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Revealing an outward-facing open conformational state in a CLC Cl(-)/H(+) exchange transporter

eLife, 2016-01, Vol.5

2016

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Spontaneous, intervesicular transfer rates of fluorescent, acyl chain-labeled phosphatidylcholine analogs

Biochimica et biophysica acta, 2007-03, Vol.1768 (3), p.502-508

2007

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Fluorescent, Acyl Chain-labeled Phosphatidylcholine Analogs Reveal Novel Transport Pathways across the Plasma Membrane of Yeast

The Journal of biological chemistry, 2005-12, Vol.280 (49), p.40957-40964

2005

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Substrate-driven conformational changes in ClC-ec1 observed by fluorine NMR

The EMBO journal, 2009-10, Vol.28 (20), p.3090-3102

2009

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Thinking outside the crystal: complementary approaches for examining transporter conformational change

Channels (Austin, Tex.), 2008-09, Vol.2 (5), p.373-379

2008

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Thinking outside the crystal: Complementary approaches for examining transporter mechanism

Channels (Austin, Tex.), 2008-09, Vol.2 (5), p.373-379

2008

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Monitoring Substrate-Driven Conformational Changes of ClC-ec1 by [Methyl-13C] Methionine NMR

Biophysical journal, 2012-01, Vol.102 (3), p.520a-521a

2012

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Structural Investigations of ClC-ec1, a Large Integral Membrane Protein, using Solution-State NMR and Nanodisc Technology

Biophysical journal, 2012-01, Vol.102 (3), p.520a-520a

2012

Volltextzugriff (PDF)

Revealing an outward-facing open conformational state in a CLC Cl.sup.--/H.sup.+ exchange transporter

eLife, 2016-01, Vol.5

2016

Volltextzugriff (PDF)

A Designed Inhibitor of a CLC Antiporter Blocks Function through a Unique Binding Mode

Chemistry & biology, 2012-11, Vol.19 (11), p.1460-1470

2012

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Revealing an outward-facing open conformational state in a CLC Cl(-)/H(+) exchange transporter

Spontaneous, intervesicular transfer rates of fluorescent, acyl chain-labeled phosphatidylcholine analogs

Fluorescent, Acyl Chain-labeled Phosphatidylcholine Analogs Reveal Novel Transport Pathways across the Plasma Membrane of Yeast

Substrate-driven conformational changes in ClC-ec1 observed by fluorine NMR

Thinking outside the crystal: complementary approaches for examining transporter conformational change

Thinking outside the crystal: Complementary approaches for examining transporter mechanism

Monitoring Substrate-Driven Conformational Changes of ClC-ec1 by [Methyl-13C] Methionine NMR

Structural Investigations of ClC-ec1, a Large Integral Membrane Protein, using Solution-State NMR and Nanodisc Technology

Revealing an outward-facing open conformational state in a CLC Cl.sup.--/H.sup.+ exchange transporter

A Designed Inhibitor of a CLC Antiporter Blocks Function through a Unique Binding Mode

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