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A.V. Kiselev

Researcher at Russian Academy of Sciences

Publications -  5
Citations -  564

A.V. Kiselev is an academic researcher from Russian Academy of Sciences. The author has contributed to research in topics: Bacteriorhodopsin & Thermolysin. The author has an hindex of 5, co-authored 5 publications receiving 561 citations. Previous affiliations of A.V. Kiselev include Laboratory of Molecular Biology.

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The structural basis of the functioning of bacteriorhodopsin: an overview.

TL;DR: The present paper is a summing up of the studies, begun in 1976, that have resulted in the complete study of bacteriorhodopsin, and gives the first indications of how the molecule is packed in the membrane.
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Recent findings in the structure—functional characteristics of bacteriorhodopsin

TL;DR: This study has been made to give a fuller chemical description of bacteriorhodopsin, including its native structure localized within purple membrane and to obtain independent data confirming and elaborating Henderson and Unwin’s model.
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Products of limited proteolysis of bacteriorhodopsin generate a membrane potential

TL;DR: The experiments revealed that the products of hydrolysis of bacteriorhodopsin that retain the AsTO,, max are still competent in generating a transmembrane electric potential difference if illuminated with continuous light or with a flash inducing a single bacteriorodopsin turnover.
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The antigenic structure and topography of bacteriorhodopsin in purple membranes as determined by interaction with monoclonal antibodies

TL;DR: The spatial organization and the antigenic structure of the bacteriorhodopsin molecule in the purple membrane were studied by immunochemical techniques and the structure of antigenic determinants was revealed by the interaction of monoclonal antibodies.
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The water‐exposed C‐terminal sequence of bacteriorhodopsin does not affect H+ pumping

TL;DR: It is concluded that a decrease in the light‐induced pH response of the C‐tail‐deprived bacteriorhodopsin is caused by the aggregation of purple sheets rather than by a special role of theC‐terminal sequence in H+ pumping.