A minimal receptor-Ig chimera of human FcepsilonRI alpha-chain efficiently binds secretory and membrane IgE.

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In vivo site-specific biotinylation of proteins within the secretory pathway using a single vector system.Selective targeting of proteins within secretory pathway for endoplasmic reticulum-associated degradation.

P2860

Q33329274-003A360A-F9EB-4ABC-B77C-159A229BC249 Q36016810-42048109-E646-4B1F-9630-1A03C9AADA4B

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A minimal receptor-Ig chimera of human FcepsilonRI alpha-chain efficiently binds secretory and membrane IgE.

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http://www.wikidata.org/entity/Q40751190

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2002 nî lūn-bûn

@nan

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

2002年论文

@zh

2002年论文

@zh-cn

name

A minimal receptor-Ig chimera ...... ds secretory and membrane IgE.

@en

type

Item

label

A minimal receptor-Ig chimera ...... ds secretory and membrane IgE.

@en

prefLabel

A minimal receptor-Ig chimera ...... ds secretory and membrane IgE.

@en

P1476

A minimal receptor-Ig chimera ...... ds secretory and membrane IgE.

@en

P2093

Michela Cesco-Gaspere

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

Oscar Burrone

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

Roberto Lorenzi

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

P2860

Structure of the Fc fragment of human IgE bound to its high-affinity receptor Fc epsilonRI alpha

The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex

Crystal structure and immunoglobulin G binding properties of the human major histocompatibility complex-related Fc receptor(,)

Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution

Crystal structure of the human high-affinity IgE receptor

SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling

The high-affinity IgE receptor (Fc epsilon RI): from physiology to pathology.

Signalling through the high-affinity IgE receptor Fc epsilonRI.

The immunoglobulin-like modules Cepsilon3 and alpha2 are the minimal units necessary for human IgE-FcepsilonRI interaction.

Recombinant soluble form of the human high-affinity immunoglobulin E (IgE) receptor inhibits IgE production through its specific binding to IgE-bearing B cells.

P304

51-57

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scholarly article

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10.1093/PROTEIN/15.1.51

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

P433

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

P478

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

P50

Luca Vangelista

P577

2002-01-01T00:00:00Z

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

P5875

247572822

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

P698

11842238

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

A minimal receptor-Ig chimera of human FcepsilonRI alpha-chain efficiently binds secretory and membrane IgE.

about

P2860

P2860

A minimal receptor-Ig chimera of human FcepsilonRI alpha-chain efficiently binds secretory and membrane IgE.

description

name

type

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prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698