Formation of ion channels by a negatively charged analog of Gramicidin A

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Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: Online-Ressource

Language: Englisch

Bibliographic citation: In: Journal of Membrane Biology ; 31 (1977), 1. - S. 171-188. - ISSN 0022-2631. - eISSN 1432-1424

Classification: Biowissenschaften, Biologie

Event: Veröffentlichung

(where): Konstanz

(who): Bibliothek der Universität Konstanz

(when): 2007

Creator: Apell, Hans-Jürgen
Bamberg, Ernst
Alpes, Heinz
Läuger, Peter

URN: urn:nbn:de:bsz:352-opus-41677

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 25.03.2025, 1:46 PM CET

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Associated

Apell, Hans-Jürgen
Bamberg, Ernst
Alpes, Heinz
Läuger, Peter
Bibliothek der Universität Konstanz

Time of origin

2007

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Formation of ion channels by a negatively charged analog of Gramicidin A

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Other Objects (12)

How do P-Type ATPases transport ions?

Subtle mutation, far-reaching effects

Finding Na,K-ATPase II : from ﬂuxes to ion movements

Finding Na,K-ATPase : I - From Cell to Molecule

Structure function relationship in P-type ATPases : a biophysical approach

Mechanistic Principles of Ion Transport in the Na,K-ATPase

Does the sodium pump have secret levels?

Toward an Understanding of Ion Transport through the Na,K-ATPase

Kinetics of luminal proton binding to the SR Ca-ATPase

Oxonol VI as an optical indicator for membrane potentials in lipid vesicles

Do H+ ions obscure electrogenic Na+ and K+ binding in the E1 state of the Na,K-ATPase?

Kinetics of the Ca2+, H+, and Mg2+ interaction with the ion-binding sites of the SR Ca-ATPase

How do P-Type ATPases transport ions?

Subtle mutation, far-reaching effects

Finding Na,K-ATPase II : from ﬂuxes to ion movements

Finding Na,K-ATPase : I - From Cell to Molecule

Structure function relationship in P-type ATPases : a biophysical approach

Mechanistic Principles of Ion Transport in the Na,K-ATPase

Does the sodium pump have secret levels?

Toward an Understanding of Ion Transport through the Na,K-ATPase

Kinetics of luminal proton binding to the SR Ca-ATPase

Oxonol VI as an optical indicator for membrane potentials in lipid vesicles

Do H+ ions obscure electrogenic Na+ and K+ binding in the E1 state of the Na,K-ATPase?

Kinetics of the Ca2+, H+, and Mg2+ interaction with the ion-binding sites of the SR Ca-ATPase

How do P-Type ATPases transport ions?

Subtle mutation, far-reaching effects

Finding Na,K-ATPase II : from ﬂuxes to ion movements

Finding Na,K-ATPase : I - From Cell to Molecule

Structure function relationship in P-type ATPases : a biophysical approach

Mechanistic Principles of Ion Transport in the Na,K-ATPase

Does the sodium pump have secret levels?

Toward an Understanding of Ion Transport through the Na,K-ATPase

Kinetics of luminal proton binding to the SR Ca-ATPase

Oxonol VI as an optical indicator for membrane potentials in lipid vesicles

Do H+ ions obscure electrogenic Na+ and K+ binding in the E1 state of the Na,K-ATPase?

Kinetics of the Ca2+, H+, and Mg2+ interaction with the ion-binding sites of the SR Ca-ATPase

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