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

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Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: Online-Ressource

Language: Englisch

Bibliographic citation: In: Journal of biological chemistry, 281.2006, 9, S. 5694-5701

Event: Veröffentlichung

(where): Frankfurt am Main

(who): Universitätsbibliothek Johann Christian Senckenberg

(when): 2021

Creator: Does, Christiaan van der
Presenti, Chiara
Schulze, Katrin
Dinkelaker, Stephanie
Tampé, Robert

DOI: 10.1074/jbc.M511730200

URN: urn:nbn:de:hebis:30:3-762409

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 15.08.2025, 7:26 AM CEST

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Associated

Does, Christiaan van der
Presenti, Chiara
Schulze, Katrin
Dinkelaker, Stephanie
Tampé, Robert
Universitätsbibliothek Johann Christian Senckenberg

Time of origin

2021

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Hochschulschrift

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

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Mechanistic and structural studies of the MHC I peptide loading complex

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High-precision nanotools for in situ photo patterning of biomolecules in 2D and 3D

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Hochschulschrift

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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 **

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High-precision nanotools for in situ photo patterning of biomolecules in 2D and 3D

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

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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

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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 **

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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Structure and mechanism of the heterodimeric ABC translocation complexes TAP and TmrAB

Semisynthetic Viral Inhibitor for Light Control of the MHC I Peptide Loading Complex

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High-precision nanotools for in situ photo patterning of biomolecules in 2D and 3D

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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 **

Mechanistic and structural studies of the MHC I peptide loading complex

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

Structure and mechanism of the heterodimeric ABC translocation complexes TAP and TmrAB

Semisynthetic Viral Inhibitor for Light Control of the MHC I Peptide Loading Complex

Semisynthetic Viral Inhibitor for Light Control of the MHC I Peptide Loading Complex

High-precision nanotools for in situ photo patterning of biomolecules in 2D and 3D

Mechanistic and structural insights into the quality control of the MHC I antigen processing pathway

Zur Wechselwirkung von Glycophorin mit Lipidkomponenten in künstlichen Phospholipid-Doppelschichten : eine spektroskopische, elektronenmikroskopische und kalorimetrische Studie zur Lipid-Protein-Wechselwirkung

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

Proofreading of peptide—MHC complexes through dynamic multivalent interactions

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 **

Mechanistic and structural studies of the MHC I peptide loading complex

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

Structure and mechanism of the heterodimeric ABC translocation complexes TAP and TmrAB

Semisynthetic Viral Inhibitor for Light Control of the MHC I Peptide Loading Complex

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High-precision nanotools for in situ photo patterning of biomolecules in 2D and 3D

Mechanistic and structural insights into the quality control of the MHC I antigen processing pathway

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