Publications

† co-first authors. *(co-)corrisponding authors. PL and trainees from the lab are in bold. 

  • Domna G. Kotsifaki,∗ Viet Giang Truong, Mirco Dindo, Paola Laurino, Sile Nic Chormaic∗. Hybrid Metamaterial Optical Tweezers for Dielectric Particles and Biomolecules Discrimination. Submitted. arXiv 2024 https://arxiv.org/abs/2402.12878

  • Weronika Jasinska†, Mirco Dindo†, Sandra M. Correa, Adrian W.R. Serohijos, Paola Laurino*, Yariv Brotman*, Shimon Bershtein* Non-consecutive enzyme interactions within TCA cycle supramolecular assembly regulate carbon-nitrogen metabolism. BioRxiv 2023 https://www.biorxiv.org/content/10.1101/2023.11.01.565101v1

  • Muthahari, A. Y.; Aditama, R.; Providaki, M.; Tsirigotaki, A.; Sarafoglou, C.; Xu, R.;  Krishnamurthy, S.; Hertadi, R.; Kokkinidis, M.; Hui, C.; Laurino, P.; Pozidis, C.*; Gouridis, G* Thermodynamic principles govern evolutionary tradeoffs by regulating allostery. Submitted 2023

  • Ochiai, Y.; Clifton, B. E.; Le Coz, M.; Terenzio, M.; Laurino, P.* SUPREM: an engineered non-site-specific m6A RNA methyltransferase with highly improved efficiency. BioRxiv 2023 https://www.biorxiv.org/content/10.1101/2023.08.23.554385v1 

  • ​Clifton, B. E.*; Alcolombri, U.; Jackson, C.; Laurino, P.* Ultrahigh-affinity transporters of a ubiquitous marine bacterium point missing links in the oceanic carbon cicle. BioRxiv, 2023 https://www.biorxiv.org/content/10.1101/2023.02.16.528805v1

2024​

19. Dindo, M.†; Bevilacqua, A.†; Soligo, G.; Calabrese, V.; Monti, A.; Shen, Q. A.; Rosti, M. Laurino, P.* Chemotatic interactions drive migration of membraneless active droplets. Journal of American Chemical Society 2024 Just accepted https://pubs.acs.org/doi/10.1021/jacs.4c02823​

18. Kozome, D.;  Sljoka, A.; Laurino, P.* Beyond the active site: The addition of a remote loop reveals a new complex biological function for chitinase enzymes Nature Comm. 2024,  15, 3227 https://rdcu.be/dELQk

2023

17. Gade, M.; Gardner, J.; Jain, P.; Laurino, P.* Nucleotide-driven specifisity of DNA Methyltransfersase ChemBioChem, 2023  24,  e2023000 https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cbic.202300094

Paola was interviewed in Nature Catalysis to discuss the Roz Inclusivity project: "Helping Hands"

2022

16. Dindo, M.; Bevilacqua, A.; Laurino, P.* Enzymes and liquid-liquid phase separation: a new era for the regulation of enzymatic activity. Review, 2022, SEIBUTSU BUTSURI Vol. 63 No. 1（通巻365号）https://www.biophys.jp/journal/journal_dl.php?fnm=63-1

15. Toledo-Patiño, S.; Pascarelli, S.; Uechi, G.; Laurino, P.* Insertions and deletions mediated functional divergence of Rossmann fold enzymes. PNAS, 2022, 119, 48, e2207965119  https://www.pnas.org/doi/10.1073/pnas.2207965119

 

14. Jayaraman, V. †; Toledo-Patiño, S.†; Noda-García, L.*; Laurino, P.* Mechanisms of Protein evolution  Protein Science, 2022, 31, e4362. https://onlinelibrary.wiley.com/doi/10.1002/pro.4362

13. Dindo, M.; Pascarelli, S.; Chiasserini, D.; Grotelli, S.; Constantini, C.; Uechi, G.; Giardina, G.*; Laurino, P.*; Cellini B.* Structural dynamics shape the fitness window of alanine:glyoxylate aminotransferase. Protein Science 2022, 31, e4303. https://onlinelibrary.wiley.com/doi/10.1002/pro.4303

12. Pascarelli, S.; Laurino, P.* Inter-paralog aminoacid inversion events in large phylogenies of duplicated proteins  Plos Comp Biol 2022, 18, 4, e1010016. https://doi.org/10.1371/journal.pcbi.1010016

11. Clifton, B. E.; Kozome, D.; Laurino. P.* Efficient exploration of sequence space by sequence-guided protein engineering and design ACS Biochemistry, 2023, 62, 2, 210-220 https://pubs.acs.org/doi/10.1021/acs.biochem.1c00757

 

2021

10. Gade, M. H.; Lynn Tan, L.; Damry, A. M.; Sandhu, M.; Brock, J. S.; Delanay, A.; Villar-Briones, A.; Jackson, C. J.*; Laurino P.* Substrate dynamics contributes to enzymatic specificity in human and bacterial methionine adenosyltransferases. JACS Au 2021, 1, 12, 2349-2360  https://pubs.acs.org/doi/10.1021/jacsau.1c00464

9. Clifton, B. E.; Fariz, M. A.; Uechi, G.; Laurino, P.* Evolutionary repair reveals an unexpected role of the tRNA modification m1G37 in aminoacylation. Nucleic Acid Res. 2021, 49, 21, 12467-12485  https://doi.org/10.1093/nar/gkab1067

8. Testa A.†; Dindo, M.†; Rebane, A.; Nasouri, B.; Style, R.; Golestanian, R.; Dufresne, E.*; Laurino, P.* Sustained Enzymatic activity and Flow in Crowded Protein Droplets  Nat. Comm. 2021, 12, 6293 https://rdcu.be/cAzZP

7. Chouhan, B. P. S.; Gade, M.; Martinez, D.; Toledo-Patino S.; Laurino P.* Implications of divergence of Methionine AdenosylTransferase in archea. FebsOpenBio 2022, 12,  130-145  https://febs.onlinelibrary.wiley.com/doi/10.1002/2211-5463.13312

6. Laurino, P.* & Tokuriki N.* Dan Salah Tawfik (1955-2021). Nat. Chem. Biol. 2021, 17, 930.  https://www.nature.com/articles/s41589-021-00864-w

5. Pascarelli, S.; Merzhakupova, D.; Uechi, G.; Laurino P.* Single EGF mutants unravel the mechanism for stabilization of Epidermal Growth Factor Receptor (EGFR) system. JBC. 2021, 297, 100872. https://www.jbc.org/article/S0021-9258(21)00672-4/fulltext

 

2020

4. Danielson, E.*; Dindo, M.; Porkovich, A. J.; Kumar, P.; Wang, Z.; Jain, P.; Mete, T.; Ziadi, Z.; Raghavendra, K.; Laurino, P.; Sowwan, M. Non-Enzymatic and Highly Sensitive Lactose Detection Utilizing Graphene Field-Effect Transistors. Biosensors and Bioelectronics. 2020, 165, 112419 https://doi.org/10.1016/j.bios.2020.112419

2019

3. Dindo, M.; Grottelli, S.; Annunziato, G.; Giardina, G.; Pieroni, M.; Pampalone, G.; Faccini, A.,;Cutruzzola, F.; Laurino, P.; Costantino, G.; Cellini, B.  Cycloserine Enantiomers Are Reversible Inhibitors of Human Alanine:Glyoxylate Aminotransferase: Implications for Primary Hyperoxaluria Type 1. Biochem J, 2019, 476, 3751-3768. doi:10.1042/BCJ20190507

​2. Chouhan, B. P. S.; Maimaiti, S.; Gade, M.; Laurino P.* Rossmann-fold Methyltransferases: taking a 'beta-turn' around their cofactor S-Adenosylmethionine. Future of Biochemistry special Issue of ACS Biochemistry, 2019, 58, 166-170.  https://pubs.acs.org/doi/10.1021/acs.biochem.8b00994 

 

2017

1. Laurino P., Tawfik D. S. Spontaneous Emergence of S-Adenosylmethionine and the Evolution of Methylation. Angew Chem Int Ed Engl. 2017, 56, 343-345. https://onlinelibrary.wiley.com/doi/10.1002/anie.201609615 This article has been recommended in F1000Prime as being of special significance in its field.

2016 or earlier

  • Goldenzweig, A.; Goldsmith, M.; Hill, S. E.; Gertman, O.; Laurino, P.; Ashani, Y.; Dym, O.; Unger, T.; Albeck, S.; Prilusky, J.; Lieberman, R. L.; Aharoni, A.; Silman, I.; Sussman, J. L.; Tawfik, D. S.; Fleishman S. J. "Automated computational design of human enzymes for high bacterial expression and stability". Mol Cell 2016, 63, 337-346.

  • Laurino, P.; Rockah-Shmuel, L.; Tawfik D. S. “Engineering and directed evolution of DNA methyltransferases” Adv Exp Med Biol 2016, 945, 491-509

  • Laurino, P.; Tóth-Petróczy, A.; Meana-Pañeda R.; Lin W.; Truhlar D. G.; Tawfik, D. S. “An ancient fingerprint of coevolution of the Rossmann fold and adenosine cofactors”. PLoS Biology 2016, 3, e1002396.

  • Alcolombri,U.; Laurino, P.; Lara-Astiaso, P.; Vardi, A.; Tawfik D. S. “DddD is a CoA-Transferase/Lyase Producing Dimethylsulfide in the Marine Environment” Biochemistry 2014, 34, 5473–5475. This article has been chosen to be highlighted on the journal’s home page.

  • Fumagalli, L.; Pallavicini, M.; Budresi, R.; Bolchi, C.; Canovi, M.; Chiodini, G.; Gobbi, M.; Laurino, P.; Micucci, M.; Straniero, V.; Valoti, E.; “6-Methoxy-7-benzofuranoxy and 6-Methoxy-7-indolyloxy Analogues of 2-[2-(2,6-Dimethoxyphenoxy)ethyl]aminomethyl-1,4-benzodioxane (WB4101):1 Discovery of a Potent and Selective α1D-Adrenoceptor Antagonist” J. Med. Chem. 2013, 16, 6402–6412.

  • Azzouz, N.; Kamena, F.; Laurino, P.; Kikkeri, R.; Mercier, C.; Cesbron-Delauw, M-F.; Dubremetz, J-F.; De Cola, L.; Seeberger, P. H. “Toxoplasma gondii secretory proteins bind to sulfated heparin structures.” Glycobiol., 2013, 1, 106–120.

  • Suzuki, Y; Laurino, P.; McQuade D. T.; Seeberger P. H. “A Capture and Release Catalytic Flow System”, Helv. Chim. Acta 2012, 12, 2578–2588.

  • Laurino, P.; Hernandez, H.; Bräuer, J.; Grützmacher, H.; Tauer, K.; Seeberger, P. H. “Snowballing Radical Generation Leads to Ultrahigh Molecular Weight Polymers” Macromol. Rapid Commun. 2012, 20, 1770–1774.

  • Laurino, P.; Kikkeri, R.; Seeberger, P. H. “Continuous-flow reactor–based synthesis of carbohydrate and dihydrolipoic acid–capped quantum dots” Nat. Prot. 2011, 6, 1209–1220.

  • Laurino, P.; Kikkeri, R.; Azzouz, N.; Seeberger, P. H. “Detection of Bacteria Using Glyco-Dendronized Polylysine Prepared by Continuous Flow Photofunctionalization” Nano Lett., 2011, 11, 73–78.

  • Kikkeri R.; Hong, S. Y.; Grünstein, D.; Laurino, P.; Seeberger, P. H. “Carbohydrate-based Nanoscience: Metallo-glycodendrimers and Quantum Dots as Multivalent Probes“ Beilstein Bozen Symposium "Functional Nanoscience" May 17th–21st, 2010.

  • Christina, D.; Laurino, P.; Azzouz, N.; Seeberger, P. H. “Accelerated Continuous Flow RAFT polymerization” Macromol. 2010, 43, 10311–10314.

  • Bernardes, G. J. L.; Kikkeri, R.; Maglinao, M.; Laurino, P.; Collot, M.; Hong, S. Y.; Lepenies, B.; Seeberger, P. H. “Design, synthesis and biological evaluation of carbohydrate functionalized cyclodextrins and liposomes for hepatocyte-specific targeting” Org. Biomol. Chem. 2010, 21, 4987–4996.

  • Kikkeri, R.; Laurino, P., Odedra, A.; Seeberger, P. H. “Synthesis of carbohydrate-functionalized quantum dots in microreactors”. Angew. Chem. Int. Ed. Engl. 2010, 49, 2054–2057.

  • Laurino, P.; Odedra, A.; Mak, X. Y.; Gustafsson, T.; Geyer, K.; Seeberger, P. H. “Microfluidic devices for organic processes”. Chemical Reactions and Processes under Flow condition (RSC publishing 2010).

  • Mak, X. Y.; Laurino, P.; Seeberger, P. H. “Asymmetric reactions in continuous flow”. Beilstein J. Org. Chem. 2009, 5, 1–11.

  • Mak, X. Y.; Laurino, P.; Seeberger, P. H. “Synthesis of pharmaceutical and bio-active compounds in microreactors” Chemistry Today 2009, 27, 15–18.

  • Kikkeri, R.; Lepenies, B.; Adibekian, A.; Laurino, P.; Seeberger P. H. “In vitro imaging and in vivo liver targeting with carbohydrate capped quantum dots”. J. Am. Chem. Soc. 2009, 131, 2110–2112.