Specific lipids modulate the transporter associated with antigen processing (TAP)
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
Online-Ressource
- Sprache
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Englisch
- Erschienen in
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In: Journal of biological chemistry, 286.2011, 15, S. 13346-13356
- Ereignis
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Veröffentlichung
- (wo)
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Frankfurt am Main
- (wer)
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Universitätsbibliothek Johann Christian Senckenberg
- (wann)
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2021
- Urheber
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Schölz, Christian
Parcej, David
Stenby Ejsing, Christer
Robenek, Horst
Urbatsch, Ina L.
Tampé, Robert
- DOI
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10.1074/jbc.M110.216416
- URN
-
urn:nbn:de:hebis:30:3-765801
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
14.08.2025, 11:01 MESZ
Datenpartner
Dieses Objekt wird bereitgestellt von:
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Beteiligte
- Schölz, Christian
- Parcej, David
- Stenby Ejsing, Christer
- Robenek, Horst
- Urbatsch, Ina L.
- Tampé, Robert
- Universitätsbibliothek Johann Christian Senckenberg
Entstanden
- 2021
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Functional non-equivalence of ATP-binding cassette signature motifs in the transporter associated with antigen processing (TAP)
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Zur Wechselwirkung von Glycophorin mit Lipidkomponenten in künstlichen Phospholipid-Doppelschichten : eine spektroskopische, elektronenmikroskopische und kalorimetrische Studie zur Lipid-Protein-Wechselwirkung
Selective and ATP-dependent translocation of peptides by the homodimeric ATP binding cassette transporter TAP-like (ABCB9)
Functional non-equivalence of ATP-binding cassette signature motifs in the transporter associated with antigen processing (TAP)
Structure and mechanism of the heterodimeric ABC translocation complexes TAP and TmrAB
Time‐Resolved Mn 2+ −NO and NO−NO Distance Measurements Reveal That Catalytic Asymmetry Regulates Alternating Access in an ABC Transporter **
Functional dissection of the transmembrane domains of the transporter associated with antigen processing (TAP)
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Engineering and stabilization of the heterodimeric ABC exporters TAP and TmrAB for functional and structural studies
Peptides induce ATP hydrolysis at both subunits of the transporter associated with antigen processing
Membrane topology of the transporter associated with antigen processing (TAP1) within an assembled functional peptide-loading complex
An annular lipid belt is essential for allosteric coupling and viral inhibition of the antigen translocation complex TAP (transporter associated with antigen processing)
Interdomain communication in a homodimeric ABC transporter
Zur Wechselwirkung von Glycophorin mit Lipidkomponenten in künstlichen Phospholipid-Doppelschichten : eine spektroskopische, elektronenmikroskopische und kalorimetrische Studie zur Lipid-Protein-Wechselwirkung
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Functional non-equivalence of ATP-binding cassette signature motifs in the transporter associated with antigen processing (TAP)
Structure and mechanism of the heterodimeric ABC translocation complexes TAP and TmrAB
Time‐Resolved Mn 2+ −NO and NO−NO Distance Measurements Reveal That Catalytic Asymmetry Regulates Alternating Access in an ABC Transporter **
Functional dissection of the transmembrane domains of the transporter associated with antigen processing (TAP)
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Engineering and stabilization of the heterodimeric ABC exporters TAP and TmrAB for functional and structural studies
Peptides induce ATP hydrolysis at both subunits of the transporter associated with antigen processing
Membrane topology of the transporter associated with antigen processing (TAP1) within an assembled functional peptide-loading complex
An annular lipid belt is essential for allosteric coupling and viral inhibition of the antigen translocation complex TAP (transporter associated with antigen processing)