Peptides induce ATP hydrolysis at both subunits of the transporter associated with antigen processing

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Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: Online-Ressource

Language: Englisch

Bibliographic citation: In: Journal of biological chemistry, 278.2003, 32, S. 29686-29692

Event: Veröffentlichung

(where): Frankfurt am Main

(who): Universitätsbibliothek Johann Christian Senckenberg

(when): 2021

Creator: Chen, Min
Abele, Rupert
Tampé, Robert

DOI: 10.1074/jbc.M302757200

URN: urn:nbn:de:hebis:30:3-760516

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 14.08.2025, 10:57 AM CEST

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Associated

Chen, Min
Abele, Rupert
Tampé, Robert
Universitätsbibliothek Johann Christian Senckenberg

Time of origin

2021

Other Objects (12)

Hochschulschrift

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)

The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p

Functional non-equivalence of ATP-binding cassette signature motifs in the transporter associated with antigen processing (TAP)

Kinetics of the ATP hydrolysis cycle of the nucleotide-binding domain of Mdl1 studied by a novel site-specific labeling technique

Purification and reconstitution of the antigen transport complex TAP: a prerequisite for determination of peptide stoichiometry and ATP hydrolysis

Time‐Resolved Mn 2+ −NO and NO−NO Distance Measurements Reveal That Catalytic Asymmetry Regulates Alternating Access in an ABC Transporter **

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

Asymmetric ATP hydrolysis cycle of the heterodimeric multidrug ABC transport complex TmrAB from Thermus thermophilus

Ribosome recycling is coordinated by processive events in two asymmetric ATP sites of ABCE1

The binding specificity of OppA determines the selectivity of the oligopeptide ATP-binding cassette transporter

Hochschulschrift

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)

The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p

Functional non-equivalence of ATP-binding cassette signature motifs in the transporter associated with antigen processing (TAP)

Kinetics of the ATP hydrolysis cycle of the nucleotide-binding domain of Mdl1 studied by a novel site-specific labeling technique

Purification and reconstitution of the antigen transport complex TAP: a prerequisite for determination of peptide stoichiometry and ATP hydrolysis

Time‐Resolved Mn 2+ −NO and NO−NO Distance Measurements Reveal That Catalytic Asymmetry Regulates Alternating Access in an ABC Transporter **

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

Asymmetric ATP hydrolysis cycle of the heterodimeric multidrug ABC transport complex TmrAB from Thermus thermophilus

Ribosome recycling is coordinated by processive events in two asymmetric ATP sites of ABCE1

The binding specificity of OppA determines the selectivity of the oligopeptide ATP-binding cassette transporter

Hochschulschrift

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)

The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p

Functional non-equivalence of ATP-binding cassette signature motifs in the transporter associated with antigen processing (TAP)

Kinetics of the ATP hydrolysis cycle of the nucleotide-binding domain of Mdl1 studied by a novel site-specific labeling technique

Purification and reconstitution of the antigen transport complex TAP: a prerequisite for determination of peptide stoichiometry and ATP hydrolysis

Time‐Resolved Mn 2+ −NO and NO−NO Distance Measurements Reveal That Catalytic Asymmetry Regulates Alternating Access in an ABC Transporter **

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

Asymmetric ATP hydrolysis cycle of the heterodimeric multidrug ABC transport complex TmrAB from Thermus thermophilus

Ribosome recycling is coordinated by processive events in two asymmetric ATP sites of ABCE1

The binding specificity of OppA determines the selectivity of the oligopeptide ATP-binding cassette transporter

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Peptides induce ATP hydrolysis at both subunits of the transporter associated with antigen processing

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Other Objects (12)

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)

The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p

Functional non-equivalence of ATP-binding cassette signature motifs in the transporter associated with antigen processing (TAP)

Kinetics of the ATP hydrolysis cycle of the nucleotide-binding domain of Mdl1 studied by a novel site-specific labeling technique

Purification and reconstitution of the antigen transport complex TAP: a prerequisite for determination of peptide stoichiometry and ATP hydrolysis

Time‐Resolved Mn 2+ −NO and NO−NO Distance Measurements Reveal That Catalytic Asymmetry Regulates Alternating Access in an ABC Transporter **

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

Asymmetric ATP hydrolysis cycle of the heterodimeric multidrug ABC transport complex TmrAB from Thermus thermophilus

Ribosome recycling is coordinated by processive events in two asymmetric ATP sites of ABCE1

The binding specificity of OppA determines the selectivity of the oligopeptide ATP-binding cassette transporter

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)

The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p

Functional non-equivalence of ATP-binding cassette signature motifs in the transporter associated with antigen processing (TAP)

Kinetics of the ATP hydrolysis cycle of the nucleotide-binding domain of Mdl1 studied by a novel site-specific labeling technique

Purification and reconstitution of the antigen transport complex TAP: a prerequisite for determination of peptide stoichiometry and ATP hydrolysis

Time‐Resolved Mn 2+ −NO and NO−NO Distance Measurements Reveal That Catalytic Asymmetry Regulates Alternating Access in an ABC Transporter **

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

Asymmetric ATP hydrolysis cycle of the heterodimeric multidrug ABC transport complex TmrAB from Thermus thermophilus

Ribosome recycling is coordinated by processive events in two asymmetric ATP sites of ABCE1

The binding specificity of OppA determines the selectivity of the oligopeptide ATP-binding cassette transporter

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)

The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p

Functional non-equivalence of ATP-binding cassette signature motifs in the transporter associated with antigen processing (TAP)

Kinetics of the ATP hydrolysis cycle of the nucleotide-binding domain of Mdl1 studied by a novel site-specific labeling technique

Purification and reconstitution of the antigen transport complex TAP: a prerequisite for determination of peptide stoichiometry and ATP hydrolysis

Time‐Resolved Mn 2+ −NO and NO−NO Distance Measurements Reveal That Catalytic Asymmetry Regulates Alternating Access in an ABC Transporter **

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

Asymmetric ATP hydrolysis cycle of the heterodimeric multidrug ABC transport complex TmrAB from Thermus thermophilus

Ribosome recycling is coordinated by processive events in two asymmetric ATP sites of ABCE1

The binding specificity of OppA determines the selectivity of the oligopeptide ATP-binding cassette transporter

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