Structural and functional fingerprint of the mitochondrial ATP-binding cassette transporter Mdl1 from Saccharomyces cerevisiae

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Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: Online-Ressource

Language: Englisch

Bibliographic citation: In: Journal of biological chemistry, 282.2007, 6, S. 3951-3961

Event: Veröffentlichung

(where): Frankfurt am Main

(who): Universitätsbibliothek Johann Christian Senckenberg

(when): 2021

Creator: Hofacker, Matthias
Gompf, Simone
Zutz, Ariane
Presenti, Chiara
Haase, Winfried
Does, Christiaan van der
Model, Kirstin
Tampé, Robert

DOI: 10.1074/jbc.M609899200

URN: urn:nbn:de:hebis:30:3-763074

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 14.08.2025, 10:57 AM CEST

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Associated

Hofacker, Matthias
Gompf, Simone
Zutz, Ariane
Presenti, Chiara
Haase, Winfried
Does, Christiaan van der
Model, Kirstin
Tampé, Robert
Universitätsbibliothek Johann Christian Senckenberg

Time of origin

2021

Other Objects (12)

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

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

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

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)

Structural organization of essential iron-sulfur clusters in the evolutionarily highly conserved ATP-binding cassette protein ABCE1

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

Cadmium transport by mammalian ATP-binding cassette transporters

Evolutionary relationships of ATP-Binding Cassette (ABC) uptake porters

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

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

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

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

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)

Structural organization of essential iron-sulfur clusters in the evolutionarily highly conserved ATP-binding cassette protein ABCE1

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

Cadmium transport by mammalian ATP-binding cassette transporters

Evolutionary relationships of ATP-Binding Cassette (ABC) uptake porters

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

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

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

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

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)

Structural organization of essential iron-sulfur clusters in the evolutionarily highly conserved ATP-binding cassette protein ABCE1

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

Cadmium transport by mammalian ATP-binding cassette transporters

Evolutionary relationships of ATP-Binding Cassette (ABC) uptake porters

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

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Structural and functional fingerprint of the mitochondrial ATP-binding cassette transporter Mdl1 from Saccharomyces cerevisiae

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Other Objects (12)

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

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

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

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)

Structural organization of essential iron-sulfur clusters in the evolutionarily highly conserved ATP-binding cassette protein ABCE1

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

Cadmium transport by mammalian ATP-binding cassette transporters

Evolutionary relationships of ATP-Binding Cassette (ABC) uptake porters

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

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

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

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

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)

Structural organization of essential iron-sulfur clusters in the evolutionarily highly conserved ATP-binding cassette protein ABCE1

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

Cadmium transport by mammalian ATP-binding cassette transporters

Evolutionary relationships of ATP-Binding Cassette (ABC) uptake porters

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

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

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

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

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)

Structural organization of essential iron-sulfur clusters in the evolutionarily highly conserved ATP-binding cassette protein ABCE1

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

Cadmium transport by mammalian ATP-binding cassette transporters

Evolutionary relationships of ATP-Binding Cassette (ABC) uptake porters

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

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