Time‐Resolved Mn 2+ −NO and NO−NO Distance Measurements Reveal That Catalytic Asymmetry Regulates Alternating Access in an ABC Transporter **
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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Time‐Resolved Mn 2+ −NO and NO−NO Distance Measurements Reveal That Catalytic Asymmetry Regulates Alternating Access in an ABC Transporter ** ; day:07 ; month:08 ; year:2023 ; extent:10
Angewandte Chemie / International edition. International edition ; (07.08.2023) (gesamt 10)
- Creator
- DOI
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10.1002/anie.202307091
- URN
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urn:nbn:de:101:1-2023080815011593372959
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 10:52 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Rudolph, Michael
- Tampé, Robert
- Joseph, Benesh
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Zeitaufgelöste Mn 2+ −NO‐ und NO−NO‐Abstandsmessungen zeigen regulierende Funktion der katalytischen Asymmetrie auf den alternierenden Zugang in einem ABC‐Transporter **
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Mechanism of the MHC I chaperone TAPBPR and its role in promoting UGGT1-mediated quality control
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Selective and ATP-dependent translocation of peptides by the homodimeric ATP binding cassette transporter TAP-like (ABCB9)
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Zur Wechselwirkung von Glycophorin mit Lipidkomponenten in künstlichen Phospholipid-Doppelschichten : eine spektroskopische, elektronenmikroskopische und kalorimetrische Studie zur Lipid-Protein-Wechselwirkung
Zeitaufgelöste Mn 2+ −NO‐ und NO−NO‐Abstandsmessungen zeigen regulierende Funktion der katalytischen Asymmetrie auf den alternierenden Zugang in einem ABC‐Transporter **
Proofreading of peptide—MHC complexes through dynamic multivalent interactions
Mechanism of the MHC I chaperone TAPBPR and its role in promoting UGGT1-mediated quality control
Mechanistic insights into ribosome recycling and quality control in mRNA translation
Mechanistic and structural studies of the MHC I peptide loading complex
Membrane topology of the transporter associated with antigen processing (TAP1) within an assembled functional peptide-loading complex
The epidermal growth factor receptor is a relevant host factor in the early stages of the Zika virus life cycle in vitro
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)
Mechanistic and structural insights into the quality control of the MHC I antigen processing pathway
Structure and mechanism of the heterodimeric ABC translocation complexes TAP and TmrAB
Zur Wechselwirkung von Glycophorin mit Lipidkomponenten in künstlichen Phospholipid-Doppelschichten : eine spektroskopische, elektronenmikroskopische und kalorimetrische Studie zur Lipid-Protein-Wechselwirkung
Zeitaufgelöste Mn 2+ −NO‐ und NO−NO‐Abstandsmessungen zeigen regulierende Funktion der katalytischen Asymmetrie auf den alternierenden Zugang in einem ABC‐Transporter **
Proofreading of peptide—MHC complexes through dynamic multivalent interactions
Mechanism of the MHC I chaperone TAPBPR and its role in promoting UGGT1-mediated quality control
Mechanistic insights into ribosome recycling and quality control in mRNA translation
Mechanistic and structural studies of the MHC I peptide loading complex
Membrane topology of the transporter associated with antigen processing (TAP1) within an assembled functional peptide-loading complex
The epidermal growth factor receptor is a relevant host factor in the early stages of the Zika virus life cycle in vitro
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)
Mechanistic and structural insights into the quality control of the MHC I antigen processing pathway