{"id":200,"date":"2020-01-17T14:22:30","date_gmt":"2020-01-17T14:22:30","guid":{"rendered":"http:\/\/heidarsson.wpengine.com\/?page_id=200"},"modified":"2026-01-28T19:12:13","modified_gmt":"2026-01-28T19:12:13","slug":"publications","status":"publish","type":"page","link":"https:\/\/heidarsson.hi.is\/?page_id=200","title":{"rendered":"Publications"},"content":{"rendered":"\t\t
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Proteasomal control of transcription factors: Mechanisms, regulation and dysregulation<\/p>\n

Larsen FB, Kragelund BB, Lindorff-Larsen K, <\/span>Heidarsson PO, and Hartmann-Petersen R (2026) Cell Mol Life Sci<\/em> (Accepted).<\/span><\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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Pathogenic mechanism of the K141E mutation in HSPB8: Insights from smFRET and simulations<\/a><\/p>

MontePietra D, Bjarnason S, \u00d3skarsson KR, Cecconi C, Carra S<\/span>, Heidarsson PO, and Brancolini G (2024) Cell Stress Chaperones<\/em>\u00a030(4), 100086.<\/span><\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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Novel mechanisms of MITF regulation identified in a mouse suppressor screen<\/a><\/p>

Vua HN, Valdimarsson MM, Sigurbj\u00f6rnsd\u00f3ttir S, Bergsteinsd\u00f3ttir K, Debbache J, Bismuth K, <\/span>Swing DA, Hallsson JH, Larue L, Arnheiter H,Copeland NG, Jenkins NA, Heidarsson PO, and Steingr\u00edmsson E (2024) EMBO Reports <\/em><\/span>25, 4252 – 4280. (PDF<\/a>)<\/span><\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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DNA binding redistributes activation domain ensemble and accessibility in pioneer factor Sox2<\/a>\u00a0<\/span><\/p>

Bjarnason S, McIvor JAP, Prestel A, Dem\u00e9ny KS, Bullerjahn JT, Kragelund BB, Mercadante D, and Heidarsson PO (2024) Nat Commun<\/em> 15, 1445.\u00a0<\/span>(PDF<\/a><\/span>)<\/span><\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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PED in 2024: Improving the community deposition of structural ensembles for intrinsically disordered proteins<\/a><\/p>

Ghafouri H, Lazar T, Del Conti A, Ku LGT, PED Consortium, Tompa P, Tosatto SCE, Monzon AM (2023) Nucleic Acids Res, <\/em>gkad947,<\/em>\u00a0https:\/\/doi.org\/10.1093\/nar\/gkad947<\/a><\/span>. (PDF<\/a>)<\/span><\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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Human small heat-shock protein B8 inhibits protein aggregation without affecting the native folding process<\/a><\/p>

Choudhary D, Mediani L, Avallaneda MJ, Bjarnason S, Alberti S, Boczek EE, Heidarsson PO, Mossa A, Carra S, Tans SJ, Cecconi C (2023)\u00a0<\/span>J Am Chem Soc <\/i>145(28)<\/b>, <\/i>15188-15196. (PDF<\/a>)<\/span><\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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Multifunctional intrinsically disordered regions in transcription factors<\/a><\/p>

M\u00e1r M, Nitsenko K & Heidarsson PO (2023)<\/span>Chemistry \u2013 A European Journal,<\/i>\u00a0doi:10.1002\/chem.202203369.\u00a0<\/span>(<\/span>PDF<\/a>)<\/span><\/p>

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The chemical features of intrinsically disordered regions in transcription factors that endow them with structural plasticity central to their functions are dissected in this Review. We highlight recent studies that illustrate the involvement of disordered regions in processes such as protein interactions, DNA binding and specificity, chromatin opening, and phase separation.\u00a0<\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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Release of linker histone from the nucleosome driven by polyelectrolyte competition with a disordered protein<\/a><\/p>

Heidarsson PO, Mercadante D, Sottini A, Nettels D, Borgia M, Borgia A, Kilic S, Fierz B, Best RB, Schuler B (2022) Nat Chem<\/em> 14<\/strong>, 224-231.\u00a0(<\/span>PDF<\/a>)<\/span><\/p>

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In this paper we show that histone H1 binds nucleosomes fast and tight yet remains disordered, allowing a disordered chaperone to facilitate dissociation by forming a ternary complex.\u00a0<\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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Protein intrinsic disorder on a dynamic nucleosomal landscape<\/span><\/a><\/p>

Bjarnason S, Ruidiaz SF, McIvor J, Mercadante D, and Heidarsson PO, (2021) Prog Mol Biol Transl Sci<\/em> 183<\/strong>, 295-354.<\/p>

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In this chapter we present and discuss the crucial role of disordered interactions in the nuclear milieu. (PDF<\/a>)<\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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From folding to function: Complex macromolecular reactions unraveled one-by-one with optical tweezers<\/a><\/p>

Heidarsson PO, Cecconi C (2021) Essays Biochem, <\/i>EBC20200024. doi: 10.1042\/EBC20200024. Epub ahead of print. PMID: 33438724.<\/p>

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This mini-review explains the basic principles of optical tweezers and highlights some recent studies on complex biological phenomena. (PDF<\/a>)<\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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Polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes<\/a><\/p>

Sottini A, Borgia A, Borgia M, Bugge K, Nettels D, Chowdhury A, Heidarsson PO, Zosel F, Best RB, Kragelund BB, Schuler B (2020) Nat Commun <\/i>11<\/strong>, 5736.<\/p>

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The highly disordered complex between histone H1 and prothymosin alpha switches from slow to fast association\/dissociation kinetics with higher concentrations due to formation of transient ternary complexes, keeping this regulatory system highly responsive despite extremely high affinites. (PDF<\/a>)<\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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Effects of Ligand Binding on the Energy Landscape of Acyl-CoA-Binding Protein<\/a><\/p>

Sonar P, Bellucci L, Mossa A, Heidarsson PO, Kragelund BB, Cecconi C (2020) Biophys J<\/em> 119<\/b>(9), 1821-1832.<\/p>

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Using the well-studied acyl-CoA binding protein, we show that the protein retains its unusual deformability after binding a natural ligand, which may be important for its transporting functions. (PDF<\/a>)<\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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DISORDER IN A TWO-DOMAIN NEURONAL CA 2+-BINDING PROTEIN REGULATES DOMAIN STABILITY AND DYNAMICS USING LIGAND MIMICRY<\/a><\/p>

Staby L, Kemplen KR, Stein A, Ploug M, Clarke J, Skriver K, Heidarsson PO,<\/span> Kragelund BB (2020)\u00a0Cell Mol Life Sci<\/em> 78<\/strong>, 2263\u20132278.<\/p>

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An investigation on the interplay of order and disorder in neuronal calcium sensor-1 reveals a critical ligand-mimicking motif for order-disorder communication. (PDF<\/a>)<\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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BINDING WITHOUT FOLDING- THE BIOMOLECULAR FUNCTION OF DISORDERED POLYELECTROLYTE COMPLEXES<\/a><\/p>

Schuler B, Borgia A, Borgia M, Heidarsson PO, Holmstrom ED, Nettels D, Sottini A (2020)\u00a0Curr Opin Struct Biol<\/em>\u00a060<\/strong>, 66-76.<\/p>

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A review article about the emerging principles of IDP binding without folding and future perspectives of merging experiment and simulations to tackle these systems. (PDF<\/a>)<\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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THE COMPLEX CONFORMATIONAL DYNAMICS OF A NEURONAL CALCIUM SENSOR: A SINGLE MOLECULE PERSPECTIVE<\/a><\/p>

Choudhary D, Kragelund BB, Heidarsson PO, Cecconi C (2018)\u00a0Front Mol Neurosci<\/em>\u00a011<\/strong>, 1-8.<\/p>

\u00a0<\/p>

This review summarizes what we have learned about the folding of a neuronal calcium sensor protein on the single-molecule level. (PDF<\/a>)<\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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Extreme disorder in an ultrahigh-affinity protein complex<\/a><\/p>\n

Borgia A, Borgia M, Bugge K, Kissling VM, Heidarsson PO, Fernandez CB, Sottini A, Soranno A, Bucholzer KJ, Nettels D, Kragelund BB, Best RB, Schuler B (2018) Nature<\/em> 555<\/strong>, 61-66.    <\/p>


<\/p>\n

Here we reveal a novel interaction mechanism for proteins: Two oppositely charged disordered proteins form a picomolar-affinity complex yet remain fully disordered and dynamic.<\/p>\n

See News & Views by Berlow & Wright (2018): \u201cTight complexes from disordered proteins<\/a>” Nature<\/em> 555<\/strong>, 37-38. (PDF<\/a>)<\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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SINGLE-MOLECULE FOLDING MECHANISMS OF THE APO AND MG2+-BOUND STATES OF HUMAN NEURONAL CALCIUM SENSOR-1<\/a><\/p>

Naqvi MM, Heidarsson PO, Otazo MR, Mossa A, Kragelund BB, Cecconi C (2015)\u00a0Biophys J<\/em>\u00a0109(1)<\/strong>, 113-123.\u00a0\u00a0\u00a0<\/p>

Front cover of issue showcased our paper. <\/strong>(PDF<\/a>)<\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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DIRECT SINGLE-MOLECULE OBSERVATION OF CALCIUM-DEPENDENT MISFOLDING IN HUMAN NEURONAL CALCIUM SENSOR-1<\/a><\/p>

Heidarsson PO, Naqvi MM, Otazo MR, Mossa A, Kragelund BB, Cecconi C (2014)\u00a0Proc Natl Acad Sci USA<\/em>\u00a0111(36)<\/strong>, 13069-13074. (PDF<\/a>)<\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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PICK1 PROMISCUITY RELIES ON ALTERNATING BINDING MODES FOR NON-TYPE II PDZ DOMAIN LIGANDS<\/a><\/p>

Erlendsson S, Rathje M, Heidarsson PO, Poulsen FM, Madsen KL, Teilum K and Gether U (2014)\u00a0J Biol Chem<\/em>\u00a0289(36)<\/strong>, 25327-25340. (PDF<\/a>)<\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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EXPLORING THE MINIMALLY FRUSTRATED ENERGY LANDSCAPE OF UNFOLDED ACBP<\/a><\/p>

Ozenne V, Noel J, Heidarsson PO, Brander S, Poulsen FM, Ringkj\u00f8bing-Jensen M, Kragelund BB, Blackledge M, Danielsson J (2014)\u00a0J Mol Biol<\/em>\u00a0426(3)<\/strong>, 722-734. (PDF<\/a>)<\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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SINGLE-MOLECULE FOLDING MECHANISM OF AN EF-HAND NEURONAL CALCIUM SENSOR<\/a><\/p>

Heidarsson PO, Otazo MR, Bellucci L, Mossa A, Imparato A, Paci E, Corni S, Di Felice R, Kragelund BB, Cecconi C (2013)\u00a0Structure<\/em>\u00a021<\/strong>, 1812-1821. (PDF<\/a>)<\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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SOLUTION PROPERTIES OF THE ARCHAEAL CRISPR DNA REPEAT-BINDING HOMEODOMAIN PROTEIN CBP2<\/a><\/p>

Kenchappa CS, Heidarsson PO, Kragelund BB, Garrett RA, Poulsen FM (2013)\u00a0Nucl Acids Res<\/em>\u00a04<\/strong>, 3424-3435. (PDF<\/a>)<\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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CONFORMATIONAL DYNAMICS OF SINGLE PROTEIN MOLECULES STUDIED WITH DIRECTED MECHANICAL MANIPULATION<\/a><\/p>

Heidarsson PO, Naqvi MN, Sonar P, Valpapuram I, Cecconi C (2013) Adv Protein Chem Struct Biol<\/em> 92<\/strong>, 93-133. (PDF<\/a>)<\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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A HIGHLY COMPLIANT PROTEIN NATIVE STATE WITH A SPONTANEOUS-LIKE MECHANICAL UNFOLDING PATHWAY<\/a><\/p>

Heidarsson PO, Valpapuram I, Camilloni C, Imparato M, Tiana G, Poulsen FM, Kragelund BB, Cecconi C (2012)\u00a0J Am Chem Soc<\/em>\u00a0134(41)<\/strong>, 17068-17065. (PDF<\/a>)<\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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THE C-TERMINAL TAIL OF HUMAN NEURONAL CALCIUM SENSOR 1 REGULATES THE CONFORMATIONAL STABILITY OF THE CA2+ ACTIVATED STATE<\/a><\/p>

Heidarsson PO, Bjerrum-Bohr I, Jensen GA, Pongs O, Finn BE, Poulsen FM, Kragelund BB (2012)\u00a0J Mol Biol<\/em>\u00a0417<\/strong>, 51-64. (PDF<\/a>)<\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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EXPLORING FOLDING PATHWAYS OF SINGLE PROTEINS USING MECHANICAL MANIPULATION<\/a><\/p>

Heidarsson PO and Cecconi C\u00a0(2012) AIP Conf Proc<\/em> 1456<\/strong>, 201-206. (PDF<\/a>)<\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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STRUCTURAL FEATURES AND DYNAMICS OF A COLD-ADAPTED ALKALINE PHOSPHATASE STUDIED WITH EPR SPECTROSCOPY<\/a><\/p>

Heidarsson PO, Sigurdsson ST, \u00c1sgeirsson B (2009)\u00a0FEBS J<\/em>\u00a0276<\/strong>, 2725-2735. (PDF<\/a>)<\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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EFFECT OF ACTIVE SITE MUTATION ON CATALYSIS AND BACKBONE DYNAMICS IN A COLD-ADAPTED ENZYME<\/p>

Heidarsson PO and \u00c1sgeirsson B (2009) Raust-Journal of applied sciences<\/em>
and mathematics<\/em>\u00a06<\/em><\/strong>, 79-85 (in Icelandic).\u00a0<\/p>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t

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Publications Proteasomal control of transcription factors: Mechanisms, regulation and dysregulation Larsen FB, Kragelund BB, Lindorff-Larsen K, Heidarsson PO, and Hartmann-Petersen R (2026) Cell Mol Life Sci (Accepted). Pathogenic mechanism of the K141E mutation in HSPB8: Insights from smFRET and simulations MontePietra D, Bjarnason S, \u00d3skarsson KR, Cecconi C, Carra S, Heidarsson PO, and Brancolini G (2024) […]<\/p>\n","protected":false},"author":1,"featured_media":0,"parent":0,"menu_order":2,"comment_status":"closed","ping_status":"closed","template":"elementor_header_footer","meta":{"footnotes":""},"class_list":["post-200","page","type-page","status-publish","hentry"],"brizy_media":[],"_links":{"self":[{"href":"https:\/\/heidarsson.hi.is\/index.php?rest_route=\/wp\/v2\/pages\/200","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/heidarsson.hi.is\/index.php?rest_route=\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/heidarsson.hi.is\/index.php?rest_route=\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/heidarsson.hi.is\/index.php?rest_route=\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/heidarsson.hi.is\/index.php?rest_route=%2Fwp%2Fv2%2Fcomments&post=200"}],"version-history":[{"count":350,"href":"https:\/\/heidarsson.hi.is\/index.php?rest_route=\/wp\/v2\/pages\/200\/revisions"}],"predecessor-version":[{"id":2025,"href":"https:\/\/heidarsson.hi.is\/index.php?rest_route=\/wp\/v2\/pages\/200\/revisions\/2025"}],"wp:attachment":[{"href":"https:\/\/heidarsson.hi.is\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=200"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}