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Walid Houry - Publications

Affiliations: 
Biochemistry University of Toronto, Toronto, ON, Canada 
Website:
http://biochemistry.utoronto.ca/houry/Labpage/index1.html
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25 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
2019 Ishizawa J, Zarabi SF, Davis RE, Halgas O, Nii T, Jitkova Y, Zhao R, St-Germain J, Heese LE, Egan G, Ruvolo VR, Barghout SH, Nishida Y, Hurren R, Ma W, ... ... Houry W, et al. Mitochondrial ClpP-Mediated Proteolysis Induces Selective Cancer Cell Lethality. Cancer Cell. PMID 31056398 DOI: 10.1016/J.Ccell.2019.03.014  0.309
2018 Vahidi S, Ripstein ZA, Bonomi M, Yuwen T, Mabanglo MF, Juravsky JB, Rizzolo K, Velyvis A, Houry WA, Vendruscolo M, Rubinstein JL, Kay LE. Reversible inhibition of the ClpP protease via an N-terminal conformational switch. Proceedings of the National Academy of Sciences of the United States of America. PMID 29941580 DOI: 10.1073/Pnas.1805125115  0.303
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  0.395
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  0.659
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  0.672
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  0.345
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  0.671
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  0.686
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  0.679
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  0.653
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  0.32
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  0.617
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  0.333
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  0.315
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  0.308
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  0.545
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  0.502
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  0.406
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  0.531
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  0.4
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  0.433
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  0.376
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  0.382
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 DOI: 10.1038/Nsb0695-495  0.36
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 DOI: 10.1021/Bi00175A022  0.383
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