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000267345 005__ 20190806130832.0
000267345 022__ $$a0969-2126
000267345 022__ $$a1878-4186
000267345 02470 $$a000463163300003$$2isi
000267345 0247_ $$a10.1016/j.str.2019.01.003$$2doi
000267345 037__ $$aARTICLE
000267345 245__ $$aAllostery in Its Many Disguises: From Theory to Applications
000267345 260__ $$c2019$$aCambridge$$bCELL PRESS
000267345 269__ $$a2019-04-02
000267345 336__ $$aReviews
000267345 520__ $$aAllosteric regulation plays an important role in many biological processes, such as signal transduction, transcriptional regulation, andmetabolism. Allostery is rooted in the fundamental physical properties of macromolecular systems, but its underlying mechanisms are still poorly understood. A collection of contributions to a recent interdisciplinary CECAM(Center Europeen de Calcul Atomique et Moleculaire) workshop is used here to provide an overview of the progress and remaining limitations in the understanding of the mechanistic foundations of allostery gained from computational and experimental analyses of real protein systems and model systems. The main conceptual frameworks instrumental in driving the field are discussed. We illustrate the role of these frameworks in illuminating molecular mechanisms and explaining cellular processes, and describe some of their promising practical applications in engineering molecular sensors and informing drug design efforts.
000267345 650__ $$aBiochemistry & Molecular Biology
000267345 650__ $$aBiophysics
000267345 650__ $$aCell Biology
000267345 650__ $$aBiochemistry & Molecular Biology
000267345 650__ $$aBiophysics
000267345 650__ $$aCell Biology
000267345 6531_ $$aconformational-changes
000267345 6531_ $$adynamic allostery
000267345 6531_ $$anuclear receptors
000267345 6531_ $$achemical rescue
000267345 6531_ $$aligand-binding
000267345 6531_ $$aprotein
000267345 6531_ $$amodulation
000267345 6531_ $$amechanisms
000267345 6531_ $$anetwork
000267345 6531_ $$apathway
000267345 700__ $$aWodak, Shoshana J.
000267345 700__ $$aPaci, Emanuele
000267345 700__ $$aDokholyan, Nikolay V.
000267345 700__ $$aBerezovsky, Igor N.
000267345 700__ $$aHorovitz, Amnon
000267345 700__ $$g205680$$aLi, Jing$$0246995
000267345 700__ $$aHilser, Vincent J.
000267345 700__ $$aBehar, Ivet
000267345 700__ $$aKaranicolas, John
000267345 700__ $$aStock, Gerhard
000267345 700__ $$aHamm, Peter
000267345 700__ $$aStote, Roland H.
000267345 700__ $$aEberhardt, Jerome
000267345 700__ $$aChebaro, Yassmine
000267345 700__ $$aDejaegere, Annick
000267345 700__ $$aCecchini, Marco
000267345 700__ $$aChangeux, Jean-Pierre
000267345 700__ $$aBolhuis, Peter G.
000267345 700__ $$aVreede, Jocelyne
000267345 700__ $$aFaccioli, Pietro
000267345 700__ $$aOrioli, Simone
000267345 700__ $$g269924$$aRavasio, Riccardo$$0249925
000267345 700__ $$aYen, Le
000267345 700__ $$aBrito, Carolina
000267345 700__ $$g263767$$aWyart, Matthieu$$0249400
000267345 700__ $$aGkeka, Paraskevi
000267345 700__ $$aRivalta, Ivan
000267345 700__ $$g212941$$aPalermo, Giulia$$0246063
000267345 700__ $$aMccammon, J. Andrew
000267345 700__ $$aPanecka-Hofman, Joanna
000267345 700__ $$aWade, Rebecca C.
000267345 700__ $$aDi Pizio, Antonella
000267345 700__ $$aNiv, Masha Y.
000267345 700__ $$aNussinov, Ruth
000267345 700__ $$aTsai, Chung-Jung
000267345 700__ $$aJang, Hyunbum
000267345 700__ $$aPadhorny, Dzmitry
000267345 700__ $$aKozakov, Dima
000267345 700__ $$aMcleish, Tom
000267345 773__ $$k4$$j27$$q566-578$$tStructure
000267345 8560_ $$fcorinne.weibel@epfl.ch
000267345 909C0 $$zPasquier, Simon$$0252562$$yApproved$$pPCSL$$xU13087$$mcorinne.weibel@epfl.ch
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000267345 910C0 $$msylvie.thomet@epfl.ch$$zGrolimund, Raphael$$xU10406$$yDeclined$$0252184$$pLIA
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000267345 973__ $$aEPFL$$sPUBLISHED$$rREVIEWED
000267345 980__ $$aREVIEW
000267345 980__ $$aWoS
000267345 981__ $$aoverwrite
000267345 999C0 $$zBorel, Alain$$xU2$$pLCBC$$mmurat.kilic@epfl.ch$$0252093