Author

Martin Moche

Karolinska InstitutetORCID 0000-0002-4834-7076Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:bacteria (other)· 1 Research Focus:drug response / drug discovery· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Research Focus:protein structure prediction· 1 Approach:statistical model· 1 Assay:structural biology· 1

Frequent Co-Authors

Adnane AchouriD· 1 shared Åke LundkvistiD· 1 shared Anja SandströmiD· 1 shared Antonio Ginés García-SauraiD· 1 shared Benedetta Maria SalaiD· 1 shared Birgitta Henriques‐NormarkiD· 1 shared Carmen EbenwaldneriD· 1 shared Dario AkaberiiD· 1 shared

Activity by Year

2024-2025 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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Curved chords = mutual co-authorship

1 shared paperMicrobiology

Adnane AchourORCID

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Regulation of ADP-ribosyltransferase activity by ART domain dimerization in PARP15

Carmen Ebenwaldner, Antonio Ginés García-Saura, Simon Ekström, Katja Bernfur, Martin Moche, Derek T. Logan, Michael S. Cohen, Herwig Schuler

This study shows that PARP15's ADP-ribosyltransferase activity is regulated by dimerization, with dimers required for catalytic function and monomers inactive.

Nature Communications · Oct 29, 2025Peer-reviewedBiochemistry

Crystallographic and NMR studies of Streptococcus pneumonia LCP protein PsrSp indicate the importance of dynamics in four long loops for ligand specificity

Tatyana Sandalova, Benedetta Maria Sala, Martin Moche, Hans‐Gustaf Ljunggren, Evren Alici, Birgitta Henriques‐Normark, Tatiana Agback, Dmitry M. Lesovoy, Peter Agback, Adnane Achour

The paper determines the crystal structure of PsrSp and uses NMR to analyze its dynamics, showing that four long loops contribute to ligand specificity through their mobility.

Crystals · Dec 19, 2024Peer-reviewedMicrobiology

Identification of unique and potent inhibitors of SARS-CoV-2 main protease from DNA-encoded chemical libraries

Dario Akaberi, Monireh Pourghasemi Lati, Janina Krambrich, Julia Berger, Grace Neilsen, Emilia Strandback, S. Pauliina Turunen, Johan Wannberg, Hjalmar Gullberg, Martin Moche, Praveen Kumar Chinthakindi, Tomas Nyman, Stefan G. Sarafianos, Anja Sandström, Josef D. Järhult, , Johan Lennerstrand

This paper identifies potent SARS-CoV-2 main protease inhibitors from a DNA-encoded chemical library using affinity-based selection, achieving an IC50 of 30 nM for compound SLL11.

Antimicrobial Agents and Chemotherapy · Aug 28, 2024Peer-reviewedMicrobiology