PublisherDOIYearVolumeIssuePageTitleAuthor(s)Link
The Korean Journal of Internal Medicine10.3904/kjim.2016.3152019343634-642MicroRNA-16 inhibits cell proliferation and migration by targeting heat shock protein 70 in heat-denatured dermal fibroblastsChun Zhang, Jinhua Dai, Youfen Fan, Xianghui He, Renxiong Weihttp://kjim.org/upload/kjim-2016-315.pdf, http://kjim.org/journal/view.php?doi=10.3904/kjim.2016.315, http://www.kjim.org/upload/kjim-2016-315.pdf
PLOS ONE10.1371/journal.pone.01318672015107e0131867MicroRNA-23b Inhibits the Proliferation and Migration of Heat-Denatured Fibroblasts by Targeting Smad3Xipeng Zhang, Jie Yang, Jiming Zhao, Pihong Zhang, Xiaoyuan Huanghttp://dx.plos.org/10.1371/journal.pone.0131867
Plant Physiology10.1104/pp.122.1.18920001221189-198A Small Heat Shock Protein Cooperates with Heat Shock Protein 70 Systems to Reactivate a Heat-Denatured ProteinGarrett J. Lee, Elizabeth Vierlinghttps://syndication.highwire.org/content/doi/10.1104/pp.122.1.189
Cancer Cell International10.1186/s12935-018-0551-x2018181microRNA-338-3p inhibits proliferation, migration, invasion, and EMT in osteosarcoma cells by targeting activator of 90 kDa heat shock protein ATPase homolog 1Riliang Cao, Jianli Shao, Yabin Hu, Liang Wang, Zhizhong Li, Guodong Sun, Xiaoliang Gaohttp://link.springer.com/content/pdf/10.1186/s12935-018-0551-x.pdf, http://link.springer.com/article/10.1186/s12935-018-0551-x/fulltext.html, http://link.springer.com/content/pdf/10.1186/s12935-018-0551-x.pdf
Phytomedicine10.1016/j.phymed.2006.02.0062006WITHDRAWN:2′,4′,7-Trihydroxyisoflavon (THF) inhibits heat-shock-induced matrix metalloproteinase-1 expression in human dermal fibroblastsH.-I. Moonhttps://api.elsevier.com/content/article/PII:S0944711306000420?httpAccept=text/xml, https://api.elsevier.com/content/article/PII:S0944711306000420?httpAccept=text/plain
Bioengineered10.1080/21655979.2016.1267885201786686-692Regulation function of MMP-1 downregulated by siRNA on migration of heat-denatured dermal fibroblastsXianghui He, Jinhua Dai, Youfen Fan, Chun Zhang, Xihong Zhaohttps://www.tandfonline.com/doi/pdf/10.1080/21655979.2016.1267885, https://www.tandfonline.com/doi/pdf/10.1080/21655979.2016.1267885
Alzheimer's & Dementia10.1016/j.jalz.2013.04.220201394P512Targeting protein-protein interactions in heat shock protein 70 (Hsp70) to treat neurodegenerative diseaseJason Gestwickihttps://api.elsevier.com/content/article/PII:S1552526013003713?httpAccept=text/xml, https://api.elsevier.com/content/article/PII:S1552526013003713?httpAccept=text/plain
The EMBO Journal10.1093/emboj/16.3.6591997163659-671A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent stateG. J. Leehttps://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1093%2Femboj%2F16.3.659, https://onlinelibrary.wiley.com/doi/full/10.1093/emboj/16.3.659
The International Journal of Biochemistry & Cell Biology10.1016/s1357-2725(04)00027-520043681585-1598A Trypanosoma cruzi heat shock protein 40 is able to stimulate the adenosine triphosphate hydrolysis activity of heat shock protein 70 and can substitute for a yeast heat shock protein 40A EDKINShttp://api.elsevier.com/content/article/PII:S1357-2725(04)00027-5?httpAccept=text/xml, http://api.elsevier.com/content/article/PII:S1357-2725(04)00027-5?httpAccept=text/plain
The International Journal of Biochemistry & Cell Biology10.1016/j.biocel.2004.01.01620043681585-1598A Trypanosoma cruzi heat shock protein 40 is able to stimulate the adenosine triphosphate hydrolysis activity of heat shock protein 70 and can substitute for a yeast heat shock protein 40Adrienne L Edkins, Michael H Ludewig, Gregory L Blatchhttps://api.elsevier.com/content/article/PII:S1357272504000275?httpAccept=text/xml, https://api.elsevier.com/content/article/PII:S1357272504000275?httpAccept=text/plain