{"id":754,"date":"2018-05-07T13:25:24","date_gmt":"2018-05-07T05:25:24","guid":{"rendered":"http:\/\/people.utm.my\/firdausw\/?p=754"},"modified":"2018-05-07T13:26:31","modified_gmt":"2018-05-07T05:26:31","slug":"our-first-review-article-on-heat-shock-protein","status":"publish","type":"post","link":"https:\/\/people.utm.my\/firdausw\/2018\/05\/07\/our-first-review-article-on-heat-shock-protein\/","title":{"rendered":"First Review Article on Heat Shock Protein 47"},"content":{"rendered":"<p>Our first review article on Heat Shock Protein 47 (HSP47) is now published on Wiley&#8217;s Encyclopaedia of Life Sciences (eLS). It can be accessed <a href=\"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/9780470015902.a0028005\" target=\"_blank\" rel=\"noopener\">here<\/a>.<\/p>\n<p>Abstract:<\/p>\n<p>&#8220;Heat shock protein 47 (HSP47), a noninhibitory serine protease inhibitor (SERPIN, clade H1) family member, is a unique collagen\u2010specific molecular chaperone. The binding of HSP47 to collagen has been the subject of intense investigation, as it binds to and only to collagen. This binding specificity presents a relatively unexplored potential of using HSP47 as a target for treatment of collagen\u2010related diseases and abnormalities. Homology model studies and structural determination have revealed the important amino acid residues for HSP47\u2010collagen binding interaction. HSP47\u2010knockout experiment in mice proved the importance of HSP47 for correct folding of collagen triple helices, thus critical for normal development. Various diagnostic and treatment strategies based on the unique HSP47 functions are now being investigated and proposed.&#8221; (eLS, DOI:\u00a010.1002\/9780470015902.a0028005)<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Our first review article on Heat Shock Protein 47 (HSP47) is now published on Wiley&#8217;s Encyclopaedia of Life Sciences (eLS). It can be accessed here. Abstract: &#8220;Heat shock protein 47 (HSP47), a noninhibitory serine protease inhibitor (SERPIN, clade H1) family member, is a unique collagen\u2010specific molecular chaperone. The binding of HSP47 to collagen has been [&hellip;]<\/p>\n","protected":false},"author":5588,"featured_media":0,"comment_status":"open","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[1],"tags":[],"class_list":["post-754","post","type-post","status-publish","format-standard","hentry","category-uncategorized"],"_links":{"self":[{"href":"https:\/\/people.utm.my\/firdausw\/wp-json\/wp\/v2\/posts\/754","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/people.utm.my\/firdausw\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/people.utm.my\/firdausw\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/people.utm.my\/firdausw\/wp-json\/wp\/v2\/users\/5588"}],"replies":[{"embeddable":true,"href":"https:\/\/people.utm.my\/firdausw\/wp-json\/wp\/v2\/comments?post=754"}],"version-history":[{"count":0,"href":"https:\/\/people.utm.my\/firdausw\/wp-json\/wp\/v2\/posts\/754\/revisions"}],"wp:attachment":[{"href":"https:\/\/people.utm.my\/firdausw\/wp-json\/wp\/v2\/media?parent=754"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/people.utm.my\/firdausw\/wp-json\/wp\/v2\/categories?post=754"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/people.utm.my\/firdausw\/wp-json\/wp\/v2\/tags?post=754"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}