{"id":1077,"date":"2014-07-17T18:00:57","date_gmt":"2014-07-17T16:00:57","guid":{"rendered":"http:\/\/news.embl.de\/?p=1077"},"modified":"2024-11-14T16:32:43","modified_gmt":"2024-11-14T15:32:43","slug":"complexity","status":"publish","type":"post","link":"https:\/\/www.embl.org\/news\/science\/complexity\/","title":{"rendered":"Embracing cellular complexity"},"content":{"rendered":"\n<p>Those not steeped in structural and computational biology will likely miss the joke; the new review completes a trilogy of papers published over the last two decades, each one upping the numerical ante on its predecessor (\u2018One thousand families for the molecular biologist\u2019 by Chothia in 1992 and \u2018Ten thousand interactions for the molecular biologist\u2019 by EMBL alumni <a href=\"http:\/\/www.irbbarcelona.org\/index.php\/en\/research\/programmes\/structural-and-computational-biology\/structural-bioinformatics\/people\/patrick-aloy\" target=\"_blank\" rel=\"noopener noreferrer\">Aloy<\/a> and <a href=\"http:\/\/www.russelllab.org\/\" target=\"_blank\" rel=\"noopener noreferrer\">Russell<\/a> in 2004). The upward trend in the literature reveals that as technology allows scientists to investigate smaller and smaller cellular structures with increasing accuracy, they are discovering a level of molecular complexity that is far beyond what earlier generations had predicted. Molecular biologists often focus years of their research on individual molecules or pathways. \u201cYou\u2019ve got to be reductionist. You\u2019ve got to tease apart the systems and then rebuild them to understand them\u201d, says Gibson, <a title=\"Gibson Team\" href=\"http:\/\/intranet.embl.de\/research\/scb\/gibson\/index.html\" target=\"_blank\" rel=\"noopener noreferrer\">a team leader<\/a> at EMBL Heidelberg. \u201cWhat happens is that you then underestimate the complexity in the system.\u201d It\u2019s that complexity that he hopes to bring to the fore and reestablish as a primary concern for the field going forward.<\/p>\n\n\n\n<h3 class=\"wp-block-heading\">Myriad motifs<\/h3>\n\n\n\n<p>In their review, Gibson and colleagues focus on specific elements called peptide motifs: which are short sites of molecular interaction within larger \u2018intrinsically disordered\u2019 regions of proteins. Being disordered doesn\u2019t mean those regions misbehave; they simply don\u2019t fold into a specified shape on their own. They need to be bound by another molecule to become more rigidly shaped, often by a so-called \u201cinduced fit mechanism.\u201d (The natively ordered regions, called \u2018globular domains,\u2019 are the most well-known protein modules because their always-folded shape makes them amenable to techniques such as X-ray crystallography, and their structure often provides insight into the protein\u2019s function.) Peptide motifs far outnumber ordered domains in the human proteome, and the number of potential interactions those motifs engage in is expected to be correspondingly high. Not only can peptide motifs bind to the ordered domains of other proteins, many of them can also be modified by a variety of enzymes at post-translational modification (PTM) sites, contained within the motif. &nbsp;Phosphorylation, the most common type of protein modification, is predicted to occur at a maximum of about 400,000 PTMs. But phosphorylation is just one type of site-specific protein modification; there are over 300 different kinds of PTMs, a number which contributes toward Gibson\u2019s estimation of one million peptide motifs.<\/p>\n\n\n\n<div class=\"wp-block-image wp-image-1113 size-full\"><figure class=\"vf-figure  | vf-figure--align vf-figure--align-centered \"><img loading=\"lazy\" decoding=\"async\" width=\"620\" height=\"254\" class=\"vf-figure__image\" src=\"http:\/\/news.embl.de\/wp-content\/uploads\/2014\/07\/1407_gibson2-e1405671093774.jpg\" alt=\"\" class=\"wp-image-1113\" srcset=\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2014\/07\/1407_gibson2-e1405671093774.jpg 620w, https:\/\/www.embl.org\/news\/wp-content\/uploads\/2014\/07\/1407_gibson2-e1405671093774-300x123.jpg 300w\" sizes=\"auto, (max-width: 620px) 100vw, 620px\" \/><figcaption class=\"vf-figure__caption\">Gibson&#8217;s paper illustrates the inherent complexity in protein interactions. PHOTO: GIBSON ET AL<\/figcaption><\/figure><\/div>\n\n\n\n<p>While acknowledging the possibility of large numbers of PTMs, some scientists argue that not all of them are functional. PTMs seem to vary quite a bit between species and accumulate changes quickly (on evolutionary timescales), traits that might imply that they aren\u2019t vital for survival. By contrast, molecules called piRNAs that protect DNA in reproductive cells from certain mutations take the same form in just about every animal. In addition (though there are exceptions, e.g. in cell cycle), a single PTM might have so small an effect that mutating it wouldn\u2019t change the observable cell function. But, says Gibson, the sheer number of possible protein interactions means that a PTM might be active only under a set of very specific conditions. \u201cYou could knock out a single phosphorylation site in a mouse and never be able to see any effects. But that [site] might only work in combination with other PTMs when an animal experiences starvation plus dehydration or some other combination of stressful conditions, and you\u2019re never going to see that, because to do so would require an unethical experiment,\u201d he says.<\/p>\n\n\n\n<blockquote class=\"vf-blockquote\"><p>All these dogmatic titles that you see in prominent articles about how the cell works are never true except in a very limited sense.<\/p><\/blockquote>\n\n\n\n<h3 class=\"wp-block-heading\">Deceptively simple<\/h3>\n\n\n\n<p>Gibson expects mixed responses to this openly opinionated article. The estimates that there are so many peptide motifs potentially worth exploring should, at the very least, be encouraging to younger molecular biologists, as it means that they have a certain level of job security over the next few decades. However, he\u2019s keenly aware that accounting for the complexity presented by transient and diverse PTMs is in direct conflict with the assertive language typical of scientific claims that garner press coverage and accolades. \u201cA paper might say, \u2018We found out how [the protein] P53 works\u2019, but if you change conditions or change cell type, P53 works very differently,\u201d says Gibson. \u201cAll these dogmatic titles that you see in prominent articles about how the cell works are never true, except in a very limited sense,\u201d he continues. \u201cThere\u2019s a kind of unholy alliance of editors and big signalling labs who want to keep on making these easy-to-sell statements.\u201d It\u2019s not just cell signalling biologists, either \u2013 he believes that many systems biologists and others whose work depends on models of cellular components are also not fond of complexity, because modelling requires that the object or process being studied be stripped to its simplest form just so that the computations are feasible. Gibson thinks this is a fundamental problem because it ignores all the potential outcomes that could happen under different circumstances, which in the biomedical context could, for example, be the difference between a drug that helps patients and one that inadvertently harms them.<\/p>\n\n\n\n<h3 class=\"wp-block-heading\">Complexity in context<\/h3>\n\n\n\n<p>How would Gibson and his colleagues recommend a molecular biologist proceed when facing the daunting prospect of a million peptide motifs? The answer is best summarised by the conclusion of their paper itself: \u201cA careful choice of experimental design to test motifs is crucial, as their sensitive functionality [\u2026] may lead to incorrect inferences. Therefore, an important challenge for the community is to not only identify binding motifs and PTM sites, but also functionally characterize these peptide motifs by investigating them in the right biological context.\u201d<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Cell biologists &#8220;underestimate the complexity&#8221; of protein interactions, says Toby Gibson.<\/p>\n","protected":false},"author":7,"featured_media":1078,"comment_status":"closed","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"footnotes":""},"categories":[2,17591],"tags":[64,467,43,69,82,45,51],"embl_taxonomy":[],"class_list":["post-1077","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-science","category-science-technology","tag-cell-biology","tag-gibson","tag-heidelberg","tag-methods","tag-modelling","tag-proteomics","tag-systems-biology"],"acf":{"article_intro":"<p>\u2018A Million Peptide Motifs for the Molecular Biologist,\u2019 a paper from Toby Gibson and like-minded colleagues in <em>Molecular Cell<\/em> boldly claims.<\/p>\n","related_links":[{"link_description":"Ten thousand interactions for the molecular biologist. ","link_url":"http:\/\/www.nature.com\/nbt\/journal\/v22\/n10\/abs\/nbt1018.html"},{"link_description":"One thousand families for the molecular biologist. ","link_url":"http:\/\/www.nature.com\/nature\/journal\/v357\/n6379\/abs\/357543a0.html"}],"article_sources":[{"source_description":"<p>Tompa <em>et al<\/em>.\u00a0<em>Molecular<\/em> Cell,<em>\u00a0<\/em>17 July 2014. DOI:10.1016\/ j.molcel.2014.05.032<\/p>\n","source_link_url":"http:\/\/www.cell.com\/molecular-cell\/abstract\/S1097-2765(14)00562-0"}],"vf_locked":false,"featured":false,"color":"#007B53"},"embl_taxonomy_terms":[],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v26.2 - https:\/\/yoast.com\/wordpress\/plugins\/seo\/ -->\n<title>Embracing cellular complexity | EMBL<\/title>\n<meta name=\"description\" content=\"Cell biologists &quot;underestimate the complexity&quot; of protein interactions, says Toby Gibson\" \/>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/www.embl.org\/news\/science\/complexity\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Embracing cellular complexity | EMBL\" \/>\n<meta property=\"og:description\" content=\"Cell biologists &quot;underestimate the complexity&quot; of protein interactions, says Toby Gibson\" \/>\n<meta property=\"og:url\" content=\"https:\/\/www.embl.org\/news\/science\/complexity\/\" \/>\n<meta property=\"og:site_name\" content=\"EMBL\" \/>\n<meta property=\"article:publisher\" content=\"https:\/\/www.facebook.com\/embl.org\/\" \/>\n<meta property=\"article:published_time\" content=\"2014-07-17T16:00:57+00:00\" \/>\n<meta property=\"article:modified_time\" content=\"2024-11-14T15:32:43+00:00\" \/>\n<meta property=\"og:image\" content=\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2014\/07\/1407_gibson_photo.jpg\" \/>\n\t<meta property=\"og:image:width\" content=\"620\" \/>\n\t<meta property=\"og:image:height\" content=\"464\" \/>\n\t<meta property=\"og:image:type\" content=\"image\/jpeg\" \/>\n<meta name=\"author\" content=\"Lindsay Brownell\" \/>\n<meta name=\"twitter:card\" content=\"summary_large_image\" \/>\n<meta name=\"twitter:creator\" content=\"@LindzBro\" \/>\n<meta name=\"twitter:site\" content=\"@embl\" \/>\n<meta name=\"twitter:label1\" content=\"Written by\" \/>\n\t<meta name=\"twitter:data1\" content=\"Lindsay Brownell\" \/>\n\t<meta name=\"twitter:label2\" content=\"Est. reading time\" \/>\n\t<meta name=\"twitter:data2\" content=\"5 minutes\" \/>\n<script type=\"application\/ld+json\" class=\"yoast-schema-graph\">{\"@context\":\"https:\/\/schema.org\",\"@graph\":[{\"@type\":\"NewsArticle\",\"@id\":\"https:\/\/www.embl.org\/news\/science\/complexity\/#article\",\"isPartOf\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/complexity\/\"},\"author\":{\"name\":\"Lindsay Brownell\",\"@id\":\"https:\/\/www.embl.org\/news\/#\/schema\/person\/93b4023d898e31d430ebb837620c8786\"},\"headline\":\"Embracing cellular complexity\",\"datePublished\":\"2014-07-17T16:00:57+00:00\",\"dateModified\":\"2024-11-14T15:32:43+00:00\",\"mainEntityOfPage\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/complexity\/\"},\"wordCount\":964,\"publisher\":{\"@id\":\"https:\/\/www.embl.org\/news\/#organization\"},\"image\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/complexity\/#primaryimage\"},\"thumbnailUrl\":\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2014\/07\/1407_gibson_photo.jpg\",\"keywords\":[\"cell biology\",\"gibson\",\"heidelberg\",\"methods\",\"modelling\",\"proteomics\",\"systems biology\"],\"articleSection\":[\"Science\",\"Science &amp; Technology\"],\"inLanguage\":\"en-US\"},{\"@type\":\"WebPage\",\"@id\":\"https:\/\/www.embl.org\/news\/science\/complexity\/\",\"url\":\"https:\/\/www.embl.org\/news\/science\/complexity\/\",\"name\":\"Embracing cellular complexity | EMBL\",\"isPartOf\":{\"@id\":\"https:\/\/www.embl.org\/news\/#website\"},\"primaryImageOfPage\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/complexity\/#primaryimage\"},\"image\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/complexity\/#primaryimage\"},\"thumbnailUrl\":\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2014\/07\/1407_gibson_photo.jpg\",\"datePublished\":\"2014-07-17T16:00:57+00:00\",\"dateModified\":\"2024-11-14T15:32:43+00:00\",\"description\":\"Cell biologists \\\"underestimate the complexity\\\" of protein interactions, says Toby Gibson\",\"inLanguage\":\"en-US\",\"potentialAction\":[{\"@type\":\"ReadAction\",\"target\":[\"https:\/\/www.embl.org\/news\/science\/complexity\/\"]}]},{\"@type\":\"ImageObject\",\"inLanguage\":\"en-US\",\"@id\":\"https:\/\/www.embl.org\/news\/science\/complexity\/#primaryimage\",\"url\":\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2014\/07\/1407_gibson_photo.jpg\",\"contentUrl\":\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2014\/07\/1407_gibson_photo.jpg\",\"width\":620,\"height\":464,\"caption\":\"PHOTO: PASIEKA SCIENCE PHOTO LIBRARY\"},{\"@type\":\"WebSite\",\"@id\":\"https:\/\/www.embl.org\/news\/#website\",\"url\":\"https:\/\/www.embl.org\/news\/\",\"name\":\"European Molecular Biology Laboratory News\",\"description\":\"News from the European Molecular Biology Laboratory\",\"publisher\":{\"@id\":\"https:\/\/www.embl.org\/news\/#organization\"},\"alternateName\":\"EMBL News\",\"potentialAction\":[{\"@type\":\"SearchAction\",\"target\":{\"@type\":\"EntryPoint\",\"urlTemplate\":\"https:\/\/www.embl.org\/news\/?s={search_term_string}\"},\"query-input\":{\"@type\":\"PropertyValueSpecification\",\"valueRequired\":true,\"valueName\":\"search_term_string\"}}],\"inLanguage\":\"en-US\"},{\"@type\":\"Organization\",\"@id\":\"https:\/\/www.embl.org\/news\/#organization\",\"name\":\"European Molecular Biology Laboratory\",\"alternateName\":\"EMBL\",\"url\":\"https:\/\/www.embl.org\/news\/\",\"logo\":{\"@type\":\"ImageObject\",\"inLanguage\":\"en-US\",\"@id\":\"https:\/\/www.embl.org\/news\/#\/schema\/logo\/image\/\",\"url\":\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2025\/09\/EMBL_logo_colour-1-300x144-1.png\",\"contentUrl\":\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2025\/09\/EMBL_logo_colour-1-300x144-1.png\",\"width\":300,\"height\":144,\"caption\":\"European Molecular Biology Laboratory\"},\"image\":{\"@id\":\"https:\/\/www.embl.org\/news\/#\/schema\/logo\/image\/\"},\"sameAs\":[\"https:\/\/www.facebook.com\/embl.org\/\",\"https:\/\/x.com\/embl\",\"https:\/\/www.instagram.com\/embl_org\/\",\"https:\/\/www.linkedin.com\/company\/15813\/\",\"https:\/\/www.youtube.com\/user\/emblmedia\/\"]},{\"@type\":\"Person\",\"@id\":\"https:\/\/www.embl.org\/news\/#\/schema\/person\/93b4023d898e31d430ebb837620c8786\",\"name\":\"Lindsay Brownell\",\"image\":{\"@type\":\"ImageObject\",\"inLanguage\":\"en-US\",\"@id\":\"https:\/\/www.embl.org\/news\/#\/schema\/person\/image\/\",\"url\":\"https:\/\/secure.gravatar.com\/avatar\/662a20dd8b58b2d277ac0cbb3e90b1579ef59dd4112b7004ec0b07dcc0a948c1?s=96&d=mm&r=g\",\"contentUrl\":\"https:\/\/secure.gravatar.com\/avatar\/662a20dd8b58b2d277ac0cbb3e90b1579ef59dd4112b7004ec0b07dcc0a948c1?s=96&d=mm&r=g\",\"caption\":\"Lindsay Brownell\"},\"description\":\"Lindsay Brownell was a science writing intern on EMBL\u2019s communications team. She once climbed into an air duct at midnight while interviewing members of MIT\u2019s hacking community for radio.\",\"sameAs\":[\"https:\/\/x.com\/LindzBro\"],\"url\":\"https:\/\/www.embl.org\/news\/author\/lindsay-brownell\/\"}]}<\/script>\n<!-- \/ Yoast SEO plugin. -->","yoast_head_json":{"title":"Embracing cellular complexity | EMBL","description":"Cell biologists \"underestimate the complexity\" of protein interactions, says Toby Gibson","robots":{"index":"index","follow":"follow","max-snippet":"max-snippet:-1","max-image-preview":"max-image-preview:large","max-video-preview":"max-video-preview:-1"},"canonical":"https:\/\/www.embl.org\/news\/science\/complexity\/","og_locale":"en_US","og_type":"article","og_title":"Embracing cellular complexity | EMBL","og_description":"Cell biologists \"underestimate the complexity\" of protein interactions, says Toby Gibson","og_url":"https:\/\/www.embl.org\/news\/science\/complexity\/","og_site_name":"EMBL","article_publisher":"https:\/\/www.facebook.com\/embl.org\/","article_published_time":"2014-07-17T16:00:57+00:00","article_modified_time":"2024-11-14T15:32:43+00:00","og_image":[{"width":620,"height":464,"url":"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2014\/07\/1407_gibson_photo.jpg","type":"image\/jpeg"}],"author":"Lindsay Brownell","twitter_card":"summary_large_image","twitter_creator":"@LindzBro","twitter_site":"@embl","twitter_misc":{"Written by":"Lindsay Brownell","Est. reading time":"5 minutes"},"schema":{"@context":"https:\/\/schema.org","@graph":[{"@type":"NewsArticle","@id":"https:\/\/www.embl.org\/news\/science\/complexity\/#article","isPartOf":{"@id":"https:\/\/www.embl.org\/news\/science\/complexity\/"},"author":{"name":"Lindsay Brownell","@id":"https:\/\/www.embl.org\/news\/#\/schema\/person\/93b4023d898e31d430ebb837620c8786"},"headline":"Embracing cellular complexity","datePublished":"2014-07-17T16:00:57+00:00","dateModified":"2024-11-14T15:32:43+00:00","mainEntityOfPage":{"@id":"https:\/\/www.embl.org\/news\/science\/complexity\/"},"wordCount":964,"publisher":{"@id":"https:\/\/www.embl.org\/news\/#organization"},"image":{"@id":"https:\/\/www.embl.org\/news\/science\/complexity\/#primaryimage"},"thumbnailUrl":"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2014\/07\/1407_gibson_photo.jpg","keywords":["cell biology","gibson","heidelberg","methods","modelling","proteomics","systems biology"],"articleSection":["Science","Science &amp; Technology"],"inLanguage":"en-US"},{"@type":"WebPage","@id":"https:\/\/www.embl.org\/news\/science\/complexity\/","url":"https:\/\/www.embl.org\/news\/science\/complexity\/","name":"Embracing cellular complexity | EMBL","isPartOf":{"@id":"https:\/\/www.embl.org\/news\/#website"},"primaryImageOfPage":{"@id":"https:\/\/www.embl.org\/news\/science\/complexity\/#primaryimage"},"image":{"@id":"https:\/\/www.embl.org\/news\/science\/complexity\/#primaryimage"},"thumbnailUrl":"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2014\/07\/1407_gibson_photo.jpg","datePublished":"2014-07-17T16:00:57+00:00","dateModified":"2024-11-14T15:32:43+00:00","description":"Cell biologists \"underestimate the complexity\" of protein interactions, says Toby Gibson","inLanguage":"en-US","potentialAction":[{"@type":"ReadAction","target":["https:\/\/www.embl.org\/news\/science\/complexity\/"]}]},{"@type":"ImageObject","inLanguage":"en-US","@id":"https:\/\/www.embl.org\/news\/science\/complexity\/#primaryimage","url":"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2014\/07\/1407_gibson_photo.jpg","contentUrl":"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2014\/07\/1407_gibson_photo.jpg","width":620,"height":464,"caption":"PHOTO: PASIEKA SCIENCE PHOTO LIBRARY"},{"@type":"WebSite","@id":"https:\/\/www.embl.org\/news\/#website","url":"https:\/\/www.embl.org\/news\/","name":"European Molecular Biology Laboratory News","description":"News from the European Molecular Biology Laboratory","publisher":{"@id":"https:\/\/www.embl.org\/news\/#organization"},"alternateName":"EMBL News","potentialAction":[{"@type":"SearchAction","target":{"@type":"EntryPoint","urlTemplate":"https:\/\/www.embl.org\/news\/?s={search_term_string}"},"query-input":{"@type":"PropertyValueSpecification","valueRequired":true,"valueName":"search_term_string"}}],"inLanguage":"en-US"},{"@type":"Organization","@id":"https:\/\/www.embl.org\/news\/#organization","name":"European Molecular Biology Laboratory","alternateName":"EMBL","url":"https:\/\/www.embl.org\/news\/","logo":{"@type":"ImageObject","inLanguage":"en-US","@id":"https:\/\/www.embl.org\/news\/#\/schema\/logo\/image\/","url":"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2025\/09\/EMBL_logo_colour-1-300x144-1.png","contentUrl":"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2025\/09\/EMBL_logo_colour-1-300x144-1.png","width":300,"height":144,"caption":"European Molecular Biology Laboratory"},"image":{"@id":"https:\/\/www.embl.org\/news\/#\/schema\/logo\/image\/"},"sameAs":["https:\/\/www.facebook.com\/embl.org\/","https:\/\/x.com\/embl","https:\/\/www.instagram.com\/embl_org\/","https:\/\/www.linkedin.com\/company\/15813\/","https:\/\/www.youtube.com\/user\/emblmedia\/"]},{"@type":"Person","@id":"https:\/\/www.embl.org\/news\/#\/schema\/person\/93b4023d898e31d430ebb837620c8786","name":"Lindsay Brownell","image":{"@type":"ImageObject","inLanguage":"en-US","@id":"https:\/\/www.embl.org\/news\/#\/schema\/person\/image\/","url":"https:\/\/secure.gravatar.com\/avatar\/662a20dd8b58b2d277ac0cbb3e90b1579ef59dd4112b7004ec0b07dcc0a948c1?s=96&d=mm&r=g","contentUrl":"https:\/\/secure.gravatar.com\/avatar\/662a20dd8b58b2d277ac0cbb3e90b1579ef59dd4112b7004ec0b07dcc0a948c1?s=96&d=mm&r=g","caption":"Lindsay Brownell"},"description":"Lindsay Brownell was a science writing intern on EMBL\u2019s communications team. She once climbed into an air duct at midnight while interviewing members of MIT\u2019s hacking community for radio.","sameAs":["https:\/\/x.com\/LindzBro"],"url":"https:\/\/www.embl.org\/news\/author\/lindsay-brownell\/"}]}},"field_target_display":"embl","field_article_language":{"value":"english","label":"English"},"fimg_url":"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2014\/07\/1407_gibson_photo.jpg","featured_image_src":"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2014\/07\/1407_gibson_photo.jpg","_links":{"self":[{"href":"https:\/\/www.embl.org\/news\/wp-json\/wp\/v2\/posts\/1077","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www.embl.org\/news\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/www.embl.org\/news\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/www.embl.org\/news\/wp-json\/wp\/v2\/users\/7"}],"replies":[{"embeddable":true,"href":"https:\/\/www.embl.org\/news\/wp-json\/wp\/v2\/comments?post=1077"}],"version-history":[{"count":7,"href":"https:\/\/www.embl.org\/news\/wp-json\/wp\/v2\/posts\/1077\/revisions"}],"predecessor-version":[{"id":19771,"href":"https:\/\/www.embl.org\/news\/wp-json\/wp\/v2\/posts\/1077\/revisions\/19771"}],"wp:featuredmedia":[{"embeddable":true,"href":"https:\/\/www.embl.org\/news\/wp-json\/wp\/v2\/media\/1078"}],"wp:attachment":[{"href":"https:\/\/www.embl.org\/news\/wp-json\/wp\/v2\/media?parent=1077"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/www.embl.org\/news\/wp-json\/wp\/v2\/categories?post=1077"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/www.embl.org\/news\/wp-json\/wp\/v2\/tags?post=1077"},{"taxonomy":"embl_taxonomy","embeddable":true,"href":"https:\/\/www.embl.org\/news\/wp-json\/wp\/v2\/embl_taxonomy?post=1077"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}