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Valentin Borshchevskiy

Name	Valentin Borshchevskiy
Ort	Jülich (Wirkungsort) Dolgoprudny (Wirkungsort) Russland Deutschland
Geschlecht	männlich
Akademischer Grad bzw. Titel	Dr.
Beziehung	Forschungszentrum Jülich Moskovskij fiziko-techničeskij institut
Quelle	Webseite: https://www.fz-juelich.de/profile/borshchevskiy_v (Stand: 07.10.2022)
Datensatztyp	Person
GND-Nummer	126970513X
Datensatz-ID	126970513X
Beteiligt an alle anzeigen Channelrhodopsin‐2 Oligomerization in Cell Membrane Revealed by Photo‐Activated Localization Microscopy Channelrhodopsin‐2 Oligomerization in Cell Membrane Revealed by Photo‐Activated Localization Microscopy CryoRhodopsins: a comprehensive characterization of a group of microbial rhodopsins from cold environments CryoRhodopsins: a comprehensive characterization of a new clade of microbial rhodopsins from cold environments Structural insights into 3Fe–4S ferredoxins diversity in M. tuberculosis highlighted by a first redox complex with P450 Structural basis for receptor selectivity and inverse agonism in S1P5 receptors Role of Mitochondrial Protein Import in Age-Related Neurodegenerative and Cardiovascular Diseases Structure-based insights into evolution of rhodopsins Author Correction: Small-wedge synchrotron and serial XFEL datasets for Cysteinyl leukotriene GPCRs Small-wedge synchrotron and serial XFEL datasets for Cysteinyl leukotriene GPCRs Molecular mechanism of light-driven sodium pumping Small-wedge synchrotron and serial XFEL datasets for Cysteinyl leukotriene GPCRs Structural basis of ligand selectivity and disease mutations in cysteinyl leukotriene receptors Structure and mechanisms of sodium-pumping KR2 rhodopsin Structure and mechanisms of sodium-pumping KR2 rhodopsin Structure-based mechanism of cysteinyl leukotriene receptor inhibition by antiasthmatic drugs Unique structure and function of viral rhodopsins Fast iodide-SAD phasing for high-throughput membrane protein structure determination Inward H + pump xenorhodopsin: Mechanism and alternative optogenetic approach

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Valentin Borshchevskiy

Channelrhodopsin‐2 Oligomerization in Cell Membrane Revealed by Photo‐Activated Localization Microscopy

Channelrhodopsin‐2 Oligomerization in Cell Membrane Revealed by Photo‐Activated Localization Microscopy

CryoRhodopsins: a comprehensive characterization of a group of microbial rhodopsins from cold environments

CryoRhodopsins: a comprehensive characterization of a new clade of microbial rhodopsins from cold environments

Structural insights into 3Fe–4S ferredoxins diversity in M. tuberculosis highlighted by a first redox complex with P450

Structural basis for receptor selectivity and inverse agonism in S1P5 receptors

Role of Mitochondrial Protein Import in Age-Related Neurodegenerative and Cardiovascular Diseases

Structure-based insights into evolution of rhodopsins

Author Correction: Small-wedge synchrotron and serial XFEL datasets for Cysteinyl leukotriene GPCRs

Small-wedge synchrotron and serial XFEL datasets for Cysteinyl leukotriene GPCRs

Molecular mechanism of light-driven sodium pumping

Small-wedge synchrotron and serial XFEL datasets for Cysteinyl leukotriene GPCRs

Structural basis of ligand selectivity and disease mutations in cysteinyl leukotriene receptors

Structure and mechanisms of sodium-pumping KR2 rhodopsin

Structure and mechanisms of sodium-pumping KR2 rhodopsin

Structure-based mechanism of cysteinyl leukotriene receptor inhibition by antiasthmatic drugs

Unique structure and function of viral rhodopsins

Fast iodide-SAD phasing for high-throughput membrane protein structure determination

Inward H + pump xenorhodopsin: Mechanism and alternative optogenetic approach