar biotin binding site

@nl

P1433

Q24645981-F90D19E5-4CBB-438B-9481-88C9D65168B1

P1476

Q24645981-4C23A7F0-ADA1-43FD-A5E2-E2E4AA23A852

P2093

Q24645981-519FE270-7464-4B5B-B24E-0CE8612E3FF2

Q24645981-5B1C02A9-0B96-4D09-B5EE-1F23C8184BB1

Q24645981-8C206A21-6F56-45CC-A4F7-26FD176E7CAE

Q24645981-A8395A2C-6D0A-4873-B960-A8015CA86F9A

Q24645981-E54DD847-1B18-45C8-B4C3-528B4F8C9614

Q24645981-EA795035-9CCD-49AC-825F-D2AC124A51EE

Q24645981-F73147B6-BF4E-4355-A911-EC871B1B6786

Q24645981-F7320413-5071-43E4-9E93-7F91B895F2C2

P2860

Q24645981-03590579-4D0D-415F-B19F-B49C6F8D0BE8

Q24645981-060B9722-3C55-4B65-8EF0-74FE6D58659B

Q24645981-09973C5C-E5C2-4CEA-A8D9-9C1647710FA0

Q24645981-0B19E82B-C52E-4152-A450-2595767914B9

Q24645981-0FBAAF46-29EE-4615-AF52-670B5FA51C4F

Q24645981-298FA6A9-9BE8-4D37-BC68-25B3092C245C

Q24645981-3E7B52F6-2949-482D-BAF4-0B0EA2337483

Q24645981-47209A06-6648-4DCE-84EC-39297625DC73

Q24645981-5AB7FF7F-B70D-444A-A219-30E9B837380E

Q24645981-5D52B6EA-4E96-47C8-99AD-D40509668372

P2888

Q24645981-68D92D25-2483-4653-B38B-0B28B1E241A5

P304

Q24645981-8EC8CCD0-7DE5-449C-A902-470E0E278557

P31

Q24645981-116010C9-10EC-4402-8E79-6DE0674FA8FC

P3181

Q24645981-0B4FDAB5-D928-4BF9-AAD6-80186AE4ADC5

P356

Q24645981-96D2A198-65A2-4F06-ACAB-AC8A29E696C4

P407

Q24645981-6D72F2BC-59EB-49EB-9B31-33AE153D0BC4

P433

Q24645981-86EDEE99-D90F-49DD-A670-0EF3389A4F6D

P478

Q24645981-C217F999-9E37-4900-AD83-F3A3407E8464

P577

Q24645981-4CB08F01-574F-4159-9E4A-7E77A39C4D56

P5875

Q24645981-BEBE4C40-5D5F-46C0-9188-E592AD4CDDB6

P6179

Q24645981-02AE33D2-4311-429A-9C66-0ABB3622E570

P698

Q24645981-9E7AFAED-6A6A-49D5-AD62-A574A7AFB10A

P932

Q24645981-5DA0A845-E8A2-4E1E-B176-68CC0F2128B1

P3181

P356

P1433

P1476

A monovalent streptavidin with a single femtomolar biotin binding site

@en

P2093

Alaa El-Husseini

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

Alice Y Ting

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

Daniel J-F Chinnapen

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

Kimberly Gerrow

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

Mark Howarth

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

Melanie R Grandy

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

Neil L Kelleher

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

Pieter C Dorrestein

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

P2860

Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons

Neurexins induce differentiation of GABA and glutamate postsynaptic specializations via neuroligins

Targeting quantum dots to surface proteins in living cells with biotin ligase.

Ser45 plays an important role in managing both the equilibrium and transition state energetics of the streptavidin-biotin system

Specific covalent labeling of recombinant protein molecules inside live cells

Neuroligins mediate excitatory and inhibitory synapse formation: involvement of PSD-95 and neurexin-1beta in neuroligin-induced synaptic specificity.

Engineered single-chain dimeric streptavidins with an unexpected strong preference for biotin-4-fluorescein

DNA-templated carbon nanotube field-effect transistor.

Bioorganic applications of semisynthetic DNA-protein conjugates.

Intersubunit contacts made by tryptophan 120 with biotin are essential for both strong biotin binding and biotin-induced tighter subunit association of streptavidin

P2888

P304

267-73

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

P31

scholarly article

P3181

2025194

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

P356

10.1038/NMETH861

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

P407

P433

4

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

P478

3

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

P577

2006-04-01T00:00:00Z

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

P5875

7224041

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

P6179

1036493223

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

P698

16554831

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

P932

2576293

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