{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,16]],"date-time":"2026-10-16T01:40:33Z","timestamp":1792114833865,"version":"4.4.0"},"reference-count":25,"publisher":"Oxford University Press (OUP)","license":[{"start":{"date-parts":[[2024,6,5]],"date-time":"2024-06-05T00:00:00Z","timestamp":1717545600000},"content-version":"vor","delay-in-days":156,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100010663","name":"H2020 European Research Council","doi-asserted-by":"publisher","award":["772257"],"award-info":[{"award-number":["772257"]}],"id":[{"id":"10.13039\/100010663","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001665","name":"French National Research Agency","doi-asserted-by":"publisher","award":["ANR-16-CONV-0001"],"award-info":[{"award-number":["ANR-16-CONV-0001"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Human Frontiers Science Program","award":["RGP0056\/2018"],"award-info":[{"award-number":["RGP0056\/2018"]}]},{"DOI":"10.13039\/100010663","name":"H2020 European Research Council","doi-asserted-by":"publisher","award":["772257"],"award-info":[{"award-number":["772257"]}],"id":[{"id":"10.13039\/100010663","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001665","name":"French National Research Agency","doi-asserted-by":"publisher","award":["ANR-16-CONV-0001"],"award-info":[{"award-number":["ANR-16-CONV-0001"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Human Frontiers Science Program","award":["RGP0056\/2018"],"award-info":[{"award-number":["RGP0056\/2018"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2024,6,5]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The mechanical stability of proteins is crucial for biological processes. To understand the mechanical functions of proteins, it is important to know the protein structure and mechanical properties. Protein mechanics is usually investigated through force spectroscopy experiments and simulations that probe the forces required to unfold the protein of interest. While there is a wealth of data in the literature on force spectroscopy experiments and steered molecular dynamics simulations of forced protein unfolding, this information is spread and difficult to access by non-experts. Here, we introduce MechanoProDB, a novel web-based database resource for collecting and mining data obtained from experimental and computational works. MechanoProDB provides a curated repository for a wide range of proteins, including muscle proteins, adhesion molecules and membrane proteins. The database incorporates relevant parameters that provide insights into the mechanical stability of proteins and their conformational stability such as the unfolding forces, energy landscape parameters and contour lengths of unfolding steps. Additionally, it provides intuitive annotations of the unfolding pathways of each protein, allowing users to explore the individual steps during mechanical unfolding. The user-friendly interface of MechanoProDB allows researchers to efficiently navigate, search and download data pertaining to specific protein folds or experimental conditions. Users can visualize protein structures using interactive tools integrated within the database, such as Mol*, and plot available data through integrated plotting tools. To ensure data quality and reliability, we have carefully manually verified and curated the data currently available on MechanoProDB. Furthermore, the database also features an interface that enables users to contribute new data and annotations, promoting community-driven comprehensiveness. The freely available MechanoProDB aims to streamline and accelerate research in the field of mechanobiology and biophysics by offering a unique platform for data sharing and analysis. MechanoProDB is freely available at https:\/\/mechanoprodb.ibdm.univ-amu.fr.<\/jats:p>","DOI":"10.1093\/database\/baae047","type":"journal-article","created":{"date-parts":[[2024,5,17]],"date-time":"2024-05-17T10:31:29Z","timestamp":1715941889000},"source":"Crossref","is-referenced-by-count":3,"title":["MechanoProDB: a web-based database for exploring the mechanical properties of proteins"],"prefix":"10.1093","volume":"2024","author":[{"ORCID":"https:\/\/orcid.org\/0009-0002-8268-5826","authenticated-orcid":false,"given":"Ismahene","family":"Mesbah","sequence":"first","affiliation":[{"name":"Aix Marseille Univ, INSERM, DyNaMo, Turing Center of Living Systems (CENTURI) , Marseille 13009, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2457-7504","authenticated-orcid":false,"given":"Bianca","family":"Habermann","sequence":"additional","affiliation":[{"name":"Aix Marseille Univ, CNRS, IBDM UMR7288, Turing Center of Living Systems (CENTURI) , Marseille 13009, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7757-8340","authenticated-orcid":false,"given":"Felix","family":"Rico","sequence":"additional","affiliation":[{"name":"Aix Marseille Univ, INSERM, DyNaMo, Turing Center of Living Systems (CENTURI) , Marseille 13009, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2024,6,5]]},"reference":[{"key":"2024062912233618000_R1","doi-asserted-by":"crossref","first-page":"1109","DOI":"10.1126\/science.276.5315.1109","article-title":"Reversible unfolding of individual titin immunoglobulin domains by AFM","volume":"276","author":"Rief","year":"1997","journal-title":"Science"},{"key":"2024062912233618000_R2","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/j.neuron.2010.03.028","article-title":"Structural determinants of Cadherin-23 function in hearing and deafness","volume":"66","author":"Sotomayor","year":"2010","journal-title":"Neuron"},{"key":"2024062912233618000_R3","doi-asserted-by":"crossref","first-page":"45865","DOI":"10.1074\/jbc.M404103200","article-title":"Chemistry on a single protein, vascular cell adhesion Molecule-1, during forced unfolding","volume":"279","author":"Bhasin","year":"2004","journal-title":"J. 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