{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nAlthough none of the provided abstracts explicitly mention “PRH2,” they collectively offer an in‐depth view of a key adhesion‐regulatory protein—talin—and its multifaceted roles in the control of integrin activation, force transmission, and cytoskeletal linkage. Because PRH2 belongs to a family of proteins that, in some cases, share mechanistic parallels with adhesion regulators, these studies can serve as a framework for understanding how similar modular proteins may function in integrin‐mediated adhesion and signaling. In these works, talin’s N‐terminal head domain binds directly to the membrane‐proximal sequences of integrin β subunits, triggering conformational changes that switch integrins from a low‐ to a high‐affinity state. This critical “inside‐out” activation event initiates cell adhesion and is essential in diverse physiological settings such as development, immune cell trafficking, and platelet function."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nOther studies emphasize how talin not only promotes integrin activation but also functions as a mechanosensor and force buffer. Under mechanical load, talin’s rod domains undergo force-induced unfolding and refolding transitions that expose cryptic binding sites for partners such as vinculin and RIAM. These dynamic structural changes provide a means to stably link integrins to the actin cytoskeleton, thereby reinforcing focal adhesions and coordinating downstream signaling events. The precise control of these processes—via force-dependent unfolding, lipid binding, and competition between autoinhibitory and activating interactions—ensures that cells can sense and respond to their extracellular environment."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditional research has delineated the context‐specific roles of talin in various cell types. In platelets, leukocytes, endothelial cells, and muscle cells, regulated recruitment and activation of talin are essential not only for integrin “inside‐out” activation but also for subsequent “outside‐in” signaling that drives cell spreading, migration, and tissue maintenance. Post‐translational modifications—including phosphorylation and calpain‐mediated proteolysis—as well as competitive binding by regulatory proteins like kindlin, RIAM, and vinculin, fine-tune talin’s activity and localization. These studies therefore underscore how precise control over talin’s conformation and its interactions with integrins and the actin cytoskeleton is critical for sustaining adhesion dynamics and mechanotransduction in both normal and pathological states."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "14", "end_ref": "29"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn summary, while PRH2 is not directly addressed in these abstracts, the extensive characterization of talin reveals that its ability to orchestrate integrin activation, mediate force-dependent adhesion reinforcement, and integrate diverse signaling inputs is critical for numerous cellular functions. By analogy, if PRH2 shares similarities in modular architecture or regulatory interactions with talin, it too might contribute to the fine regulation of adhesion dynamics and mechanotransduction. This integrated view—spanning from molecular interactions and force sensing to cell behavior and tissue homeostasis—provides an essential context for exploring the function of adhesion‐regulated proteins like PRH2 in both physiological and disease settings.\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Kate L Wegener, Anthony W Partridge, Jaewon Han, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structural basis of integrin activation by talin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cell.2006.10.048"}], "href": "https://doi.org/10.1016/j.cell.2006.10.048"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17218263"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17218263"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Kun Ling, Renee L Doughman, Ari J Firestone, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Type I gamma phosphatidylinositol phosphate kinase targets and regulates focal adhesions."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nature (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/nature01082"}], "href": "https://doi.org/10.1038/nature01082"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12422220"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12422220"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Benjamin A Freiberg, Hannah Kupfer, William Maslanik, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Staging and resetting T cell activation in SMACs."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Immunol (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ni836"}], "href": "https://doi.org/10.1038/ni836"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12244310"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12244310"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Esen Goksoy, Yan-Qing Ma, Xiaoxia Wang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structural basis for the autoinhibition of talin in regulating integrin activation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molcel.2008.06.011"}], "href": "https://doi.org/10.1016/j.molcel.2008.06.011"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18614051"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18614051"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Guoying Jiang, Grégory Giannone, David R Critchley, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nature (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/nature01805"}], "href": "https://doi.org/10.1038/nature01805"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12867986"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12867986"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Katharina Austen, Pia Ringer, Alexander Mehlich, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Extracellular rigidity sensing by talin isoform-specific mechanical linkages."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Cell Biol (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ncb3268"}], "href": "https://doi.org/10.1038/ncb3268"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26523364"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26523364"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Mingxi Yao, Benjamin T Goult, Benjamin Klapholz, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The mechanical response of talin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ncomms11966"}], "href": "https://doi.org/10.1038/ncomms11966"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27384267"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27384267"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Marina Theodosiou, Moritz Widmaier, Ralph T Böttcher, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Kindlin-2 cooperates with talin to activate integrins and induces cell spreading by directly binding paxillin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Elife (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.7554/eLife.10130"}], "href": "https://doi.org/10.7554/eLife.10130"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26821125"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26821125"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Cai Huang, Zenon Rajfur, Nima Yousefi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Talin phosphorylation by Cdk5 regulates Smurf1-mediated talin head ubiquitylation and cell migration."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Cell Biol (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ncb1868"}], "href": "https://doi.org/10.1038/ncb1868"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19363486"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19363486"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Paul Atherton, Ben Stutchbury, De-Yao Wang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Vinculin controls talin engagement with the actomyosin machinery."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ncomms10038"}], "href": "https://doi.org/10.1038/ncomms10038"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26634421"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26634421"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Alexandre R Gingras, Neil Bate, Benjamin T Goult, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The structure of the C-terminal actin-binding domain of talin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "EMBO J (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/sj.emboj.7601965"}], "href": "https://doi.org/10.1038/sj.emboj.7601965"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18157087"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18157087"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Benjamin T Goult, Thomas Zacharchenko, Neil Bate, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M112.438119"}], "href": "https://doi.org/10.1074/jbc.M112.438119"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23389036"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23389036"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Merry Gunawan, Nandini Venkatesan, Jia Tong Loh, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The methyltransferase Ezh2 controls cell adhesion and migration through direct methylation of the extranuclear regulatory protein talin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Immunol (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ni.3125"}], "href": "https://doi.org/10.1038/ni.3125"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25751747"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25751747"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Xian Zhang, Guoying Jiang, Yunfei Cai, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Talin depletion reveals independence of initial cell spreading from integrin activation and traction."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Cell Biol (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ncb1765"}], "href": "https://doi.org/10.1038/ncb1765"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19160486"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19160486"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Pere Roca-Cusachs, Nils C Gauthier, Armando Del Rio, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Clustering of alpha(5)beta(1) integrins determines adhesion strength whereas alpha(v)beta(3) and talin enable mechanotransduction."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.0902818106"}], "href": "https://doi.org/10.1073/pnas.0902818106"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19805288"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19805288"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Brian G Petrich, Patrizia Marchese, Zaverio M Ruggeri, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Talin is required for integrin-mediated platelet function in hemostasis and thrombosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Exp Med (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1084/jem.20071800"}], "href": "https://doi.org/10.1084/jem.20071800"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18086863"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18086863"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Bernhard Nieswandt, Markus Moser, Irina Pleines, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Loss of talin1 in platelets abrogates integrin activation, platelet aggregation, and thrombus formation in vitro and in vivo."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Exp Med (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1084/jem.20071827"}], "href": "https://doi.org/10.1084/jem.20071827"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18086864"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18086864"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Craig T Lefort, Jan Rossaint, Markus Moser, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Distinct roles for talin-1 and kindlin-3 in LFA-1 extension and affinity regulation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Blood (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1182/blood-2011-08-373118"}], "href": "https://doi.org/10.1182/blood-2011-08-373118"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22431571"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22431571"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Naohide Watanabe, Laurent Bodin, Manjula Pandey, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mechanisms and consequences of agonist-induced talin recruitment to platelet integrin alphaIIbbeta3."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Biol (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1083/jcb.200803094"}], "href": "https://doi.org/10.1083/jcb.200803094"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18573917"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18573917"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Paul R Elliott, Benjamin T Goult, Petra M Kopp, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The Structure of the talin head reveals a novel extended conformation of the FERM domain."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Structure (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.str.2010.07.011"}], "href": "https://doi.org/10.1016/j.str.2010.07.011"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20947018"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20947018"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Guilherme P F Nader, Ellen J Ezratty, Gregg G Gundersen "}, {"type": "b", "children": [{"type": "t", "text": "FAK, talin and PIPKIγ regulate endocytosed integrin activation to polarize focal adhesion assembly."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Cell Biol (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ncb3333"}], "href": "https://doi.org/10.1038/ncb3333"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27043085"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27043085"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "Jose M de Pereda, Kate L Wegener, Eugenio Santelli, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structural basis for phosphatidylinositol phosphate kinase type Igamma binding to talin at focal adhesions."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M413180200"}], "href": "https://doi.org/10.1074/jbc.M413180200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15623515"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15623515"}]}, {"type": "r", "ref": 23, "children": [{"type": "t", "text": "Coert Margadant, Maaike Kreft, Dirk-Jan de Groot, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Distinct roles of talin and kindlin in regulating integrin α5β1 function and trafficking."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Curr Biol (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cub.2012.06.060"}], "href": "https://doi.org/10.1016/j.cub.2012.06.060"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22795696"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22795696"}]}, {"type": "r", "ref": 24, "children": [{"type": "t", "text": "Jenson Lim, Agnès Wiedemann, George Tzircotis, et al. "}, {"type": "b", "children": [{"type": "t", "text": "An essential role for talin during alpha(M)beta(2)-mediated phagocytosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Biol Cell (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1091/mbc.e06-09-0813"}], "href": "https://doi.org/10.1091/mbc.e06-09-0813"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17202407"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17202407"}]}, {"type": "r", "ref": 25, "children": [{"type": "t", "text": "Homaira Nawabi, Stephane Belin, Romain Cartoni, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Doublecortin-Like Kinases Promote Neuronal Survival and Induce Growth Cone Reformation via Distinct Mechanisms."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Neuron (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.neuron.2015.10.005"}], "href": "https://doi.org/10.1016/j.neuron.2015.10.005"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26526391"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26526391"}]}, {"type": "r", "ref": 26, "children": [{"type": "t", "text": "Euikyung Shin, Yutaro Kashiwagi, Toshihiko Kuriu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Doublecortin-like kinase enhances dendritic remodelling and negatively regulates synapse maturation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ncomms2443"}], "href": "https://doi.org/10.1038/ncomms2443"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23385585"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23385585"}]}, {"type": "r", "ref": 27, "children": [{"type": "t", "text": "Tadayuki Yago, Brian G Petrich, Nan Zhang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Blocking neutrophil integrin activation prevents ischemia-reperfusion injury."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Exp Med (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1084/jem.20142358"}], "href": "https://doi.org/10.1084/jem.20142358"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26169939"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26169939"}]}, {"type": "r", "ref": 28, "children": [{"type": "t", "text": "Liang Zhu, Jun Yang, Thomas Bromberger, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structure of Rap1b bound to talin reveals a pathway for triggering integrin activation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41467-017-01822-8"}], "href": "https://doi.org/10.1038/s41467-017-01822-8"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29170462"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29170462"}]}, {"type": "r", "ref": 29, "children": [{"type": "t", "text": "Thomas Bromberger, Sarah Klapproth, Ina Rohwedder, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Direct Rap1/Talin1 interaction regulates platelet and neutrophil integrin activity in mice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Blood (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1182/blood-2018-04-846766"}], "href": "https://doi.org/10.1182/blood-2018-04-846766"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30442677"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30442677"}]}]}]}