Walid Houry - Publications

Affiliations: 
Biochemistry University of Toronto, Toronto, ON, Canada 
Website:
http://biochemistry.utoronto.ca/houry/Labpage/index1.html

77 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2016 Chan SW, Yau J, Ing C, Liu K, Farber P, Won A, Bhandari V, Kara-Yacoubian N, Seraphim TV, Chakrabarti N, Kay LE, Yip CM, Pomès R, Sharpe S, Houry WA. Mechanism of Amyloidogenesis of a Bacterial AAA+ Chaperone. Structure (London, England : 1993). PMID 27265850 DOI: 10.1016/j.str.2016.05.002  0.52
2016 Ewens CA, Su M, Zhao L, Nano N, Houry WA, Southworth DR. Architecture and Nucleotide-Dependent Conformational Changes of the Rvb1-Rvb2 AAA+ Complex Revealed by Cryoelectron Microscopy. Structure (London, England : 1993). PMID 27112599 DOI: 10.1016/j.str.2016.03.018  0.52
2016 Kandiah E, Carriel D, Perard J, Malet H, Bacia M, Liu K, Chan SW, Houry WA, Ollagnier de Choudens S, Elsen S, Gutsche I. Structural insights into the Escherichia coli lysine decarboxylases and molecular determinants of interaction with the AAA+ ATPase RavA. Scientific Reports. 6: 24601. PMID 27080013 DOI: 10.1038/srep24601  0.52
2016 Goodreid JD, Janetzko J, Santa Maria JP, Wong KS, Leung E, Eger BT, Bryson S, Pai EF, Gray-Owen SD, Walker S, Houry WA, Batey RA. Development and Characterization of Potent Cyclic Acyldepsipeptide Analogues with Increased Antimicrobial Activity. Journal of Medicinal Chemistry. 59: 624-46. PMID 26818454 DOI: 10.1021/acs.jmedchem.5b01451  0.52
2015 Cole A, Wang Z, Coyaud E, Voisin V, Gronda M, Jitkova Y, Mattson R, Hurren R, Babovic S, Maclean N, Restall I, Wang X, Jeyaraju DV, Sukhai MA, Prabha S, ... ... Houry WA, et al. Inhibition of the Mitochondrial Protease ClpP as a Therapeutic Strategy for Human Acute Myeloid Leukemia. Cancer Cell. 27: 864-76. PMID 26058080 DOI: 10.1016/j.ccell.2015.05.004  0.52
2015 Jeganathan A, Leong V, Zhao L, Huen J, Nano N, Houry WA, Ortega J. Yeast rvb1 and rvb2 proteins oligomerize as a conformationally variable dodecamer with low frequency. Journal of Molecular Biology. 427: 1875-86. PMID 25636407 DOI: 10.1016/j.jmb.2015.01.010  0.52
2015 Vlasblom J, Zuberi K, Rodriguez H, Arnold R, Gagarinova A, Deineko V, Kumar A, Leung E, Rizzolo K, Samanfar B, Chang L, Phanse S, Golshani A, Greenblatt JF, Houry WA, et al. Novel function discovery with GeneMANIA: a new integrated resource for gene function prediction in Escherichia coli. Bioinformatics (Oxford, England). 31: 306-10. PMID 25316676 DOI: 10.1093/bioinformatics/btu671  0.52
2014 Goodreid JD, Wong K, Leung E, McCaw SE, Gray-Owen SD, Lough A, Houry WA, Batey RA. Total synthesis and antibacterial testing of the A54556 cyclic acyldepsipeptides isolated from Streptomyces hawaiiensis. Journal of Natural Products. 77: 2170-81. PMID 25255326 DOI: 10.1021/np500158q  0.52
2014 Malet H, Liu K, El Bakkouri M, Chan SW, Effantin G, Bacia M, Houry WA, Gutsche I. Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins. Elife. 3: e03653. PMID 25097238 DOI: 10.7554/eLife.03653  0.52
2014 Kakihara Y, Makhnevych T, Zhao L, Tang W, Houry WA. Nutritional status modulates box C/D snoRNP biogenesis by regulated subcellular relocalization of the R2TP complex. Genome Biology. 15: 404. PMID 25060708 DOI: 10.1186/s13059-014-0404-4  0.52
2014 Liu K, Ologbenla A, Houry WA. Dynamics of the ClpP serine protease: a model for self-compartmentalized proteases. Critical Reviews in Biochemistry and Molecular Biology. 49: 400-12. PMID 24915503 DOI: 10.3109/10409238.2014.925421  0.52
2014 Babu M, Arnold R, Bundalovic-Torma C, Gagarinova A, Wong KS, Kumar A, Stewart G, Samanfar B, Aoki H, Wagih O, Vlasblom J, Phanse S, Lad K, Yeou Hsiung Yu A, Graham C, ... ... Houry WA, et al. Quantitative genome-wide genetic interaction screens reveal global epistatic relationships of protein complexes in Escherichia coli. Plos Genetics. 10: e1004120. PMID 24586182 DOI: 10.1371/journal.pgen.1004120  0.52
2014 Wong KS, Snider JD, Graham C, Greenblatt JF, Emili A, Babu M, Houry WA. The MoxR ATPase RavA and its cofactor ViaA interact with the NADH:ubiquinone oxidoreductase I in Escherichia coli. Plos One. 9: e85529. PMID 24454883 DOI: 10.1371/journal.pone.0085529  0.52
2013 Kamano Y, Saeki M, Egusa H, Kakihara Y, Houry WA, Yatani H, Kamisaki Y. PIH1D1 interacts with mTOR complex 1 and enhances ribosome RNA transcription. Febs Letters. 587: 3303-8. PMID 24036451 DOI: 10.1016/j.febslet.2013.09.001  0.52
2013 Saeki M, Egusa H, Kamano Y, Kakihara Y, Houry WA, Yatani H, Noguchi S, Kamisaki Y. Exosome-bound WD repeat protein Monad inhibits breast cancer cell invasion by degrading amphiregulin mRNA. Plos One. 8: e67326. PMID 23844004 DOI: 10.1371/journal.pone.0067326  0.52
2013 Kanjee U, Houry WA. Mechanisms of acid resistance in Escherichia coli. Annual Review of Microbiology. 67: 65-81. PMID 23701194 DOI: 10.1146/annurev-micro-092412-155708  0.52
2013 Nano N, Houry WA. Chaperone-like activity of the AAA+ proteins Rvb1 and Rvb2 in the assembly of various complexes. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 368: 20110399. PMID 23530256 DOI: 10.1098/rstb.2011.0399  0.52
2013 Rosenbaum J, Baek SH, Dutta A, Houry WA, Huber O, Hupp TR, Matias PM. The emergence of the conserved AAA+ ATPases Pontin and Reptin on the signaling landscape. Science Signaling. 6: mr1. PMID 23482663 DOI: 10.1126/scisignal.2003906  0.52
2013 Makhnevych T, Houry WA. The control of spindle length by Hsp70 and Hsp110 molecular chaperones. Febs Letters. 587: 1067-72. PMID 23434584 DOI: 10.1016/j.febslet.2013.02.018  0.52
2013 El Bakkouri M, Rathore S, Calmettes C, Wernimont AK, Liu K, Sinha D, Asad M, Jung P, Hui R, Mohmmed A, Houry WA. Structural insights into the inactive subunit of the apicoplast-localized caseinolytic protease complex of Plasmodium falciparum. The Journal of Biological Chemistry. 288: 1022-31. PMID 23192353 DOI: 10.1074/jbc.M112.416560  0.52
2013 Liu K, Houry WA. Chaperones and proteases of plasmodium falciparum Heat Shock Proteins of Malaria. 161-187. DOI: 10.1007/978-94-007-7438-4_9  0.52
2012 Paci A, Liu XH, Huang H, Lim A, Houry WA, Zhao R. The stability of the small nucleolar ribonucleoprotein (snoRNP) assembly protein Pih1 in Saccharomyces cerevisiae is modulated by its C terminus. The Journal of Biological Chemistry. 287: 43205-14. PMID 23139418 DOI: 10.1074/jbc.M112.408849  0.52
2012 Makhnevych T, Wong P, Pogoutse O, Vizeacoumar FJ, Greenblatt JF, Emili A, Houry WA. Hsp110 is required for spindle length control. The Journal of Cell Biology. 198: 623-36. PMID 22908312 DOI: 10.1083/jcb.201111105  0.52
2012 Kanjee U, Ogata K, Houry WA. Direct binding targets of the stringent response alarmone (p)ppGpp. Molecular Microbiology. 85: 1029-43. PMID 22812515 DOI: 10.1111/j.1365-2958.2012.08177.x  0.52
2012 Wong KS, Houry WA. Novel structural and functional insights into the MoxR family of AAA+ ATPases. Journal of Structural Biology. 179: 211-21. PMID 22491058 DOI: 10.1016/j.jsb.2012.03.010  0.52
2012 Thibault G, Houry WA. Role of the N-terminal domain of the chaperone ClpX in the recognition and degradation of lambda phage protein O. The Journal of Physical Chemistry. B. 116: 6717-24. PMID 22360725 DOI: 10.1021/jp212024b  0.52
2012 Jiménez B, Ugwu F, Zhao R, Ortí L, Makhnevych T, Pineda-Lucena A, Houry WA. Structure of minimal tetratricopeptide repeat domain protein Tah1 reveals mechanism of its interaction with Pih1 and Hsp90. The Journal of Biological Chemistry. 287: 5698-709. PMID 22179618 DOI: 10.1074/jbc.M111.287458  0.52
2012 Makhnevych T, Houry WA. The role of Hsp90 in protein complex assembly. Biochimica Et Biophysica Acta. 1823: 674-82. PMID 21945180 DOI: 10.1016/j.bbamcr.2011.09.001  0.52
2012 Kakihara Y, Houry WA. The R2TP complex: discovery and functions. Biochimica Et Biophysica Acta. 1823: 101-7. PMID 21925213 DOI: 10.1016/j.bbamcr.2011.08.016  0.52
2011 Kanjee U, Gutsche I, Ramachandran S, Houry WA. The enzymatic activities of the Escherichia coli basic aliphatic amino acid decarboxylases exhibit a pH zone of inhibition. Biochemistry. 50: 9388-98. PMID 21957966 DOI: 10.1021/bi201161k  0.52
2011 Leung E, Datti A, Cossette M, Goodreid J, McCaw SE, Mah M, Nakhamchik A, Ogata K, El Bakkouri M, Cheng YQ, Wodak SJ, Eger BT, Pai EF, Liu J, Gray-Owen S, ... ... Houry WA, et al. Activators of cylindrical proteases as antimicrobials: identification and development of small molecule activators of ClpP protease. Chemistry & Biology. 18: 1167-78. PMID 21944755 DOI: 10.1016/j.chembiol.2011.07.023  0.52
2011 Gong Y, Zhang Z, Houry WA. Bioinformatic approach to identify chaperone pathway relationship from large-scale interaction networks. Methods in Molecular Biology (Clifton, N.J.). 787: 189-203. PMID 21898237 DOI: 10.1007/978-1-61779-295-3_15  0.52
2011 Kanjee U, Gutsche I, Alexopoulos E, Zhao B, El Bakkouri M, Thibault G, Liu K, Ramachandran S, Snider J, Pai EF, Houry WA. Linkage between the bacterial acid stress and stringent responses: the structure of the inducible lysine decarboxylase. The Embo Journal. 30: 931-44. PMID 21278708 DOI: 10.1038/emboj.2011.5  0.52
2010 Kanjee U, Houry WA. An assay for measuring the activity of Escherichia coli inducible lysine decarboxylase. Journal of Visualized Experiments : Jove. PMID 21494223 DOI: 10.3791/2094  0.52
2010 El Bakkouri M, Gutsche I, Kanjee U, Zhao B, Yu M, Goret G, Schoehn G, Burmeister WP, Houry WA. Structure of RavA MoxR AAA+ protein reveals the design principles of a molecular cage modulating the inducible lysine decarboxylase activity. Proceedings of the National Academy of Sciences of the United States of America. 107: 22499-504. PMID 21148420 DOI: 10.1073/pnas.1009092107  0.52
2010 Cheung KL, Huen J, Kakihara Y, Houry WA, Ortega J. Alternative oligomeric states of the yeast Rvb1/Rvb2 complex induced by histidine tags. Journal of Molecular Biology. 404: 478-92. PMID 20934430 DOI: 10.1016/j.jmb.2010.10.003  0.52
2010 El Bakkouri M, Pow A, Mulichak A, Cheung KL, Artz JD, Amani M, Fell S, de Koning-Ward TF, Goodman CD, McFadden GI, Ortega J, Hui R, Houry WA. The Clp chaperones and proteases of the human malaria parasite Plasmodium falciparum. Journal of Molecular Biology. 404: 456-77. PMID 20887733 DOI: 10.1016/j.jmb.2010.09.051  0.52
2010 Kimber MS, Yu AY, Borg M, Leung E, Chan HS, Houry WA. Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. Structure (London, England : 1993). 18: 798-808. PMID 20637416 DOI: 10.1016/j.str.2010.04.008  0.52
2010 Zhao B, Houry WA. Acid stress response in enteropathogenic gammaproteobacteria: an aptitude for survival. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 88: 301-14. PMID 20453931 DOI: 10.1139/o09-182  0.52
2010 Zhao R, Leung E, Grüner S, Schapira M, Houry WA. Tamoxifen enhances the Hsp90 molecular chaperone ATPase activity. Plos One. 5: e9934. PMID 20376192 DOI: 10.1371/journal.pone.0009934  0.52
2010 Houry WA, Ortega J. AAA proteins: movers and shakers. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 88: i-iv. PMID 20162845 DOI: 10.1139/O09-906  0.52
2010 Cheung KL, Huen J, Houry WA, Ortega J. Comparison of the multiple oligomeric structures observed for the Rvb1 and Rvb2 proteins. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 88: 77-88. PMID 20130681 DOI: 10.1139/o09-159  0.52
2010 Huen J, Kakihara Y, Ugwu F, Cheung KL, Ortega J, Houry WA. Rvb1-Rvb2: essential ATP-dependent helicases for critical complexes. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 88: 29-40. PMID 20130677 DOI: 10.1139/o09-122  0.52
2010 Costanzo M, Baryshnikova A, Bellay J, Kim Y, Spear ED, Sevier CS, Ding H, Koh JL, Toufighi K, Mostafavi S, Prinz J, St Onge RP, VanderSluis B, Makhnevych T, Vizeacoumar FJ, ... ... Houry WA, et al. The genetic landscape of a cell. Science (New York, N.Y.). 327: 425-31. PMID 20093466 DOI: 10.1126/science.1180823  0.52
2009 Gong Y, Kakihara Y, Krogan N, Greenblatt J, Emili A, Zhang Z, Houry WA. An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell. Molecular Systems Biology. 5: 275. PMID 19536198 DOI: 10.1038/msb.2009.26  0.52
2008 Alexopoulos E, Kanjee U, Snider J, Houry WA, Pai EF. Crystallization and preliminary X-ray analysis of the inducible lysine decarboxylase from Escherichia coli. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 64: 700-6. PMID 18678936 DOI: 10.1107/S1744309108018757  0.52
2008 Snider J, Thibault G, Houry WA. The AAA+ superfamily of functionally diverse proteins. Genome Biology. 9: 216. PMID 18466635 DOI: 10.1186/gb-2008-9-4-216  0.52
2008 Zhao R, Kakihara Y, Gribun A, Huen J, Yang G, Khanna M, Costanzo M, Brost RL, Boone C, Hughes TR, Yip CM, Houry WA. Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation. The Journal of Cell Biology. 180: 563-78. PMID 18268103 DOI: 10.1083/jcb.200709061  0.52
2008 Gribun A, Cheung KL, Huen J, Ortega J, Houry WA. Yeast Rvb1 and Rvb2 are ATP-dependent DNA helicases that form a heterohexameric complex. Journal of Molecular Biology. 376: 1320-33. PMID 18234224 DOI: 10.1016/j.jmb.2007.12.049  0.52
2008 Snider J, Houry WA. AAA+ proteins: diversity in function, similarity in structure. Biochemical Society Transactions. 36: 72-7. PMID 18208389 DOI: 10.1042/BST0360072  0.52
2007 Yu AY, Houry WA. ClpP: a distinctive family of cylindrical energy-dependent serine proteases. Febs Letters. 581: 3749-57. PMID 17499722 DOI: 10.1016/j.febslet.2007.04.076  0.52
2007 Zhao R, Houry WA. Molecular interaction network of the Hsp90 chaperone system. Advances in Experimental Medicine and Biology. 594: 27-36. PMID 17205672 DOI: 10.1007/978-0-387-39975-1_3  0.52
2006 Thibault G, Yudin J, Wong P, Tsitrin V, Sprangers R, Zhao R, Houry WA. Specificity in substrate and cofactor recognition by the N-terminal domain of the chaperone ClpX. Proceedings of the National Academy of Sciences of the United States of America. 103: 17724-9. PMID 17090685 DOI: 10.1073/pnas.0601505103  0.52
2006 Wong KS, Houry WA. Hsp90 at the crossroads of genetics and epigenetics. Cell Research. 16: 742-9. PMID 16940964 DOI: 10.1038/sj.cr.7310090  0.52
2006 Thibault G, Tsitrin Y, Davidson T, Gribun A, Houry WA. Large nucleotide-dependent movement of the N-terminal domain of the ClpX chaperone. The Embo Journal. 25: 3367-76. PMID 16810315 DOI: 10.1038/sj.emboj.7601223  0.52
2006 Snider J, Houry WA. MoxR AAA+ ATPases: a novel family of molecular chaperones? Journal of Structural Biology. 156: 200-9. PMID 16677824 DOI: 10.1016/j.jsb.2006.02.009  0.52
2006 Snider J, Gutsche I, Lin M, Baby S, Cox B, Butland G, Greenblatt J, Emili A, Houry WA. Formation of a distinctive complex between the inducible bacterial lysine decarboxylase and a novel AAA+ ATPase. The Journal of Biological Chemistry. 281: 1532-46. PMID 16301313 DOI: 10.1074/jbc.M511172200  0.52
2005 Zhao R, Houry WA. Hsp90: a chaperone for protein folding and gene regulation. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 83: 703-10. PMID 16333321 DOI: 10.1139/o05-158  0.52
2005 Sprangers R, Gribun A, Hwang PM, Houry WA, Kay LE. Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release. Proceedings of the National Academy of Sciences of the United States of America. 102: 16678-83. PMID 16263929 DOI: 10.1073/pnas.0507370102  0.52
2005 Zhao R, Davey M, Hsu YC, Kaplanek P, Tong A, Parsons AB, Krogan N, Cagney G, Mai D, Greenblatt J, Boone C, Emili A, Houry WA. Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone. Cell. 120: 715-27. PMID 15766533 DOI: 10.1016/j.cell.2004.12.024  0.52
2005 Gribun A, Kimber MS, Ching R, Sprangers R, Fiebig KM, Houry WA. The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation. The Journal of Biological Chemistry. 280: 16185-96. PMID 15701650 DOI: 10.1074/jbc.M414124200  0.52
2004 Wong P, Houry WA. Chaperone networks in bacteria: analysis of protein homeostasis in minimal cells. Journal of Structural Biology. 146: 79-89. PMID 15037239 DOI: 10.1016/j.jsb.2003.11.006  0.52
2003 Donaldson LW, Wojtyra U, Houry WA. Solution structure of the dimeric zinc binding domain of the chaperone ClpX. The Journal of Biological Chemistry. 278: 48991-6. PMID 14525985 DOI: 10.1074/jbc.M307826200  0.52
2003 Wojtyra UA, Thibault G, Tuite A, Houry WA. The N-terminal zinc binding domain of ClpX is a dimerization domain that modulates the chaperone function. The Journal of Biological Chemistry. 278: 48981-90. PMID 12937164 DOI: 10.1074/jbc.M307825200  0.52
2003 Wong P, Kolesov G, Frishman D, Houry WA. Phylogenetic web profiler. Bioinformatics (Oxford, England). 19: 782-3. PMID 12691995 DOI: 10.1093/bioinformatics/btg064  0.52
2001 Houry WA. Chaperone-assisted protein folding in the cell cytoplasm. Current Protein & Peptide Science. 2: 227-44. PMID 12369934 DOI: 10.2174/1389203013381134  0.52
2001 Houry WA. Mechanism of substrate recognition by the chaperonin GroEL. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 79: 569-77. PMID 11716298 DOI: 10.1139/bcb-79-5-569  0.52
1999 Houry WA, Frishman D, Eckerskorn C, Lottspeich F, Hartl FU. Identification of in vivo substrates of the chaperonin GroEL. Nature. 402: 147-54. PMID 10647006 DOI: 10.1038/45977  0.52
1999 Teter SA, Houry WA, Ang D, Tradler T, Rockabrand D, Fischer G, Blum P, Georgopoulos C, Hartl FU. Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains. Cell. 97: 755-65. PMID 10380927 DOI: 10.1016/S0092-8674(00)80787-4  0.52
1998 Houry WA, Sauder JM, Roder H, Scheraga HA. Definition of amide protection factors for early kinetic intermediates in protein folding. Proceedings of the National Academy of Sciences of the United States of America. 95: 4299-302. PMID 9539731 DOI: 10.1073/pnas.95.8.4299  0.52
1997 Ewalt KL, Hendrick JP, Houry WA, Hartl FU. In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell. 90: 491-500. PMID 9267029 DOI: 10.1016/S0092-8674(00)80509-7  0.52
1996 Sendak RA, Rothwarf DM, Wedemeyer WJ, Houry WA, Scheraga HA. Kinetic and thermodynamic studies of the folding/unfolding of a tryptophan-containing mutant of ribonuclease A. Biochemistry. 35: 12978-92. PMID 8841145 DOI: 10.1021/bi961280r  0.52
1996 Houry WA, Scheraga HA. Structure of a hydrophobically collapsed intermediate on the conformational folding pathway of ribonuclease A probed by hydrogen-deuterium exchange. Biochemistry. 35: 11734-46. PMID 8794754 DOI: 10.1021/bi961085c  0.52
1996 Houry WA, Scheraga HA. Nature of the unfolded state of ribonuclease A: effect of cis-trans X-Pro peptide bond isomerization. Biochemistry. 35: 11719-33. PMID 8794753 DOI: 10.1021/bi960745a  0.52
1996 Houry WA, Rothwarf DM, Scheraga HA. Circular dichroism evidence for the presence of burst-phase intermediates on the conformational folding pathway of ribonuclease A. Biochemistry. 35: 10125-33. PMID 8756476 DOI: 10.1021/bi960617m  0.52
1995 Houry WA, Rothwarf DM, Scheraga HA. The nature of the initial step in the conformational folding of disulphide-intact ribonuclease A. Nature Structural Biology. 2: 495-503. PMID 7664113  0.52
1994 Houry WA, Rothwarf DM, Scheraga HA. A very fast phase in the refolding of disulfide-intact ribonuclease A: implications for the refolding and unfolding pathways. Biochemistry. 33: 2516-30. PMID 8117713  0.52
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