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Items: 1 to 20 of 43


Function, evolution, and structure of J-domain proteins.

Kampinga HH, Andreasson C, Barducci A, Cheetham ME, Cyr D, Emanuelsson C, Genevaux P, Gestwicki JE, Goloubinoff P, Huerta-Cepas J, Kirstein J, Liberek K, Mayer MP, Nagata K, Nillegoda NB, Pulido P, Ramos C, De Los Rios P, Rospert S, Rosenzweig R, Sahi C, Taipale M, Tomiczek B, Ushioda R, Young JC, Zimmermann R, Zylicz A, Zylicz M, Craig EA, Marszalek J.

Cell Stress Chaperones. 2018 Nov 26. doi: 10.1007/s12192-018-0948-4. [Epub ahead of print] Review.


Structures of ubiquitin-like (Ubl) and Hsp90-like domains of sacsin provide insight into pathological mutations.

Ménade M, Kozlov G, Trempe JF, Pande H, Shenker S, Wickremasinghe S, Li X, Hojjat H, Dicaire MJ, Brais B, McPherson PS, Wong MJH, Young JC, Gehring K.

J Biol Chem. 2018 Aug 17;293(33):12832-12842. doi: 10.1074/jbc.RA118.003939. Epub 2018 Jun 26.


Chaperones rescue the energetic landscape of mutant CFTR at single molecule and in cell.

Bagdany M, Veit G, Fukuda R, Avramescu RG, Okiyoneda T, Baaklini I, Singh J, Sovak G, Xu H, Apaja PM, Sattin S, Beitel LK, Roldan A, Colombo G, Balch W, Young JC, Lukacs GL.

Nat Commun. 2017 Aug 30;8(1):398. doi: 10.1038/s41467-017-00444-4.


Bag1 Co-chaperone Promotes TRC8 E3 Ligase-dependent Degradation of Misfolded Human Ether a Go-Go-related Gene (hERG) Potassium Channels.

Hantouche C, Williamson B, Valinsky WC, Solomon J, Shrier A, Young JC.

J Biol Chem. 2017 Feb 10;292(6):2287-2300. doi: 10.1074/jbc.M116.752618. Epub 2016 Dec 20.


Heat Shock Protein 90 kDa (Hsp90) Has a Second Functional Interaction Site with the Mitochondrial Import Receptor Tom70.

Zanphorlin LM, Lima TB, Wong MJ, Balbuena TS, Minetti CA, Remeta DP, Young JC, Barbosa LR, Gozzo FC, Ramos CH.

J Biol Chem. 2016 Sep 2;291(36):18620-31. doi: 10.1074/jbc.M115.710137. Epub 2016 Jul 8.


Function and Chemotypes of Human Hsp70 Chaperones.

Shrestha L, Young JC.

Curr Top Med Chem. 2016;16(25):2812-28. Review.


hERG quality control and the long QT syndrome.

Foo B, Williamson B, Young JC, Lukacs G, Shrier A.

J Physiol. 2016 May 1;594(9):2469-81. doi: 10.1113/JP270531. Epub 2016 Feb 9. Review.


Heat shock protein 70 inhibitors. 2. 2,5'-thiodipyrimidines, 5-(phenylthio)pyrimidines, 2-(pyridin-3-ylthio)pyrimidines, and 3-(phenylthio)pyridines as reversible binders to an allosteric site on heat shock protein 70.

Taldone T, Kang Y, Patel HJ, Patel MR, Patel PD, Rodina A, Patel Y, Gozman A, Maharaj R, Clement CC, Lu A, Young JC, Chiosis G.

J Med Chem. 2014 Feb 27;57(4):1208-24. doi: 10.1021/jm401552y. Epub 2014 Feb 18.


Heat shock protein 70 inhibitors. 1. 2,5'-thiodipyrimidine and 5-(phenylthio)pyrimidine acrylamides as irreversible binders to an allosteric site on heat shock protein 70.

Kang Y, Taldone T, Patel HJ, Patel PD, Rodina A, Gozman A, Maharaj R, Clement CC, Patel MR, Brodsky JL, Young JC, Chiosis G.

J Med Chem. 2014 Feb 27;57(4):1188-207. doi: 10.1021/jm401551n. Epub 2014 Feb 18.


A G protein-coupled receptor and the intracellular synthase of its agonist functionally cooperate.

Binda C, Génier S, Cartier A, Larrivée JF, Stankova J, Young JC, Parent JL.

J Cell Biol. 2014 Feb 3;204(3):377-93. doi: 10.1083/jcb.201304015.


Hsp70 cochaperones HspBP1 and BAG-1M differentially regulate steroid hormone receptor function.

Knapp RT, Wong MJ, Kollmannsberger LK, Gassen NC, Kretzschmar A, Zschocke J, Hafner K, Young JC, Rein T.

PLoS One. 2014 Jan 14;9(1):e85415. doi: 10.1371/journal.pone.0085415. eCollection 2014.


Identification of an allosteric pocket on human hsp70 reveals a mode of inhibition of this therapeutically important protein.

Rodina A, Patel PD, Kang Y, Patel Y, Baaklini I, Wong MJ, Taldone T, Yan P, Yang C, Maharaj R, Gozman A, Patel MR, Patel HJ, Chirico W, Erdjument-Bromage H, Talele TT, Young JC, Chiosis G.

Chem Biol. 2013 Dec 19;20(12):1469-80. doi: 10.1016/j.chembiol.2013.10.008. Epub 2013 Nov 14.


The DNAJA2 substrate release mechanism is essential for chaperone-mediated folding.

Baaklini I, Wong MJ, Hantouche C, Patel Y, Shrier A, Young JC.

J Biol Chem. 2012 Dec 7;287(50):41939-54. doi: 10.1074/jbc.M112.413278. Epub 2012 Oct 22.


Interaction between the human mitochondrial import receptors Tom20 and Tom70 in vitro suggests a chaperone displacement mechanism.

Fan AC, Kozlov G, Hoegl A, Marcellus RC, Wong MJ, Gehring K, Young JC.

J Biol Chem. 2011 Sep 16;286(37):32208-19. doi: 10.1074/jbc.M111.280446. Epub 2011 Jul 19.


OEP61 is a chaperone receptor at the plastid outer envelope.

von Loeffelholz O, Kriechbaumer V, Ewan RA, Jonczyk R, Lehmann S, Young JC, Abell BM.

Biochem J. 2011 Aug 15;438(1):143-53. doi: 10.1042/BJ20110448.


Regulation of activation-induced deaminase stability and antibody gene diversification by Hsp90.

Orthwein A, Patenaude AM, Affar el B, Lamarre A, Young JC, Di Noia JM.

J Exp Med. 2010 Nov 22;207(12):2751-65. doi: 10.1084/jem.20101321. Epub 2010 Nov 1.


Function of cytosolic chaperones in Tom70-mediated mitochondrial import.

Fan AC, Young JC.

Protein Pept Lett. 2011 Feb;18(2):122-31. Review.


Peripheral protein quality control removes unfolded CFTR from the plasma membrane.

Okiyoneda T, Barrière H, Bagdány M, Rabeh WM, Du K, Höhfeld J, Young JC, Lukacs GL.

Science. 2010 Aug 13;329(5993):805-10. doi: 10.1126/science.1191542. Epub 2010 Jul 1.


Human mitochondrial import receptor Tom70 functions as a monomer.

Fan AC, Gava LM, Ramos CH, Young JC.

Biochem J. 2010 Aug 1;429(3):553-63. doi: 10.1042/BJ20091855.

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