Sökresultat - "protein folding"

Mechanisms of helix induction by the closed loop.

Yanagida Y; Department of Biosciences, Soka University, Tokyo, Japan., Yoshida K; Department of Bioinformatics, Soka University, Tokyo, Japan., Ohtomo M; Department of Bioinformatics, Soka University, Tokyo, Japan., Fujiwara K; Department of Biosciences, Soka University, Tokyo, Japan.; Department of Bioinformatics, Soka University, Tokyo, Japan., Ikeguchi M; Department of Biosciences, Soka University, Tokyo, Japan.; Department of Bioinformatics, Soka University, Tokyo, Japan.

Journal Article , 2025

A single buried cysteine acts as a hydrophobic stabilizer of a folding intermediate and transition state in the MATH domain of SPOP.

Pagano L; Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli', Sapienza Università di Roma, Rome, Italy.; Laboratory affiliated to Istituto Pasteur, Fondazione Cenci Bolognetti, Rome, Italy., Diop A; Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli', Sapienza Università di Roma, Rome, Italy.; Laboratory affiliated to Istituto Pasteur, Fondazione Cenci Bolognetti, Rome, Italy., Pennacchietti V; Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli', Sapienza Università di Roma, Rome, Italy.; Laboratory affiliated to Istituto Pasteur, Fondazione Cenci Bolognetti, Rome, Italy., Di Felice M; Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli', Sapienza Università di Roma, Rome, Italy.; Laboratory affiliated to Istituto Pasteur, Fondazione Cenci Bolognetti, Rome, Italy., Ventura ES; Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli', Sapienza Università di Roma, Rome, Italy.; Laboratory affiliated to Istituto Pasteur, Fondazione Cenci Bolognetti, Rome, Italy., Toso J; Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli', Sapienza Università di Roma, Rome, Italy.; Laboratory affiliated to Istituto Pasteur, Fondazione Cenci Bolognetti, Rome, Italy., Toto A; Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli', Sapienza Università di Roma, Rome, Italy.; Laboratory affiliated to Istituto Pasteur, Fondazione Cenci Bolognetti, Rome, Italy., Gianni S; Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli', Sapienza Università di Roma, Rome, Italy.; Laboratory affiliated to Istituto Pasteur, Fondazione Cenci Bolognetti, Rome, Italy.

Journal Article , 2025

Conserved structural topologies in RNase A-like and trypsin-like serine proteases: a sequence-based folding analysis.

Kabir KMA; Research Organization of Science and Technology, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu-City, Shiga, Japan., Takahashi T; Department of Bioinformatics, College of Life Sciences, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu-City, Shiga, Japan., Kikuchi T; Department of Bioinformatics, College of Life Sciences, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu-City, Shiga, Japan. tkikuchi@sk.ritsumei.ac.jp.

Journal Article , 2025

Emerging Patterns in Membrane Protein Folding Pathways.

Kim SA; School of Biological Sciences and Institute of Molecular Biology and Genetics, Seoul National University, Seoul, South Korea; email: tyyoon@snu.ac.kr., Kim HG; School of Biological Sciences and Institute of Molecular Biology and Genetics, Seoul National University, Seoul, South Korea; email: tyyoon@snu.ac.kr., Wijesinghe WCB; Department of Chemistry, Ulsan National Institute of Science and Technology, Ulsan, South Korea; email: dymin@unist.ac.kr., Min D; Department of Chemistry, Ulsan National Institute of Science and Technology, Ulsan, South Korea; email: dymin@unist.ac.kr., Yoon TY; School of Biological Sciences and Institute of Molecular Biology and Genetics, Seoul National University, Seoul, South Korea; email: tyyoon@snu.ac.kr.

Journal Article; Review , 2025

Direct comparison of the structural dynamics between spontaneous and ligand-induced folding of staphylococcal nuclease.

Mori Y; Graduate School of Science, Nagoya University, Nagoya, Japan.; Fox Chase Cancer Center, Philadelphia, Pennsylvania, USA., Mizukami T; Department of Chemistry and Biochemistry, University of North Carolina Wilmington, Wilmington, North Carolina, USA., Suzuki I; Graduate School of Science, Nagoya University, Nagoya, Japan.; School of Science, Nagoya University, Nagoya, Japan., Fukazawa S; Graduate School of Science, Nagoya University, Nagoya, Japan., Miki K; School of Science, Nagoya University, Nagoya, Japan., Roder H; Fox Chase Cancer Center, Philadelphia, Pennsylvania, USA., Maki K; Graduate School of Science, Nagoya University, Nagoya, Japan.

Journal Article; Comparative Study , 2025

The proteomic code: Novel amino acid residue pairing models "encode" protein folding and protein-protein interactions.

Hameduh T; Department of Chemistry and Biochemistry, Mendel University in Brno, Zemědělská 1665/1, CZ-613 00, Brno, Czech Republic; MendelFOLD s.r.o., Zezulova 174/3, CZ-613 00, Brno, Czech Republic., Miller AD; Department of Chemistry and Biochemistry, Mendel University in Brno, Zemědělská 1665/1, CZ-613 00, Brno, Czech Republic; MendelFOLD s.r.o., Zezulova 174/3, CZ-613 00, Brno, Czech Republic; Veterinary Research Institute, Hudcova 296/70, CZ-621 00, Brno, Czech Republic; KP Therapeutics (Europe) s.r.o., Purkyňova 649/127, CZ-612 00, Brno, Czech Republic., Heger Z; Department of Chemistry and Biochemistry, Mendel University in Brno, Zemědělská 1665/1, CZ-613 00, Brno, Czech Republic; MendelFOLD s.r.o., Zezulova 174/3, CZ-613 00, Brno, Czech Republic., Haddad Y; Department of Chemistry and Biochemistry, Mendel University in Brno, Zemědělská 1665/1, CZ-613 00, Brno, Czech Republic; MendelFOLD s.r.o., Zezulova 174/3, CZ-613 00, Brno, Czech Republic. Electronic address: yazan.haddad@mendelu.cz.

Journal Article , 2025

Studying the Protein Thermostabilities and Folding Rates by the Interaction Energy Network in Solvent.

Liao J; Institute of Biophysics, School of Physics, Huazhong University of Science and Technology, Wuhan, China., Wu M; Institute of Biophysics, School of Physics, Huazhong University of Science and Technology, Wuhan, China., Meng F; Institute of Biophysics, School of Physics, Huazhong University of Science and Technology, Wuhan, China., Chen C; Institute of Biophysics, School of Physics, Huazhong University of Science and Technology, Wuhan, China.

Journal Article , 2025

New Insights on Protein Folding and Misfolding: Histidine Behaviors.

Sun Y; School of Chemistry and Chemical Engineering, Institute of Molecular Science, Shanxi University, Taiyuan, Shanxi 030006, China., Shi H; School of Chemistry and Chemical Engineering, Institute of Molecular Science, Shanxi University, Taiyuan, Shanxi 030006, China.

Journal Article , 2025

Topological determinants in protein folding dynamics: a comparative analysis of metamorphic proteins.

Toso J; Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli', Sapienza Università di Roma, Laboratory affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, P.le Aldo Moro 5, Rome, 00185, Italy., Pennacchietti V; Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli', Sapienza Università di Roma, Laboratory affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, P.le Aldo Moro 5, Rome, 00185, Italy., Di Felice M; Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli', Sapienza Università di Roma, Laboratory affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, P.le Aldo Moro 5, Rome, 00185, Italy., Ventura ES; Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli', Sapienza Università di Roma, Laboratory affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, P.le Aldo Moro 5, Rome, 00185, Italy., Toto A; Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli', Sapienza Università di Roma, Laboratory affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, P.le Aldo Moro 5, Rome, 00185, Italy., Gianni S; Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli', Sapienza Università di Roma, Laboratory affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, P.le Aldo Moro 5, Rome, 00185, Italy. stefano.gianni@uniroma1.it.

Journal Article; Comparative Study , 2025

Benchmarking inverse folding models for antibody CDR sequence design.

Li Y; BioMap Research, Haidian District, Beijing, China., Lang Y; BioMap Research, Haidian District, Beijing, China., Xu C; BioMap Research, Haidian District, Beijing, China., Zhou Y; BioMap Research, Haidian District, Beijing, China., Pang Z; BioMap Research, Haidian District, Beijing, China., Greisen PJ; BioMap Research, Haidian District, Beijing, China.; BioMap Research, Palo Alto, California, United States of America.

Journal Article , 2025

Polyglutamine expansion induced dynamic misfolding of androgen receptor.

Heling LWHJ; Medical Systems Biophysics and Bioengineering, Division of Systems Pharmacology and Pharmacy, Leiden Academic Centre for Drug Research, Leiden University, Leiden, The Netherlands.; Laboratory for Interdisciplinary Medical Innovations, Centre for Interdisciplinary Genome Research, Leiden University, Leiden, The Netherlands., Sheikhhassani V; Medical Systems Biophysics and Bioengineering, Division of Systems Pharmacology and Pharmacy, Leiden Academic Centre for Drug Research, Leiden University, Leiden, The Netherlands.; Laboratory for Interdisciplinary Medical Innovations, Centre for Interdisciplinary Genome Research, Leiden University, Leiden, The Netherlands., Ng J; Medical Systems Biophysics and Bioengineering, Division of Systems Pharmacology and Pharmacy, Leiden Academic Centre for Drug Research, Leiden University, Leiden, The Netherlands.; Laboratory for Interdisciplinary Medical Innovations, Centre for Interdisciplinary Genome Research, Leiden University, Leiden, The Netherlands., van Vliet M; Medical Systems Biophysics and Bioengineering, Division of Systems Pharmacology and Pharmacy, Leiden Academic Centre for Drug Research, Leiden University, Leiden, The Netherlands., Jiménez-Panizo A; Department of Biochemistry and Molecular Biomedicine, Institute of Biomedicine (IBUB) of the University of Barcelona (UB), Barcelona, Spain., Alegre-Martí A; Department of Biochemistry and Molecular Biomedicine, Institute of Biomedicine (IBUB) of the University of Barcelona (UB), Barcelona, Spain., Woodard J; Department of Biomedical Engineering, University of Michigan, Ann Arbor, Michigan, USA., van Roon-Mom W; Department of Human Genetics, Leiden University Medical Center, Leiden, The Netherlands., McEwan IJ; Institute of Medical Sciences, School of Medicine, Medical Sciences and Nutrition, University of Aberdeen, Aberdeen, Scotland., Estébanez-Perpiñá E; Department of Biochemistry and Molecular Biomedicine, Institute of Biomedicine (IBUB) of the University of Barcelona (UB), Barcelona, Spain., Mashaghi A; Medical Systems Biophysics and Bioengineering, Division of Systems Pharmacology and Pharmacy, Leiden Academic Centre for Drug Research, Leiden University, Leiden, The Netherlands.; Laboratory for Interdisciplinary Medical Innovations, Centre for Interdisciplinary Genome Research, Leiden University, Leiden, The Netherlands.

Journal Article , 2025

Insights into amyloid-β misfolding: The impact of histidine tautomerism and Au(111) surfaces through MD simulations and 2DIR spectroscopy.

Parida R; Department of Chemistry, Sungkyunkwan University, Suwon 16419, Republic of Korea., Rafiq F; Department of Chemistry, Sungkyunkwan University, Suwon 16419, Republic of Korea., Chatterjee S; Department of Chemistry, Sungkyunkwan University, Suwon 16419, Republic of Korea., Salimi A; Department of Chemistry, Sungkyunkwan University, Suwon 16419, Republic of Korea., Lee JY; Department of Chemistry, Sungkyunkwan University, Suwon 16419, Republic of Korea. Electronic address: jinylee@skku.edu.

Journal Article , 2025

Enhanced secretion through type 1 secretion system by grafting a calcium-binding sequence to modify the folding of cargo proteins.

Uehara R; Department of Biotechnology, College of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, Japan., Kamiya Y; Graduate School of Life and Environmental Science, Kyoto Prefectural University, Kyoto, Japan., Maeda S; Graduate School of Life and Environmental Science, Kyoto Prefectural University, Kyoto, Japan., Okamoto K; Graduate School of Life and Environmental Science, Kyoto Prefectural University, Kyoto, Japan., Toya S; Graduate School of Life and Environmental Science, Kyoto Prefectural University, Kyoto, Japan., Chiba R; Department of Biotechnology, College of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, Japan., Amesaka H; Graduate School of Life and Environmental Science, Kyoto Prefectural University, Kyoto, Japan., Takano K; Graduate School of Life and Environmental Science, Kyoto Prefectural University, Kyoto, Japan., Matsumura H; Department of Biotechnology, College of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, Japan., Tanaka SI; Graduate School of Life and Environmental Science, Kyoto Prefectural University, Kyoto, Japan.

Journal Article , 2025

Natural Spy Chaperone Mimic: Tailored Nanochaperone with Electrostatic-Hydrophobic Synergy To Enhance Protein Folding Regulation.

Zhao S; Key Laboratory of Functional Polymer Materials of Ministry of Education, Institute of Polymer Chemistry, State Key Laboratory of Medicinal Chemical Biology, Frontiers Science Center for New Organic Matter, College of Chemistry, Nankai University, Tianjin 300071, P. R. China., Quan S; State Key Laboratory of Microbial Metabolism, School of Life Sciences and Biotechnology, Zhangjiang Institute for Advanced Study, Shanghai Jiao Tong University, Shanghai 200240, P. R. China., He W; State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai 200031, P. R. China., Xu L; Key Laboratory of Functional Polymer Materials of Ministry of Education, Institute of Polymer Chemistry, State Key Laboratory of Medicinal Chemical Biology, Frontiers Science Center for New Organic Matter, College of Chemistry, Nankai University, Tianjin 300071, P. R. China., Hu H; Key Laboratory of Functional Polymer Materials of Ministry of Education, Institute of Polymer Chemistry, State Key Laboratory of Medicinal Chemical Biology, Frontiers Science Center for New Organic Matter, College of Chemistry, Nankai University, Tianjin 300071, P. R. China., Ma Z; Key Laboratory of Functional Polymer Materials of Ministry of Education, Institute of Polymer Chemistry, State Key Laboratory of Medicinal Chemical Biology, Frontiers Science Center for New Organic Matter, College of Chemistry, Nankai University, Tianjin 300071, P. R. China., Ma R; Key Laboratory of Functional Polymer Materials of Ministry of Education, Institute of Polymer Chemistry, State Key Laboratory of Medicinal Chemical Biology, Frontiers Science Center for New Organic Matter, College of Chemistry, Nankai University, Tianjin 300071, P. R. China., Huang F; State Key Laboratory of Advanced Medical Materials and Devices, Tianjin Key Laboratory of Radiation Medicine and Molecular Nuclear Medicine, Key Laboratory of Radiopharmacokinetics for Innovative Drugs, Tianjin Institutes of Health Science, Institute of Radiation Medicine, Chinese Academy of Medical Sciences & Peking Union Medical College, Tianjin 300192, P. R. China., Shi L; Key Laboratory of Functional Polymer Materials of Ministry of Education, Institute of Polymer Chemistry, State Key Laboratory of Medicinal Chemical Biology, Frontiers Science Center for New Organic Matter, College of Chemistry, Nankai University, Tianjin 300071, P. R. China.; Haihe Laboratory of Sustainable Chemical Transformations, Tianjin 300192P. R. China.

Journal Article , 2025

In silico design of foldable lasso peptides.

Nguyen JDM; Department of Chemistry, University of Utah, Salt Lake City, Utah., da Hora GCA; Department of Chemistry, University of Utah, Salt Lake City, Utah., Mifflin MC; Department of Chemistry, University of Utah, Salt Lake City, Utah., Roberts AG; Department of Chemistry, University of Utah, Salt Lake City, Utah., Swanson JMJ; Department of Chemistry, University of Utah, Salt Lake City, Utah. Electronic address: j.swanson@utah.edu.

Journal Article , 2025

Structural Biology in the AlphaFold Era: How Far Is Artificial Intelligence from Deciphering the Protein Folding Code?

Balasco N; Institute of Molecular Biology and Pathology, National Research Council (CNR), c/o Department Chemistry, Sapienza University of Rome, 00185 Rome, Italy., Esposito L; Institute of Biostructure and Bioimaging, Department of Biomedical Sciences, National Research Council (CNR), 80131 Naples, Italy., Vitagliano L; Institute of Biostructure and Bioimaging, Department of Biomedical Sciences, National Research Council (CNR), 80131 Naples, Italy.

Journal Article; Review , 2025

DNA origami-enhanced force spectroscopy and AlphaFold structural analyses reveal the folding landscape of calcium-binding proteins.

Zhang H; School of Sensing Science and Engineering, School of Electronic Information and Electrical Engineering, Shanghai Jiao Tong University, Shanghai 200240, China.; Jason L. Choy Laboratory for Single Molecule Biophysics. Institute for Quantitative Biosciences-QB3, University of California, Berkeley, Berkeley, CA 94720, USA., Cañari-Chumpitaz C; Jason L. Choy Laboratory for Single Molecule Biophysics. Institute for Quantitative Biosciences-QB3, University of California, Berkeley, Berkeley, CA 94720, USA.; Department of Chemistry, University of California, Berkeley, Berkeley, CA 94720, USA.; Howard Hughes Medical Institute, Stanford University, Stanford, CA 94305, USA., Alexander L; Jason L. Choy Laboratory for Single Molecule Biophysics. Institute for Quantitative Biosciences-QB3, University of California, Berkeley, Berkeley, CA 94720, USA.; Department of Chemistry, University of California, Berkeley, Berkeley, CA 94720, USA.; Metagenomi Inc., Discovery, Emeryville, CA 94608, USA., Zhang H; School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai 200240, China., Fan C; School of Chemistry and Chemical Engineering, Frontiers Science Center for Transformative Molecules, National Center for Translational Medicine, Shanghai Jiao Tong University, Shanghai 200240, China.; Shanghai Key Laboratory for Nucleic Acids Chemistry and Nanomedicine, Institute of Molecular Medicine, Renji Hospital, School of Medicine, Shanghai Jiao Tong University, Shanghai 200240, China., Bustamante C; Jason L. Choy Laboratory for Single Molecule Biophysics. Institute for Quantitative Biosciences-QB3, University of California, Berkeley, Berkeley, CA 94720, USA.; Department of Chemistry, University of California, Berkeley, Berkeley, CA 94720, USA.; Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA.; Department of Physics, University of California, Berkeley, Berkeley, CA 94720, USA.; Howard Hughes Medical Institute, University of California, Berkeley, Berkeley, CA 94720, USA.; Kavli Energy Nanoscience Institute, University of California, Berkeley, Berkeley, CA 94720, USA.

Journal Article , 2025

Deglycosylation significantly affects the activity, stability and appropriate folding of recombinant Aspergillus niger α-L-rhamnosidase expressed in Pichia pastoris.

Lu Q; College of Ocean Food and Biological Engineering, Jimei University, Xiamen 361021, China., Liao H; College of Ocean Food and Biological Engineering, Jimei University, Xiamen 361021, China., Jiang Z; College of Ocean Food and Biological Engineering, Jimei University, Xiamen 361021, China; Fujian Provincial Key Laboratory of Food Microbiology and Enzyme Engineering, Xiamen 361021, China; Research Center of Food Biotechnology of Xiamen City, Xiamen 361021, China., Zhu Y; College of Ocean Food and Biological Engineering, Jimei University, Xiamen 361021, China; Fujian Provincial Key Laboratory of Food Microbiology and Enzyme Engineering, Xiamen 361021, China; Research Center of Food Biotechnology of Xiamen City, Xiamen 361021, China., Han Y; Fujian Universities Engineering Research Center of Marine Biology and Drugs, College of Geography and Oceanography, Minjiang University, Fuzhou 350108, China., Li L; College of Ocean Food and Biological Engineering, Jimei University, Xiamen 361021, China; Fujian Provincial Key Laboratory of Food Microbiology and Enzyme Engineering, Xiamen 361021, China; Research Center of Food Biotechnology of Xiamen City, Xiamen 361021, China. Electronic address: ljli@jmu.edu.cn., Ni H; College of Ocean Food and Biological Engineering, Jimei University, Xiamen 361021, China; Xiamen Ocean Vocational College, Xiamen 361102, China., Li Q; College of Ocean Food and Biological Engineering, Jimei University, Xiamen 361021, China; Fujian Provincial Key Laboratory of Food Microbiology and Enzyme Engineering, Xiamen 361021, China; Research Center of Food Biotechnology of Xiamen City, Xiamen 361021, China.

Journal Article , 2025

IgG4 and IgG1 undergo common acid-induced compaction into an alternatively folded state.

Imamura H; Department of Biological Data Science, Nagahama Institute of Bio-Science and Technology, Japan., Honda S; Biomedical Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Japan.

Journal Article , 2025

Unveiling an unexpected redox regulation of the folding, function and inhibition in the phosphotyrosine binding domain of FRS2.

Pennacchietti V; Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli', Sapienza Università di Roma, Laboratory affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, 00185 Rome, Italy., Pagano L; Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli', Sapienza Università di Roma, Laboratory affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, 00185 Rome, Italy., Di Felice M; Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli', Sapienza Università di Roma, Laboratory affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, 00185 Rome, Italy., Toso J; Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli', Sapienza Università di Roma, Laboratory affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, 00185 Rome, Italy., Bufano M; Dipartimento di Chimica e Tecnologie del Farmaco, Sapienza Università di Roma, Piazzale Aldo Moro 5, Laboratory affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, 00185 Rome, Italy., Coluccia A; Dipartimento di Chimica e Tecnologie del Farmaco, Sapienza Università di Roma, Piazzale Aldo Moro 5, Laboratory affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, 00185 Rome, Italy., Silvestri R; Dipartimento di Chimica e Tecnologie del Farmaco, Sapienza Università di Roma, Piazzale Aldo Moro 5, Laboratory affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, 00185 Rome, Italy., Capelli R; Dipartimento di Bioscienze, Università degli Studi di Milano, 20133 Milano, Italy., Camilloni C; Dipartimento di Bioscienze, Università degli Studi di Milano, 20133 Milano, Italy., Malagrinò F; Dipartimento di Medicina Clinica, Sanità Pubblica, Scienze della vita e dell'ambiente, Università dell'Aquila, Piazzale Salvatore Tommasi 1, 67010 L'Aquila-Coppito, Italy., Toto A; Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli', Sapienza Università di Roma, Laboratory affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, 00185 Rome, Italy. Electronic address: angelo.toto@uniroma1.it., Gianni S; Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli', Sapienza Università di Roma, Laboratory affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, 00185 Rome, Italy. Electronic address: stefano.gianni@uniroma1.it.

Journal Article , 2025