Publications by authors named "Thomas Heitkamp"

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Protein succinylome analysis identifies citrate synthase as a central regulator of osteoclast metabolic activity.
Dayoung Yu, Yue Gao, Marcin Luzarowski, Elisabeth Seebach, Thomas Heitkamp

FEBS J· July 2025

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Mechanism of ADP-Inhibited ATP Hydrolysis in Single Proton-Pumping FF-ATP Synthase Trapped in Solution.
Iván Pérez, Thomas Heitkamp, Michael Börsch

Int J Mol Sci· May 2023

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Fast ATP-Dependent Subunit Rotation in Reconstituted FF-ATP Synthase Trapped in Solution.
Thomas Heitkamp, Michael Börsch

J Phys Chem B· July 2021

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Light-Driven ATP Regeneration in Diblock/Grafted Hybrid Vesicles.
Christin Kleineberg, Christian Wölfer, Amirhossein Abbasnia, Dennis Pischel, Claudia Bednarz, Thomas Heitkamp

Chembiochem· August 2020

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Towards monitoring conformational changes of the GPCR neurotensin receptor 1 by single-molecule FRET.
Thomas Heitkamp, Reinhard Grisshammer, Michael Börsch

Proc SPIE Int Soc Opt Eng· February 2018

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Sequential bottom-up assembly of mechanically stabilized synthetic cells by microfluidics.
Marian Weiss, Johannes Patrick Frohnmayer, Lucia Theresa Benk, Barbara Haller, Jan-Willi Janiesch, Thomas Heitkamp

Nat Mater· January 2018

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Regulatory conformational changes of the ε subunit in single FRET-labeled FF-ATP synthase.
Thomas M Duncan, Monika G Düser, Thomas Heitkamp, Duncan G G McMillan, Michael Börsch

Proc SPIE Int Soc Opt Eng· February 2014

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Generation of an antibody toolbox to characterize hERG.
Georg J Hausammann, Thomas Heitkamp, Hugues Matile, Bernard Gsell, Ralf Thoma

Biochem Biophys Res Commun· February 2013

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Solution structure of the KdpFABC P-type ATPase from Escherichia coli by electron microscopic single particle analysis.
Thomas Heitkamp, Bettina Böttcher, Jörg-Christian Greie

J Struct Biol· June 2009

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K+-translocating KdpFABC P-type ATPase from Escherichia coli acts as a functional and structural dimer.
Thomas Heitkamp, René Kalinowski, Bettina Böttcher, Michael Börsch, Karlheinz Altendorf

Biochemistry· March 2008

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The transmembrane domain of subunit b of the Escherichia coli F1F(O) ATP synthase is sufficient for H(+)-translocating activity together with subunits a and c.
Jörg-Christian Greie, Thomas Heitkamp, Karlheinz Altendorf

Eur J Biochem· July 2004

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