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Joachim Koch (1972-)

Biologe

Name	Joachim Koch
Zeit	1972- (Lebensdaten)
Ort	Heidelberg (Wirkungsort) Remagen (Geburtsort) Deutschland
Geschlecht	männlich
Akademischer Grad bzw. Titel	Dr. (Fakultät für Biowissenschaften, Institu für Molekulare Genetik, Universität Heidelberg)
Beruf	Biologe (charakteristischer Beruf)
Variante	J. Koch
Beziehung	Universität Heidelberg Molekularbiologie (Thema)
Datensatztyp	Person
GND-Nummer	132932415
Datensatz-ID	132932415
Beteiligt an alle anzeigen A soluble fragment of the tumor antigen BCL2-associated athanogene 6 (BAG-6) is essential and sufficient for inhibition of NKp30 receptor-dependent cytotoxicity of natural killer cells Assembly and function of the major histocompatibility complex (MHC) I peptide-loading complex are conserved across higher vertebrates Crystal structure of the human Fe65-PTB1 domain Engineering ATPase activity in the isolated ABC cassette of human TAP1 Epstein-Barr viral BNLF2a protein hijacks the tail-anchored protein insertion machinery to block antigen processing by the transport complex TAP Functional dissection of the transmembrane domains of the transporter associated with antigen processing (TAP) Membrane topology of the transporter associated with antigen processing (TAP1) within an assembled functional peptide-loading complex Signaling of a varicelloviral factor across the endoplasmic reticulum membrane induces destruction of the peptide-loading complex and immune evasion Structure and dynamics of membrane-associated ICP47, a viral inhibitor of the MHC I antigen-processing machinery The C terminus of the Alb3 membrane insertase recruits cpSRP43 to the thylakoid membrane The stalk domain and the glycosylation status of the activating natural killer cell receptor NKp30 are important for ligand binding The stalk domain of NKp30 contributes to ligand binding and signaling of a preassembled NKp30-CD3ζ complex Schlauer als die Krebszellen : Biochemiker unterstützen die Arbeit natürlicher Killerzellen [[Elektronische Ressource]] Ökosystem statt Nutzwald Nano-coating protects biofunctional materials Humane rekombinante Antikörper gegen Hantaviren

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Joachim Koch (1972-)

A soluble fragment of the tumor antigen BCL2-associated athanogene 6 (BAG-6) is essential and sufficient for inhibition of NKp30 receptor-dependent cytotoxicity of natural killer cells

Assembly and function of the major histocompatibility complex (MHC) I peptide-loading complex are conserved across higher vertebrates

Crystal structure of the human Fe65-PTB1 domain

Engineering ATPase activity in the isolated ABC cassette of human TAP1

Epstein-Barr viral BNLF2a protein hijacks the tail-anchored protein insertion machinery to block antigen processing by the transport complex TAP

Functional dissection of the transmembrane domains of the transporter associated with antigen processing (TAP)

Membrane topology of the transporter associated with antigen processing (TAP1) within an assembled functional peptide-loading complex

Signaling of a varicelloviral factor across the endoplasmic reticulum membrane induces destruction of the peptide-loading complex and immune evasion

Structure and dynamics of membrane-associated ICP47, a viral inhibitor of the MHC I antigen-processing machinery

The C terminus of the Alb3 membrane insertase recruits cpSRP43 to the thylakoid membrane

The stalk domain and the glycosylation status of the activating natural killer cell receptor NKp30 are important for ligand binding

The stalk domain of NKp30 contributes to ligand binding and signaling of a preassembled NKp30-CD3ζ complex

Schlauer als die Krebszellen : Biochemiker unterstützen die Arbeit natürlicher Killerzellen [[Elektronische Ressource]]

Ökosystem statt Nutzwald

Nano-coating protects biofunctional materials

Humane rekombinante Antikörper gegen Hantaviren