Author

V. M. Korkhov

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 8 Biophysics· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 10 Assay:cryo-EM· 9 Research Focus:protein structure prediction· 8 Organism:human· 4 Organism:bacteria (other)· 1 Approach:deep learning· 1 Organism:Drosophila· 1 Research Focus:drug response / drug discovery· 1

Frequent Co-Authors

C. Qi· 6 shared P. Lavriha· 6 shared B. Khanppnavar· 5 shared D. Schuster· 5 shared P. Picotti· 5 shared A. Vaithia· 3 shared V. Mehta· 3 shared E. Bayraktar· 2 shared

Activity by Year

2018-2023 · peak 5/yr

Co-Author Collaboration Network

10 top collaborators · 37 mutual co-author links

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6 shared papersBiochemistry

C. Qi

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10 papers

Recent·Most cited

Mechanism of connexin channel inhibition by mefloquine and 2-aminoethoxydiphenyl borate

P. Lavriha, Y. Han, X. Ding, C. Qi, A. Vaithia, V. M. Korkhov

The paper identifies two distinct binding sites for connexin channel inhibitors mefloquine and 2APB, showing they block channel function through different mechanisms.

bioRxiv · Dec 11, 2023 · PreprintBiochemistry

Structural basis of connexin-36 gap junction channel inhibition

X. Ding, S. Aureli, A. Vaithia, P. Lavriha, D. Schuster, B. Khanppnavar, X. Li, T. B. Blum, P. Picotti, F. L. Gervasio, V. M. Korkhov

The paper reports the cryo-EM structure of connexin-36 bound to mefloquine, revealing how small molecules inhibit gap junction channels by partially occluding the pore and altering electrostatics.

bioRxiv · Dec 9, 2023Biophysics

Structure of the human Duffy antigen receptor

S. Saha, B. Khanppnavar, J. Maharana, H. Kim, C. M. C. Carino, C. Daly, S. Houston, P. Kumari, P. N. Yadav, B. Plouffe, A. Inoue, K. Y. Chung, R. Banerjee, V. M. Korkhov, A. K. Shukla

This study determines the cryo-EM structure of the Duffy antigen receptor bound to CCL7, revealing structural features that explain its unique functional properties and lack of G protein coupling.

bioRxiv · Jul 9, 2023 · PreprintBiochemistry

Structures of wild-type and selected CMT1X mutant connexin 32 gap junction channels and hemichannels

C. Qi, P. Lavriha, E. Bayraktar, A. Vaithia, D. Schuster, M. Pannella, V. Sala, P. Picotti, M. Bortolozzi, V. M. Korkhov

The paper presents cryo-EM structures of wild-type and CMT1X mutant connexin 32 gap junction channels and hemichannels, revealing a gating helix defect in disease-associated mutants.

bioRxiv · Mar 8, 2023Biophysics

Regulatory sites of CaM-sensitive adenylyl cyclase AC8 revealed by cryo-EM and structural proteomics

B. Khanppnavar, D. Schuster, P. Lavriha, F. Uliana, M. Özel, V. Mehta, A. Leitner, P. Picotti, V. M. Korkhov

The paper determines the cryo-EM structure of bovine AC8 bound to CaM and Gs, identifies interaction sites, and infers conformational changes in the regulation mechanism.

bioRxiv · Mar 3, 2023Biochemistry

Structure of the connexin-43 gap junction channel in a putative closed state

C. Qi, S. Acosta-Gutierrez, P. Lavriha, A. Othman, D. Lopez-Pigozzi, E. Bayraktar, D. Schuster, P. Picotti, N. Zamboni, M. Bortolozzi, F. L. Gervasio, V. M. Korkhov

The paper determines the structure of a human Cx43 gap junction channel in a closed state using cryo-EM, revealing a previously unknown conformation stabilized by a small molecule.

bioRxiv · Mar 26, 2022Biochemistry

Structure of Mycobacterium tuberculosis Cya, an evolutionary ancestor of the mammalian membrane adenylyl cyclases

V. Mehta, B. Khanppnavar, D. Schuster, I. Kantarci, I. Vercellino, A. Kosturanova, T. Iype, S. Stefanic, P. Picotti, V. M. Korkhov

The paper determines the cryo-EM structure of Mycobacterium tuberculosis Cya, revealing its TM domain's role in catalytic activity regulation.

bioRxiv · Dec 1, 2021Biochemistry

Structural basis of adenylyl cyclase 9 activation

C. Qi, P. Lavriha, V. Mehta, B. Khanppnavar, I. Mohammed, Y. Li, M. Lazaratos, J. V. Schaefer, B. Dreier, A. Plueckthun, A.-N. Bondar, C. W. Dessauer, V. M. Korkhov

The paper presents cryo-EM structures of AC9 in different states to reveal activator-induced conformational changes essential for its activation.

bioRxiv · Aug 11, 2021Biochemistry

Cryo-EM structure of the Hedgehog release protein Dispatched

F. Cannac, C. Qi, J. Falschlunger, G. Hausmann, K. Basler, V. M. Korkhov

This study presents the cryo-EM structure of Drosophila Dispatched, revealing its open conformation and unique Hh-binding mode, suggesting a receptor-chaperone role in Hedgehog release.

bioRxiv · Jul 18, 2019Biochemistry

Structural basis of sterol recognition by human hedgehog receptor PTCH1

C. Qi, G. Di Minin, I. Vercellino, A. Wutz, V. M. Korkhov

This study presents a cryo-EM structure of human PTCH1 bound to a modified hedgehog ligand, revealing sterol interactions and potential translocation pathways.

bioRxiv · Dec 30, 2018Biochemistry