Author

P. Lavriha

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· 4 Biophysics· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 6 Assay:cryo-EM· 5 Research Focus:protein structure prediction· 4 Organism:human· 2 Approach:deep learning· 1 Research Focus:drug response / drug discovery· 1 Approach:mechanistic / dynamical model· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

V. M. Korkhov· 6 shared C. Qi· 4 shared D. Schuster· 4 shared P. Picotti· 4 shared A. Vaithia· 3 shared B. Khanppnavar· 3 shared E. Bayraktar· 2 shared F. L. Gervasio· 2 shared

Activity by Year

2021-2023 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 39 mutual co-author links

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6 shared papersBiochemistry

V. M. Korkhov

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6 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

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

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