Cross-reactivity of two human IL-6 family cytokines OSM and LIF explored by protein-protein docking and molecular dynamics simulation
Oncostatin M (OSM) and leukemia inhibitory factor (LIF) are two important pro-inflammatory cytokines of the interleukin-6 (IL-6) family. The two cytokines mediated signaling was recently found to be closely associated with cancer and chronic inflammation, which represent promising therapeutic target...
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| Published in: | Biochimica et biophysica acta. General subjects Vol. 1865; no. 7; p. 129907 |
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| Format: | Journal Article |
| Language: | English |
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01.07.2021
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| ISSN: | 0304-4165, 1872-8006, 1872-8006 |
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| Abstract | Oncostatin M (OSM) and leukemia inhibitory factor (LIF) are two important pro-inflammatory cytokines of the interleukin-6 (IL-6) family. The two cytokines mediated signaling was recently found to be closely associated with cancer and chronic inflammation, which represent promising therapeutic targets for the treatment of many solid tumors and inflammatory disease. As the most closely related members, cross-reactivity of them may result in undesired activation of off-target cells, leading to toxicity or lack of efficacy of the therapeutic effects. However, the mechanism of the cross-reactivity of OSM and LIF is not well understood.
In this work, protein-protein docking, molecular dynamics (MD) simulations with explicit solvent and post endpoints binding free energy (BFE) analysis were carried out to further understand the structural and energetic principles of interactions between the two cytokines and the shared receptor LIFR.
For the first time, the simulation given a computational model of OSM-LIFR interaction, and provided significant insights into the mechanism of OSM and LIF cross-react with LIFR. The identified common features shared by OSM and LIF bind to LIFR involving 10 “conserved” residues (90% similarity) distributed at the binding site III comprised of AB loop, BC loop and D helix. In addition, 11 shared residues were identified in LIFR contribute 77.85% and 84.63% energies for OSM and LIF binding, which play a critical role in the formation of the two cytokine-receptor complexes. Moreover, the “nonconserved” residues at the same position of cytokines such as Asp41 in OSM and Pro51 in LIF as well as the three residues (Glu338, Asn201 and Glu260) in LIFR were also discovered.
These important information may facilitate the rational design of novel chemical or biological agents with less toxicity and improved efficacy.
•A computational model of OSM-LIFR interaction was constructed for the first time.•The mechanism of OSM and LIF cross-react with LIFR were provided from per-residues interaction energy calculations.•The “conserved” and “nonconserved” residues at the same position of the two cytokines’ binding interface were discovered. |
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| AbstractList | Oncostatin M (OSM) and leukemia inhibitory factor (LIF) are two important pro-inflammatory cytokines of the interleukin-6 (IL-6) family. The two cytokines mediated signaling was recently found to be closely associated with cancer and chronic inflammation, which represent promising therapeutic targets for the treatment of many solid tumors and inflammatory disease. As the most closely related members, cross-reactivity of them may result in undesired activation of off-target cells, leading to toxicity or lack of efficacy of the therapeutic effects. However, the mechanism of the cross-reactivity of OSM and LIF is not well understood.
In this work, protein-protein docking, molecular dynamics (MD) simulations with explicit solvent and post endpoints binding free energy (BFE) analysis were carried out to further understand the structural and energetic principles of interactions between the two cytokines and the shared receptor LIFR.
For the first time, the simulation given a computational model of OSM-LIFR interaction, and provided significant insights into the mechanism of OSM and LIF cross-react with LIFR. The identified common features shared by OSM and LIF bind to LIFR involving 10 "conserved" residues (90% similarity) distributed at the binding site III comprised of AB loop, BC loop and D helix. In addition, 11 shared residues were identified in LIFR contribute 77.85% and 84.63% energies for OSM and LIF binding, which play a critical role in the formation of the two cytokine-receptor complexes. Moreover, the "nonconserved" residues at the same position of cytokines such as Asp41 in OSM and Pro51 in LIF as well as the three residues (Glu338, Asn201 and Glu260) in LIFR were also discovered.
These important information may facilitate the rational design of novel chemical or biological agents with less toxicity and improved efficacy. Oncostatin M (OSM) and leukemia inhibitory factor (LIF) are two important pro-inflammatory cytokines of the interleukin-6 (IL-6) family. The two cytokines mediated signaling was recently found to be closely associated with cancer and chronic inflammation, which represent promising therapeutic targets for the treatment of many solid tumors and inflammatory disease. As the most closely related members, cross-reactivity of them may result in undesired activation of off-target cells, leading to toxicity or lack of efficacy of the therapeutic effects. However, the mechanism of the cross-reactivity of OSM and LIF is not well understood.BACKGROUNDOncostatin M (OSM) and leukemia inhibitory factor (LIF) are two important pro-inflammatory cytokines of the interleukin-6 (IL-6) family. The two cytokines mediated signaling was recently found to be closely associated with cancer and chronic inflammation, which represent promising therapeutic targets for the treatment of many solid tumors and inflammatory disease. As the most closely related members, cross-reactivity of them may result in undesired activation of off-target cells, leading to toxicity or lack of efficacy of the therapeutic effects. However, the mechanism of the cross-reactivity of OSM and LIF is not well understood.In this work, protein-protein docking, molecular dynamics (MD) simulations with explicit solvent and post endpoints binding free energy (BFE) analysis were carried out to further understand the structural and energetic principles of interactions between the two cytokines and the shared receptor LIFR.METHODSIn this work, protein-protein docking, molecular dynamics (MD) simulations with explicit solvent and post endpoints binding free energy (BFE) analysis were carried out to further understand the structural and energetic principles of interactions between the two cytokines and the shared receptor LIFR.For the first time, the simulation given a computational model of OSM-LIFR interaction, and provided significant insights into the mechanism of OSM and LIF cross-react with LIFR. The identified common features shared by OSM and LIF bind to LIFR involving 10 "conserved" residues (90% similarity) distributed at the binding site III comprised of AB loop, BC loop and D helix. In addition, 11 shared residues were identified in LIFR contribute 77.85% and 84.63% energies for OSM and LIF binding, which play a critical role in the formation of the two cytokine-receptor complexes. Moreover, the "nonconserved" residues at the same position of cytokines such as Asp41 in OSM and Pro51 in LIF as well as the three residues (Glu338, Asn201 and Glu260) in LIFR were also discovered.RESULTSFor the first time, the simulation given a computational model of OSM-LIFR interaction, and provided significant insights into the mechanism of OSM and LIF cross-react with LIFR. The identified common features shared by OSM and LIF bind to LIFR involving 10 "conserved" residues (90% similarity) distributed at the binding site III comprised of AB loop, BC loop and D helix. In addition, 11 shared residues were identified in LIFR contribute 77.85% and 84.63% energies for OSM and LIF binding, which play a critical role in the formation of the two cytokine-receptor complexes. Moreover, the "nonconserved" residues at the same position of cytokines such as Asp41 in OSM and Pro51 in LIF as well as the three residues (Glu338, Asn201 and Glu260) in LIFR were also discovered.These important information may facilitate the rational design of novel chemical or biological agents with less toxicity and improved efficacy.CONCLUSIONSThese important information may facilitate the rational design of novel chemical or biological agents with less toxicity and improved efficacy. Oncostatin M (OSM) and leukemia inhibitory factor (LIF) are two important pro-inflammatory cytokines of the interleukin-6 (IL-6) family. The two cytokines mediated signaling was recently found to be closely associated with cancer and chronic inflammation, which represent promising therapeutic targets for the treatment of many solid tumors and inflammatory disease. As the most closely related members, cross-reactivity of them may result in undesired activation of off-target cells, leading to toxicity or lack of efficacy of the therapeutic effects. However, the mechanism of the cross-reactivity of OSM and LIF is not well understood.In this work, protein-protein docking, molecular dynamics (MD) simulations with explicit solvent and post endpoints binding free energy (BFE) analysis were carried out to further understand the structural and energetic principles of interactions between the two cytokines and the shared receptor LIFR.For the first time, the simulation given a computational model of OSM-LIFR interaction, and provided significant insights into the mechanism of OSM and LIF cross-react with LIFR. The identified common features shared by OSM and LIF bind to LIFR involving 10 “conserved” residues (90% similarity) distributed at the binding site III comprised of AB loop, BC loop and D helix. In addition, 11 shared residues were identified in LIFR contribute 77.85% and 84.63% energies for OSM and LIF binding, which play a critical role in the formation of the two cytokine-receptor complexes. Moreover, the “nonconserved” residues at the same position of cytokines such as Asp41 in OSM and Pro51 in LIF as well as the three residues (Glu338, Asn201 and Glu260) in LIFR were also discovered.These important information may facilitate the rational design of novel chemical or biological agents with less toxicity and improved efficacy. Oncostatin M (OSM) and leukemia inhibitory factor (LIF) are two important pro-inflammatory cytokines of the interleukin-6 (IL-6) family. The two cytokines mediated signaling was recently found to be closely associated with cancer and chronic inflammation, which represent promising therapeutic targets for the treatment of many solid tumors and inflammatory disease. As the most closely related members, cross-reactivity of them may result in undesired activation of off-target cells, leading to toxicity or lack of efficacy of the therapeutic effects. However, the mechanism of the cross-reactivity of OSM and LIF is not well understood. In this work, protein-protein docking, molecular dynamics (MD) simulations with explicit solvent and post endpoints binding free energy (BFE) analysis were carried out to further understand the structural and energetic principles of interactions between the two cytokines and the shared receptor LIFR. For the first time, the simulation given a computational model of OSM-LIFR interaction, and provided significant insights into the mechanism of OSM and LIF cross-react with LIFR. The identified common features shared by OSM and LIF bind to LIFR involving 10 “conserved” residues (90% similarity) distributed at the binding site III comprised of AB loop, BC loop and D helix. In addition, 11 shared residues were identified in LIFR contribute 77.85% and 84.63% energies for OSM and LIF binding, which play a critical role in the formation of the two cytokine-receptor complexes. Moreover, the “nonconserved” residues at the same position of cytokines such as Asp41 in OSM and Pro51 in LIF as well as the three residues (Glu338, Asn201 and Glu260) in LIFR were also discovered. These important information may facilitate the rational design of novel chemical or biological agents with less toxicity and improved efficacy. •A computational model of OSM-LIFR interaction was constructed for the first time.•The mechanism of OSM and LIF cross-react with LIFR were provided from per-residues interaction energy calculations.•The “conserved” and “nonconserved” residues at the same position of the two cytokines’ binding interface were discovered. |
| ArticleNumber | 129907 |
| Author | Du, Qingqing Qian, Yan Xue, Weiwei |
| Author_xml | – sequence: 1 givenname: Qingqing surname: Du fullname: Du, Qingqing organization: Depart of Pharmacy, the Second Affiliated Hospital of Chongqing Medical University, Chongqing 400010, China – sequence: 2 givenname: Yan surname: Qian fullname: Qian, Yan email: cqqianyan@hospital.cqmu.edu.cn organization: Depart of Pharmacy, the Second Affiliated Hospital of Chongqing Medical University, Chongqing 400010, China – sequence: 3 givenname: Weiwei surname: Xue fullname: Xue, Weiwei email: xueww@cqu.edu.cn organization: School of Pharmaceutical Sciences, Chongqing Key Laboratory of Natural Product Synthesis and Drug Research, Chongqing University, Chongqing 401331, China |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/33845142$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1073/pnas.1922729117 10.1158/1535-7163.MCT-18-1258 10.1074/jbc.M303168200 10.1073/pnas.0705577104 10.1093/nar/gku316 10.1002/jcc.25592 10.1080/01621459.1963.10500845 10.1016/j.phymed.2020.153372 10.1158/0008-5472.CAN-15-2790 10.1016/j.jmgm.2005.12.005 10.1002/prot.21123 10.1371/journal.pone.0020161 10.1021/acs.jctc.5b00255 10.1093/nar/gkz397 10.1021/acs.chemrev.9b00055 10.1074/jbc.RA118.004375 10.1021/ar000033j 10.1016/S0022-2836(03)00670-3 10.1093/bioinformatics/btl529 10.1371/journal.pone.0022477 10.1021/j100058a043 10.1093/bioinformatics/btm404 10.1074/jbc.RA118.001920 10.1038/nm0617-788d 10.1002/prot.20033 10.3389/fmolb.2020.00029 10.1016/S0065-2911(08)60166-6 10.1073/pnas.1101835108 10.1080/14728222.2019.1677608 10.1074/jbc.M112.387324 10.1016/S0969-2126(00)00176-3 10.1126/science.1542794 10.1038/517109a 10.1038/s41577-018-0066-7 10.1038/nm.4307 10.1021/acs.jctc.7b00125 10.1146/annurev-immunol-032713-120211 |
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| Keywords | Molecular simulation Drug design Cytokines Cross-reactivity Protein-protein interactions |
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| References | Jones, Jenkins (bb0005) 2018; 18 Adrian-Segarra, Sreenivasan, Gajawada, Lorchner, Braun, Poling (bb0170) 2018; 293 Alford, Leaver-Fay, Jeliazkov, O’Meara, DiMaio, Park, Shapovalov, Renfrew, Mulligan, Kappel, Labonte, Pacella, Bonneau, Bradley, Dunbrack, Das, Baker, Kuhlman, Kortemme, Gray (bb0105) 2017; 13 Verstockt, Verstockt, Vermeire (bb0045) 2019; 23 Li, Chen, Xie, Yang, Luo, Jia, Shi, Wang, Zheng (bb0050) 2021; 80 Onufriev, Bashford, Case (bb0145) 2004; 55 Tippmann (bb0155) 2015; 517 Kollman, Massova, Reyes, Kuhn, Huo, Chong, Lee, Lee, Duan, Wang, Donini, Cieplak, Srinivasan, Case, Cheatham (bb0140) 2000; 33 Kim, Marquez, Sperberg, Wu, Bae, Huang, Sweet-Cordero, Cochran (bb0015) 2020; 117 Huang, Qi, Song, Zhang (bb0175) 2019; 40 Ward (bb0195) 1963; 58 Plun-Favreau, Perret, Diveu, Froger, Chevalier, Lelievre, Gascan, Chabbert (bb0075) 2003; 278 Sitkoff, Sharp, Honig (bb0150) 1994; 98 West, Hegazy, Owens, Bullers, Linggi, Buonocore, Coccia, Gortz, This, Stockenhuber, Pott, Friedrich, Ryzhakov, Baribaud, Brodmerkel, Cieluch, Rahman, Muller-Newen, Owens, Kuhl, Maloy, Plevy, Oxford, Keshav, Travis, Powrie (bb0035) 2017; 23 Hornak, Abel, Okur, Strockbine, Roitberg, Simmerling (bb0135) 2006; 65 Robert, Gouet (bb0090) 2014; 42 Kozakov, Hall, Chuang, Cencic, Brenke, Grove, Beglov, Pelletier, Whitty, Vajda (bb0200) 2011; 108 Maier, Martinez, Kasavajhala, Wickstrom, Hauser, Simmerling (bb0130) 2015; 11 Chollangi, Mather, Rodgers, Ash (bb0065) 2012; 287 Larkin, Blackshields, Brown, Chenna, McGettigan, McWilliam, Valentin, Wallace, Wilm, Lopez, Thompson, Gibson, Higgins (bb0085) 2007; 23 Huyton, Zhang, Luo, Lou, Hilton, Nicola, Garrett (bb0080) 2007; 104 Gray, Moughon, Wang, Schueler-Furman, Kuhlman, Rohl, Baker (bb0110) 2003; 331 Adrian-Segarra, Schindler, Gajawada, Lorchner, Braun, Poling (bb0025) 2018; 293 Gearing, Comeau, Friend, Gimpel, Thut, McGourty, Brasher, King, Gillis, Mosley (bb0060) 1992; 255 Wang, Sun, Wang, Wang, Liu, Zhang, Hou (bb0180) 2019; 119 Weng, Wang, Wang, Liu, Zhu, Li, Hou (bb0185) 2019; 47 Du, Qian, Xue (bb0070) 2020; 7 Webb, Sali (bb0100) 2016; 54 Viswanadhapalli, Luo, Sareddy, Santhamma, Zhou, Li, Ma, Sonavane, Pratap, Altwegg, Li, Chang, Chavez-Riveros, Dileep, Zhang, Pan, Murali, Bajda, Raj, Brenner, Manthati, Rao, Tekmal, Nair, Nickisch, Vadlamudi (bb0020) 2019; 18 Barer, Harwood (bb0160) 1999; 41 Spangler, Moraga, Mendoza, Garcia (bb0190) 2015; 33 Chaudhury, Berrondo, Weitzner, Muthu, Bergman, Gray (bb0120) 2011; 6 Fiser, Do, Sali (bb0095) 2000; 9 Letunic, Bork (bb0165) 2007; 23 West, Hegazy, Owens, Bullers, Linggi, Buonocore, Coccia, Gortz, This, Stockenhuber, Pott, Friedrich, Ryzhakov, Baribaud, Brodmerkel, Cieluch, Rahman, Muller-Newen, Owens, Kuhl, Maloy, Plevy, Oxford, Keshav, Travis, Powrie (bb0040) 2017; 23 Deller, Hudson, Ikemizu, Bravo, Jones, Heath (bb0055) 2000; 8 Kang, Narazaki, Metwally, Kishimoto (bb0010) 2020 Bressy, Lac, Nigri, Leca, Roques, Lavaut, Secq, Guillaumond, Bui, Pietrasz, Granjeaud, Bachet, Ouaissi, Iovanna, Vasseur, Tomasini (bb0030) 2018; 78 Fleishman, Leaver-Fay, Corn, Strauch, Khare, Koga, Ashworth, Murphy, Richter, Lemmon, Meiler, Baker (bb0115) 2011; 6 Wang, Wang, Kollman, Case (bb0125) 2006; 25 Gearing (10.1016/j.bbagen.2021.129907_bb0060) 1992; 255 Webb (10.1016/j.bbagen.2021.129907_bb0100) 2016; 54 Adrian-Segarra (10.1016/j.bbagen.2021.129907_bb0170) 2018; 293 Kang (10.1016/j.bbagen.2021.129907_bb0010) 2020 Viswanadhapalli (10.1016/j.bbagen.2021.129907_bb0020) 2019; 18 Chollangi (10.1016/j.bbagen.2021.129907_bb0065) 2012; 287 Huang (10.1016/j.bbagen.2021.129907_bb0175) 2019; 40 Huyton (10.1016/j.bbagen.2021.129907_bb0080) 2007; 104 Spangler (10.1016/j.bbagen.2021.129907_bb0190) 2015; 33 Bressy (10.1016/j.bbagen.2021.129907_bb0030) 2018; 78 Fiser (10.1016/j.bbagen.2021.129907_bb0095) 2000; 9 West (10.1016/j.bbagen.2021.129907_bb0035) 2017; 23 West (10.1016/j.bbagen.2021.129907_bb0040) 2017; 23 Plun-Favreau (10.1016/j.bbagen.2021.129907_bb0075) 2003; 278 Onufriev (10.1016/j.bbagen.2021.129907_bb0145) 2004; 55 Tippmann (10.1016/j.bbagen.2021.129907_bb0155) 2015; 517 Jones (10.1016/j.bbagen.2021.129907_bb0005) 2018; 18 Ward (10.1016/j.bbagen.2021.129907_bb0195) 1963; 58 Kozakov (10.1016/j.bbagen.2021.129907_bb0200) 2011; 108 Letunic (10.1016/j.bbagen.2021.129907_bb0165) 2007; 23 Kim (10.1016/j.bbagen.2021.129907_bb0015) 2020; 117 Sitkoff (10.1016/j.bbagen.2021.129907_bb0150) 1994; 98 Maier (10.1016/j.bbagen.2021.129907_bb0130) 2015; 11 Larkin (10.1016/j.bbagen.2021.129907_bb0085) 2007; 23 Verstockt (10.1016/j.bbagen.2021.129907_bb0045) 2019; 23 Fleishman (10.1016/j.bbagen.2021.129907_bb0115) 2011; 6 Wang (10.1016/j.bbagen.2021.129907_bb0180) 2019; 119 Adrian-Segarra (10.1016/j.bbagen.2021.129907_bb0025) 2018; 293 Kollman (10.1016/j.bbagen.2021.129907_bb0140) 2000; 33 Chaudhury (10.1016/j.bbagen.2021.129907_bb0120) 2011; 6 Du (10.1016/j.bbagen.2021.129907_bb0070) 2020; 7 Alford (10.1016/j.bbagen.2021.129907_bb0105) 2017; 13 Barer (10.1016/j.bbagen.2021.129907_bb0160) 1999; 41 Wang (10.1016/j.bbagen.2021.129907_bb0125) 2006; 25 Gray (10.1016/j.bbagen.2021.129907_bb0110) 2003; 331 Deller (10.1016/j.bbagen.2021.129907_bb0055) 2000; 8 Robert (10.1016/j.bbagen.2021.129907_bb0090) 2014; 42 Hornak (10.1016/j.bbagen.2021.129907_bb0135) 2006; 65 Weng (10.1016/j.bbagen.2021.129907_bb0185) 2019; 47 Li (10.1016/j.bbagen.2021.129907_bb0050) 2021; 80 |
| References_xml | – volume: 255 start-page: 1434 year: 1992 end-page: 1437 ident: bb0060 article-title: The IL-6 signal transducer, gp130: an oncostatin M receptor and affinity converter for the LIF receptor publication-title: Science – volume: 55 start-page: 383 year: 2004 end-page: 394 ident: bb0145 article-title: Exploring protein native states and large-scale conformational changes with a modified generalized born model publication-title: Proteins – volume: 25 start-page: 247 year: 2006 end-page: 260 ident: bb0125 article-title: Automatic atom type and bond type perception in molecular mechanical calculations publication-title: J. Mol. Graph. Model. – volume: 117 start-page: 14110 year: 2020 end-page: 14118 ident: bb0015 article-title: Engineering a potent receptor superagonist or antagonist from a novel IL-6 family cytokine ligand publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 41 start-page: 93 year: 1999 end-page: 137 ident: bb0160 article-title: Bacterial viability and culturability publication-title: Adv. Microb. Physiol. – volume: 293 start-page: 20181 year: 2018 end-page: 20199 ident: bb0170 article-title: The AB loop of oncostatin M (OSM) determines species-specific signaling in humans and mice publication-title: J. Biol. Chem. – volume: 23 start-page: 2947 year: 2007 end-page: 2948 ident: bb0085 article-title: Clustal W and clustal X version 2.0 publication-title: Bioinformatics – volume: 9 start-page: 1753 year: 2000 end-page: 1773 ident: bb0095 article-title: Modeling of loops in protein structures publication-title: Protein science : a publication of the Protein Society – volume: 98 start-page: 1978 year: 1994 end-page: 1988 ident: bb0150 article-title: Accurate calculation of hydration free energies using macroscopic solvent models publication-title: J. Phys. Chem. – volume: 40 start-page: 1045 year: 2019 end-page: 1056 ident: bb0175 article-title: Calculation of hot spots for protein-protein interaction in p53/PMI-MDM2/MDMX complexes publication-title: J. Comput. Chem. – volume: 23 start-page: 943 year: 2019 end-page: 954 ident: bb0045 article-title: Oncostatin M as a new diagnostic, prognostic and therapeutic target in inflammatory bowel disease (IBD) publication-title: Expert Opin. Ther. Targets – volume: 65 start-page: 712 year: 2006 end-page: 725 ident: bb0135 article-title: Comparison of multiple Amber force fields and development of improved protein backbone parameters publication-title: Proteins – volume: 23 start-page: 127 year: 2007 end-page: 128 ident: bb0165 article-title: Interactive Tree Of Life (iTOL): an online tool for phylogenetic tree display and annotation publication-title: Bioinformatics – volume: 331 start-page: 281 year: 2003 end-page: 299 ident: bb0110 article-title: Protein-protein docking with simultaneous optimization of rigid-body displacement and side-chain conformations publication-title: J. Mol. Biol. – volume: 78 start-page: 909 year: 2018 end-page: 921 ident: bb0030 article-title: LIF drives neural remodeling in pancreatic cancer and offers a new candidate biomarker publication-title: Cancer Res. – volume: 23 start-page: 579 year: 2017 end-page: 589 ident: bb0035 article-title: Oncostatin M drives intestinal inflammation and predicts response to tumor necrosis factor-neutralizing therapy in patients with inflammatory bowel disease publication-title: Nat. Med. – volume: 119 start-page: 9478 year: 2019 end-page: 9508 ident: bb0180 article-title: End-point binding free energy calculation with MM/PBSA and MM/GBSA: strategies and applications in drug design publication-title: Chem. Rev. – volume: 104 start-page: 12737 year: 2007 end-page: 12742 ident: bb0080 article-title: An unusual cytokine:Ig-domain interaction revealed in the crystal structure of leukemia inhibitory factor (LIF) in complex with the LIF receptor publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 6 year: 2011 ident: bb0120 article-title: Benchmarking and analysis of protein docking performance in Rosetta v3.2 publication-title: PLoS One – volume: 517 start-page: 109 year: 2015 end-page: 110 ident: bb0155 article-title: Programming tools: adventures with R publication-title: Nature – volume: 18 start-page: 1341 year: 2019 end-page: 1354 ident: bb0020 article-title: EC359: a first-in-class small-molecule inhibitor for targeting oncogenic LIFR signaling in triple-negative breast cancer publication-title: Mol. Cancer Ther. – volume: 11 start-page: 3696 year: 2015 end-page: 3713 ident: bb0130 article-title: ff14SB: improving the accuracy of protein side chain and backbone parameters from ff99SB publication-title: J. Chem. Theory Comput. – volume: 7 start-page: 29 year: 2020 ident: bb0070 article-title: Molecular simulation of oncostatin m and receptor (OSM-OSMR) interaction as a potential therapeutic target for inflammatory bowel disease publication-title: Front. Mol. Biosci. – volume: 278 start-page: 27169 year: 2003 end-page: 27179 ident: bb0075 article-title: Leukemia inhibitory factor (LIF), cardiotrophin-1, and oncostatin M share structural binding determinants in the immunoglobulin-like domain of LIF receptor publication-title: J. Biol. Chem. – volume: 293 start-page: 7017 year: 2018 end-page: 7029 ident: bb0025 article-title: The AB loop and D-helix in binding site III of human Oncostatin M (OSM) are required for OSM receptor activation publication-title: J. Biol. Chem. – volume: 18 start-page: 773 year: 2018 end-page: 789 ident: bb0005 article-title: Recent insights into targeting the IL-6 cytokine family in inflammatory diseases and cancer publication-title: Nat. Rev. Immunol. – start-page: 217 year: 2020 ident: bb0010 article-title: Historical overview of the interleukin-6 family cytokine publication-title: J. Exp. Med. – volume: 54 year: 2016 ident: bb0100 article-title: Comparative protein structure modeling using MODELLER publication-title: Current Protocols in Bioinformatics – volume: 108 start-page: 13528 year: 2011 end-page: 13533 ident: bb0200 article-title: Structural conservation of druggable hot spots in protein-protein interfaces publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 23 start-page: 788 year: 2017 ident: bb0040 article-title: Erratum: Oncostatin M drives intestinal inflammation and predicts response to tumor necrosis factor-neutralizing therapy in patients with inflammatory bowel disease publication-title: Nat. Med. – volume: 47 start-page: W322 year: 2019 end-page: W330 ident: bb0185 article-title: HawkDock: a web server to predict and analyze the protein-protein complex based on computational docking and MM/GBSA publication-title: Nucleic Acids Res. – volume: 33 start-page: 889 year: 2000 end-page: 897 ident: bb0140 article-title: Calculating structures and free energies of complex molecules: combining molecular mechanics and continuum models publication-title: Acc. Chem. Res. – volume: 6 year: 2011 ident: bb0115 article-title: RosettaScripts: a scripting language interface to the Rosetta macromolecular modeling suite publication-title: PLoS One – volume: 8 start-page: 863 year: 2000 end-page: 874 ident: bb0055 article-title: Crystal structure and functional dissection of the cytostatic cytokine oncostatin M publication-title: Structure – volume: 80 start-page: 153372 year: 2021 ident: bb0050 article-title: Feiyangchangweiyan capsule protects against ulcerative colitis in mice by modulating the OSM/OSMR pathway and improving gut microbiota publication-title: Phytomed. – volume: 287 start-page: 32848 year: 2012 end-page: 32859 ident: bb0065 article-title: A unique loop structure in oncostatin M determines binding affinity toward oncostatin M receptor and leukemia inhibitory factor receptor publication-title: J. Biol. Chem. – volume: 42 start-page: W320 year: 2014 end-page: W324 ident: bb0090 article-title: Deciphering key features in protein structures with the new ENDscript server publication-title: Nucleic Acids Res. – volume: 13 start-page: 3031 year: 2017 end-page: 3048 ident: bb0105 article-title: The rosetta all-atom energy function for macromolecular modeling and design publication-title: J. Chem. Theory Comput. – volume: 58 start-page: 236 year: 1963 end-page: 244 ident: bb0195 article-title: Hierarchical grouping to optimize an objective function publication-title: J. Am. Stat. Assoc. – volume: 33 start-page: 139 year: 2015 end-page: 167 ident: bb0190 article-title: Insights into cytokine-receptor interactions from cytokine engineering publication-title: Annu. Rev. Immunol. – volume: 117 start-page: 14110 year: 2020 ident: 10.1016/j.bbagen.2021.129907_bb0015 article-title: Engineering a potent receptor superagonist or antagonist from a novel IL-6 family cytokine ligand publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.1922729117 – volume: 18 start-page: 1341 year: 2019 ident: 10.1016/j.bbagen.2021.129907_bb0020 article-title: EC359: a first-in-class small-molecule inhibitor for targeting oncogenic LIFR signaling in triple-negative breast cancer publication-title: Mol. Cancer Ther. doi: 10.1158/1535-7163.MCT-18-1258 – volume: 278 start-page: 27169 year: 2003 ident: 10.1016/j.bbagen.2021.129907_bb0075 article-title: Leukemia inhibitory factor (LIF), cardiotrophin-1, and oncostatin M share structural binding determinants in the immunoglobulin-like domain of LIF receptor publication-title: J. Biol. Chem. doi: 10.1074/jbc.M303168200 – volume: 104 start-page: 12737 year: 2007 ident: 10.1016/j.bbagen.2021.129907_bb0080 article-title: An unusual cytokine:Ig-domain interaction revealed in the crystal structure of leukemia inhibitory factor (LIF) in complex with the LIF receptor publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.0705577104 – volume: 42 start-page: W320 year: 2014 ident: 10.1016/j.bbagen.2021.129907_bb0090 article-title: Deciphering key features in protein structures with the new ENDscript server publication-title: Nucleic Acids Res. doi: 10.1093/nar/gku316 – volume: 40 start-page: 1045 year: 2019 ident: 10.1016/j.bbagen.2021.129907_bb0175 article-title: Calculation of hot spots for protein-protein interaction in p53/PMI-MDM2/MDMX complexes publication-title: J. Comput. Chem. doi: 10.1002/jcc.25592 – volume: 58 start-page: 236 year: 1963 ident: 10.1016/j.bbagen.2021.129907_bb0195 article-title: Hierarchical grouping to optimize an objective function publication-title: J. Am. Stat. Assoc. doi: 10.1080/01621459.1963.10500845 – volume: 80 start-page: 153372 year: 2021 ident: 10.1016/j.bbagen.2021.129907_bb0050 article-title: Feiyangchangweiyan capsule protects against ulcerative colitis in mice by modulating the OSM/OSMR pathway and improving gut microbiota publication-title: Phytomed. doi: 10.1016/j.phymed.2020.153372 – volume: 78 start-page: 909 year: 2018 ident: 10.1016/j.bbagen.2021.129907_bb0030 article-title: LIF drives neural remodeling in pancreatic cancer and offers a new candidate biomarker publication-title: Cancer Res. doi: 10.1158/0008-5472.CAN-15-2790 – volume: 25 start-page: 247 year: 2006 ident: 10.1016/j.bbagen.2021.129907_bb0125 article-title: Automatic atom type and bond type perception in molecular mechanical calculations publication-title: J. Mol. Graph. Model. doi: 10.1016/j.jmgm.2005.12.005 – volume: 65 start-page: 712 year: 2006 ident: 10.1016/j.bbagen.2021.129907_bb0135 article-title: Comparison of multiple Amber force fields and development of improved protein backbone parameters publication-title: Proteins doi: 10.1002/prot.21123 – volume: 6 year: 2011 ident: 10.1016/j.bbagen.2021.129907_bb0115 article-title: RosettaScripts: a scripting language interface to the Rosetta macromolecular modeling suite publication-title: PLoS One doi: 10.1371/journal.pone.0020161 – volume: 11 start-page: 3696 year: 2015 ident: 10.1016/j.bbagen.2021.129907_bb0130 article-title: ff14SB: improving the accuracy of protein side chain and backbone parameters from ff99SB publication-title: J. Chem. Theory Comput. doi: 10.1021/acs.jctc.5b00255 – volume: 47 start-page: W322 year: 2019 ident: 10.1016/j.bbagen.2021.129907_bb0185 article-title: HawkDock: a web server to predict and analyze the protein-protein complex based on computational docking and MM/GBSA publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkz397 – volume: 54 year: 2016 ident: 10.1016/j.bbagen.2021.129907_bb0100 article-title: Comparative protein structure modeling using MODELLER – volume: 119 start-page: 9478 year: 2019 ident: 10.1016/j.bbagen.2021.129907_bb0180 article-title: End-point binding free energy calculation with MM/PBSA and MM/GBSA: strategies and applications in drug design publication-title: Chem. Rev. doi: 10.1021/acs.chemrev.9b00055 – volume: 293 start-page: 20181 year: 2018 ident: 10.1016/j.bbagen.2021.129907_bb0170 article-title: The AB loop of oncostatin M (OSM) determines species-specific signaling in humans and mice publication-title: J. Biol. Chem. doi: 10.1074/jbc.RA118.004375 – volume: 33 start-page: 889 year: 2000 ident: 10.1016/j.bbagen.2021.129907_bb0140 article-title: Calculating structures and free energies of complex molecules: combining molecular mechanics and continuum models publication-title: Acc. Chem. Res. doi: 10.1021/ar000033j – volume: 331 start-page: 281 year: 2003 ident: 10.1016/j.bbagen.2021.129907_bb0110 article-title: Protein-protein docking with simultaneous optimization of rigid-body displacement and side-chain conformations publication-title: J. Mol. Biol. doi: 10.1016/S0022-2836(03)00670-3 – volume: 23 start-page: 127 year: 2007 ident: 10.1016/j.bbagen.2021.129907_bb0165 article-title: Interactive Tree Of Life (iTOL): an online tool for phylogenetic tree display and annotation publication-title: Bioinformatics doi: 10.1093/bioinformatics/btl529 – volume: 6 year: 2011 ident: 10.1016/j.bbagen.2021.129907_bb0120 article-title: Benchmarking and analysis of protein docking performance in Rosetta v3.2 publication-title: PLoS One doi: 10.1371/journal.pone.0022477 – volume: 98 start-page: 1978 year: 1994 ident: 10.1016/j.bbagen.2021.129907_bb0150 article-title: Accurate calculation of hydration free energies using macroscopic solvent models publication-title: J. Phys. Chem. doi: 10.1021/j100058a043 – volume: 23 start-page: 2947 year: 2007 ident: 10.1016/j.bbagen.2021.129907_bb0085 article-title: Clustal W and clustal X version 2.0 publication-title: Bioinformatics doi: 10.1093/bioinformatics/btm404 – volume: 293 start-page: 7017 year: 2018 ident: 10.1016/j.bbagen.2021.129907_bb0025 article-title: The AB loop and D-helix in binding site III of human Oncostatin M (OSM) are required for OSM receptor activation publication-title: J. Biol. Chem. doi: 10.1074/jbc.RA118.001920 – volume: 23 start-page: 788 year: 2017 ident: 10.1016/j.bbagen.2021.129907_bb0040 article-title: Erratum: Oncostatin M drives intestinal inflammation and predicts response to tumor necrosis factor-neutralizing therapy in patients with inflammatory bowel disease publication-title: Nat. Med. doi: 10.1038/nm0617-788d – volume: 55 start-page: 383 year: 2004 ident: 10.1016/j.bbagen.2021.129907_bb0145 article-title: Exploring protein native states and large-scale conformational changes with a modified generalized born model publication-title: Proteins doi: 10.1002/prot.20033 – start-page: 217 year: 2020 ident: 10.1016/j.bbagen.2021.129907_bb0010 article-title: Historical overview of the interleukin-6 family cytokine publication-title: J. Exp. Med. – volume: 7 start-page: 29 year: 2020 ident: 10.1016/j.bbagen.2021.129907_bb0070 article-title: Molecular simulation of oncostatin m and receptor (OSM-OSMR) interaction as a potential therapeutic target for inflammatory bowel disease publication-title: Front. Mol. Biosci. doi: 10.3389/fmolb.2020.00029 – volume: 41 start-page: 93 year: 1999 ident: 10.1016/j.bbagen.2021.129907_bb0160 article-title: Bacterial viability and culturability publication-title: Adv. Microb. Physiol. doi: 10.1016/S0065-2911(08)60166-6 – volume: 108 start-page: 13528 year: 2011 ident: 10.1016/j.bbagen.2021.129907_bb0200 article-title: Structural conservation of druggable hot spots in protein-protein interfaces publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.1101835108 – volume: 23 start-page: 943 year: 2019 ident: 10.1016/j.bbagen.2021.129907_bb0045 article-title: Oncostatin M as a new diagnostic, prognostic and therapeutic target in inflammatory bowel disease (IBD) publication-title: Expert Opin. Ther. Targets doi: 10.1080/14728222.2019.1677608 – volume: 287 start-page: 32848 year: 2012 ident: 10.1016/j.bbagen.2021.129907_bb0065 article-title: A unique loop structure in oncostatin M determines binding affinity toward oncostatin M receptor and leukemia inhibitory factor receptor publication-title: J. Biol. Chem. doi: 10.1074/jbc.M112.387324 – volume: 8 start-page: 863 year: 2000 ident: 10.1016/j.bbagen.2021.129907_bb0055 article-title: Crystal structure and functional dissection of the cytostatic cytokine oncostatin M publication-title: Structure doi: 10.1016/S0969-2126(00)00176-3 – volume: 255 start-page: 1434 year: 1992 ident: 10.1016/j.bbagen.2021.129907_bb0060 article-title: The IL-6 signal transducer, gp130: an oncostatin M receptor and affinity converter for the LIF receptor publication-title: Science doi: 10.1126/science.1542794 – volume: 517 start-page: 109 year: 2015 ident: 10.1016/j.bbagen.2021.129907_bb0155 article-title: Programming tools: adventures with R publication-title: Nature doi: 10.1038/517109a – volume: 18 start-page: 773 year: 2018 ident: 10.1016/j.bbagen.2021.129907_bb0005 article-title: Recent insights into targeting the IL-6 cytokine family in inflammatory diseases and cancer publication-title: Nat. Rev. Immunol. doi: 10.1038/s41577-018-0066-7 – volume: 23 start-page: 579 year: 2017 ident: 10.1016/j.bbagen.2021.129907_bb0035 article-title: Oncostatin M drives intestinal inflammation and predicts response to tumor necrosis factor-neutralizing therapy in patients with inflammatory bowel disease publication-title: Nat. Med. doi: 10.1038/nm.4307 – volume: 13 start-page: 3031 year: 2017 ident: 10.1016/j.bbagen.2021.129907_bb0105 article-title: The rosetta all-atom energy function for macromolecular modeling and design publication-title: J. Chem. Theory Comput. doi: 10.1021/acs.jctc.7b00125 – volume: 33 start-page: 139 year: 2015 ident: 10.1016/j.bbagen.2021.129907_bb0190 article-title: Insights into cytokine-receptor interactions from cytokine engineering publication-title: Annu. Rev. Immunol. doi: 10.1146/annurev-immunol-032713-120211 – volume: 9 start-page: 1753 year: 2000 ident: 10.1016/j.bbagen.2021.129907_bb0095 article-title: Modeling of loops in protein structures |
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