{"id":32,"date":"2015-02-03T22:56:38","date_gmt":"2015-02-04T03:56:38","guid":{"rendered":"http:\/\/localhost\/wordpress\/?page_id=32"},"modified":"2025-01-11T12:08:36","modified_gmt":"2025-01-11T17:08:36","slug":"publications","status":"publish","type":"page","link":"https:\/\/lab.walidhoury.com\/?page_id=32","title":{"rendered":"Publications"},"content":{"rendered":"\n

See PubMed<\/a> for a recent list of publications.<\/p>\n\n\n\n

2024<\/strong><\/h3>\n\n\n\n
    \n
  1. Mao, Y.-Q., Jahanshahi, S., Malty, R., Van Ommen, D. A. J., Wan, Y., Ahmed, C., Dahal, S., Lin, F., Mangos, M., Nurtanto, J., Been, T., Christie-Holmes, N., Gray-Owen, S. D., Babu, M., Batey, R. A., Attisano, L., Cochrane, A., & Houry<\/strong>, W. A. \u201cTargeting Protein Homeostasis with Small Molecules as a Strategy for the Development of Pan-Coronavirus Antiviral Therapies\u201d Communications Biology<\/em> 7:1460 (2024). (<\/span>PDF file<\/a>)<\/span><\/li>\n\n\n\n
  2. Lin, F., Mabanglo, M. F., Zhou, J. L., Binepal, G., Barghash, M. M., Wong, K. S., Gray-Owen, S. D., Batey, R. A., & Houry<\/strong>, W. A. \u201cStructure-Based Design and Development of Phosphine Oxides as a Novel Chemotype for Antibiotics that Dysregulate Bacterial ClpP Proteases\u201d Journal of Medicinal Chemistry<\/em> 67(17):15131-15147 (2024). (<\/span>PDF file<\/a>)<\/span><\/li>\n\n\n\n
  3. Wallach, I. \u2026, Leung, E., \u2026, Wong, K. S., \u2026, Barghash, M. M.,\u2026 Ip, P., \u2026, \u2026 Houry<\/strong>, W. A., \u2026, Heifets, A. (581 authors) \u201cMachine Learning is a Viable Alternative to High Throughput Screening: A 281 target case study\u201d Scientific Reports<\/em> 14:7526, 1-16 (2024). (<\/span>PDF file<\/a>)<\/span><\/li>\n\n\n\n
  4. Mao, Y.-Q., Seraphim, T. V., Wan, Y., Wu, R., Coyaud, E., Bin Munim, M., Mollica, A., Laurent, E., Babu, M., Mennella, V., Raught, B., & Houry<\/strong>, W. A. \u201cDPCD is a Regulator of R2TP in Ciliogenesis Initiation through Akt Signaling\u201d Cell Reports<\/em> 43(2), 113713, 1-27 (2024). (<\/span>PDF file<\/a>)<\/span><\/li>\n\n\n\n
  5. Jahanshahi, S., Ouyang, H., Ahmed, C., Amiri, A. Z., Dahal, S., Mao, Y.-Q., Van Ommen, D. A. J., Malty, R., Duan, W., Been, T., Hernandez, J., Mangos, M., Nurtanto, J., Babu, M., Attisano, L., Houry<\/strong>, W. A., Moraes, T. J., & Cochrane, A. \u201cBroad Spectrum Post-Entry Inhibitors of Coronavirus Replication: Cardiotonic Steroids and Monensin\u201d Virology<\/em> 589, 109915, 1-13 (2024). (<\/span>PDF file<\/a>)<\/span><\/li>\n\n\n\n
  6. Morey, T. M. & Houry<\/strong>, W. A. \u201cTarget-locked: A mechanism for disaggregase binding to aggregated proteins\u201d The Journal of Biological Chemistry<\/em> 300(4), 107165, 1-3 (2024).\u00a0(<\/span>PDF file<\/a>)<\/span><\/li>\n\n\n\n
  7. Buchner, J., Alasady, M. J., Backe, S. J., Blagg, B. S. J., Carpenter, R. L., Colombo, G., Gelis, I., Gewirth, D. T., Gierasch, L. M., Houry<\/strong>, W. A., Johnson, J. L., Kang, B. H., Kao, A. W., LaPointe, P., Mattoo, S., McClellan, A. J., Neckers, L. M., Prodromou, C., Rasola, A., Sager, R. A., Theodoraki, M. A., Truman, A. W., Truttman, M. C., Zachara, N. E., Bourboulia, D., Mollapour, M., & Woodford, M. R. \u201cSecond international symposium on the chaperone code, 2023\u201d Cell Stress and Chaperones<\/em> 29(1), 88-96 (2024). (<\/span>PDF file<\/a>)<\/span><\/li>\n<\/ol>\n\n\n\n

    2023<\/strong><\/h3>\n\n\n\n
      \n
    1. Dahal, S., Clayton, K., Cabral, T., Cheng, R., Jahanshahi, S., Ahmed, C., Koirala, A., Ocando, A. V., Malty, R., Been, T., Hernandez, J., Mangos, M., Shen, D., Babu, M., Calarco, J., Chabot, B., Attisano, L., Houry<\/strong>, W. A., & Cochrane, A. \u201cOn a Path Toward a Broad-Spectrum Antiviral: Inhibition of HIV-1 and Coronavirus Replication by a SR Kinase Inhibitor Harmine\u201d Journal of Virology<\/em> 97(10), 1-31 (2023). (<\/span>PDF file<\/a>)<\/span><\/li>\n\n\n\n
    2. Bhandari, V., Reichheld, S. E., Houliston, S., Lemak, A., Arrowsmith, C. H., Sharpe, S., & Houry<\/strong>, W. A. \u201cThe Role of RavA-ViaA Chaperone Complex in Bacterial Persistence\u201d The Journal of Biological Chemistry<\/em> 299(10), 105199, 1-13 (2023). (<\/span>PDF file<\/a>)<\/span><\/li>\n\n\n\n
    3. Antonio, L. M., Martins, G. H., Arag\u00e3o, A. Z. B., Quel, N. G., Zazeri, G., Houry<\/strong>, W. A., & Ramos, C. H. I. \u201cUnveiling the Role of Sorghum RPAP3 in the R2TP Complex Function: Insights into Protein Assembly in Plants\u201d Plants<\/em> 12(16), 2925, pages 1-15; https:\/\/doi.org\/10.3390\/plants12162925 (2023). (<\/span>PDF file<\/a>)<\/span><\/li>\n\n\n\n
    4. Mabanglo, M. F., Wong, K. S., Barghash, M. M., Leung, E., Chuang, S. H. W., Ardalan, A., Majaesic, E. M., Wong, C. J., Zhang, S., Lang, H., Karanewsky, D. S., Iwanowicz, A. A., Graves, L. M., Iwanowicz, E. J., Gingras, A.-C., & Houry<\/strong>, W. A. \u201cPotent ClpP Agonists with Anticancer Properties Bind with Improved Structural Complementarity and Alter the Mitochondrial N-Terminome\u201d Structure<\/em> 31<\/u>, 1\u201316 (2023). (<\/span>PDF file<\/a>)<\/span><\/li>\n\n\n\n
    5. van Oosten\u2011Hawle, P., Backe, S. J., Ben\u2011Zvi, A., Bourboulia, D., Brancaccio, M., Brodsky, J., Clark, M., Colombo, G., Cox, M. B., De Los Rios, P., Echtenkamp, F., Edkins, A., Freeman, B., Goloubinoff, P., Houry<\/strong>, W. A., Johnson, J., LaPointe, P., Li, W., Mezger, V., Neckers, L., Nillegoda, N. B., Prahlad, V., Reitzel1, A., Scherz\u2011Shouva, R., Sistonen, L., Tsai, F. T. F., Woodford, M. R., Mollapour, M., & Truman, A. W. \u201cSecond Virtual International Symposium on Cellular and Organismal Stress Responses, September 8\u20139, 2022\u201d Cell Stress and Chaperones<\/em> 28<\/u>(1), 1\u20139 (2023). (<\/span>PDF file<\/a>)<\/span><\/li>\n<\/ol>\n\n\n\n

      2022<\/strong><\/h3>\n\n\n\n
        \n
      1. Bhandari, V., Van Ommen, D. A. J., Wong, K. S., & Houry<\/strong>, W. A. \u201cAnalysis of the Evolution of the MoxR ATPases\u201d The Journal of Physical Chemistry A<\/em> 126<\/u>(29), 4734-4746 (2022). (<\/span>PDF file<\/a>)<\/span><\/li>\n\n\n\n
      2. Fennell, E. M. J., Aponte-Collazo, L. J., Wynn, J. D., Drizyte-Miller, K., Leung, E., Greer, Y. E., Graves, P. R., Iwanowicz, A. A., Ashamalla, H., Holmuhamedov, E., Lang, H., Karanewsky, D. S., Der, C. J., Houry<\/strong>, W. A., Lipkowitz, S., Iwanowicz, E. J., & Graves, L. M. \u201cCharacterization of TR-107, a Novel Chemical Activator of the Human Mitochondrial Protease ClpP\u201d Pharmacology Research & Perspectives<\/em> 10<\/u>(4):e00993 (2022). (<\/span>PDF file<\/a>)<\/span><\/li>\n\n\n\n
      3. Seraphim, T. V., Nano, N., Cheung, Y. W. S., Aluksanasuwan, S., Colleti, C., Mao, Y.-Q., Bhandari, V., Young, G., H\u00f6ll, L., Phanse, S., Gordiyenko, Y., Southworth, D. R., Robinson, C. V., Thongboonkerd, V., Gava, L. M., Borges, J. C., Babu, M., Barbosa, L. R. S., Ramos, C. H. I., Kukura, P., & Houry<\/strong>, W. A. \u201cAssembly Principles of the Human R2TP Chaperone Complex Reveal the Presence of R2T and R2P Complexes\u201d Structure<\/em> 30<\/u>(1):156-171.e12 (2022). (<\/span>PDF file<\/a>)<\/span><\/li>\n\n\n\n
      4. Dahal, S., Cheng, R., Cheung, P. K., Been, T., Malty, R., Geng, M., Manianis, S., Shkreta, L., Jahanshahi, S., Toutant, J., Chan, R., Park, S., Brockman, M. A., Babu, M., Mubareka, S., Mossman, K., Banerjee, A., Gray-Owen, S., Brown, M., Houry<\/strong>, W. A., Chabot, B., Grierson, D., & Cochrane, A. \u201cThe Thiazole-5-carboxamide GPS491 Inhibits HIV-1, Adenovirus, and Coronavirus Replication by Altering RNA Processing\/Accumulation\u201d Viruses<\/em> 14<\/u>(60), 1-26, https:\/\/doi.org\/10.3390\/v14010060 (2022). (<\/span>PDF file<\/a>)<\/span><\/li>\n\n\n\n
      5. Aljghami, M. E., Barghash, M. M., Majaesic, E., Bhandari, V., & Houry<\/strong>, W. A. \u201cCellular Functions of the ClpP Protease Impacting Bacterial Virulence\u201d Frontiers in Molecular Biosciences<\/em> (section on Protein Folding, Misfolding and Degradation) 9:1054408. doi: 10.3389\/fmolb.2022.1054408 (2022). (<\/span>PDF file<\/a>)<\/span><\/li>\n\n\n\n
      6. Editor of the thematic series on \u201cProteostasis\u201d, published in Journal of Biological Chemistry<\/em> (October, 2022), https:\/\/www.jbc.org\/thematic-proteostasis<\/a>. Gierasch, L. & Houry<\/strong>, W. A. editors.<\/li>\n\n\n\n
      7. Lynham, J. & Houry<\/strong>, W. A. \u201cThe Role of Hsp90-R2TP in Macromolecular Complex Assembly and Stabilization\u201d Biomolecules<\/em> 12<\/u>, 1045, 1-29; https:\/\/doi.org\/10.3390\/biom12081045 (2022). (<\/span>PDF file<\/a>)<\/span><\/li>\n\n\n\n
      8. Mabanglo, M. F. & Houry<\/strong>, W. A. \u201cRecent Structural Insights into the Mechanism of ClpP Protease Regulation by AAA+ Chaperones and Small Molecules\u201d Journal of Biological Chemistry<\/em> 298<\/u>(5):101781, 1-20 (2022). (<\/span>PDF file<\/a>)<\/span><\/li>\n\n\n\n
      9. Mabanglo, M. F., Bhandari, V., & Houry<\/strong>, W. A. \u201cSubstrates and Interactors of the ClpP Protease in the Mitochondria\u201d Current Opinion in Chemical Biology<\/em> 66<\/u>:102078, 1-10 (2022). (<\/span>PDF file<\/a>)<\/span><\/li>\n<\/ol>\n\n\n\n

        2021<\/strong><\/h3>\n\n\n\n
          \n
        1. Abrah\u00e3o, J., Amaro, B. T., Peres, B. R., Quela, N. G., Arag\u00e3o, A. Z. B., Moreab, E. G. O., Cano, M. I. N., Houry<\/strong>, W. A., & Ramos, C. H. I. \u201cLeishmania major<\/em> RUVBL1 has a Hexameric Conformation in Solution and, in the Presence of RUVBL2, Forms a Heterodimer with ATPase Activity\u201d Archives of Biochemistry and Biophysics<\/em> 703<\/u>, article number 108841 (2021). (<\/span>PDF file<\/a>)<\/span><\/li>\n\n\n\n
        2. Araujo, S. A., Martins, G. H., Quel, N. G., Arag\u00e3o, A. Z. B., Morea, E. G. O., Borges, J. C., Houry<\/strong>, W. A., Cano, M. I. N., & Ramos, C. H. I. \u201cPurification and Characterization of a Novel and Conserved TPR-Domain Protein that Binds both Hsp90 and Hsp70 and is Expressed in all Developmental Stages of Leishmania major<\/em>\u201d Biochimie<\/em> 182<\/u>, 51-60 (2021). (<\/span>PDF file<\/a>)<\/span><\/li>\n\n\n\n
        3. Rizzolo, K., Yu, A. Y. H., Ologbenla, A., Kim, S.-R., Zhu, H., Ishimori, K., Thibault, G., Leung, E., Zhang, Y. W., Teng, M., Haniszewski, M., Miah, N., Phanse, S., Minic, Z., Lee, S., Caballero. J. D., Babu, M., Tsai, F. T. F., Saio, T., & Houry<\/strong>, W. A. \u201cFunctional Cooperativity Between the Trigger Factor Chaperone and the ClpXP Proteolytic Complex\u201d Nature Communications<\/em> 12<\/u>, article number 281, 1\u201318 (2021). (<\/span>PDF file<\/a>)<\/span><\/li>\n<\/ol>\n\n\n\n

          2020<\/strong><\/h3>\n\n\n\n
            \n
          1. Binepal, G., Mabanglo, M. F., Goodreid, J. D., Leung, E., Barghash, M. M., Wong, K. S., Lin, F., Cossette, M., Bansagi, J., Song, B., Serr\u00e3o, V. H. B., Pai, E. F., Batey, R. A., Gray-Owen, S. D., & Houry<\/strong>, W. A. \u201cDevelopment of Antibiotics that Dysregulate the Neisserial ClpP Protease\u201d ACS Infectious Disease<\/em> 6<\/u>(12), 3224\u22123236 (2020). (<\/span>PDF file<\/a>)<\/span><\/li>\n\n\n\n
          2. Quel, N. G., Pinheiro, G. M. S., Rodrigues, L. F. de C., Barbosa, L. R. S., Houry<\/strong>, W. A., & Ramos, C. H. I. \u201cHeat Shock Protein 90 kDa (Hsp90) from Aedes aegypti<\/em> has an Open Conformation and is Expressed Under Heat Stress\u201d International Journal of Biological Macromolecules<\/em> 156<\/u>, 522\u2013530 (2020). (<\/span>PDF file<\/a>)<\/span><\/li>\n\n\n\n
          3. Nano, N., Ugwu, F., Seraphim, T. V., Li, T., Azer, G., Isaac, M., Prakesch, M., Barbosa, L. R. S., Ramos, C. H. I., Datti, A., & Houry<\/strong>, W. A. \u201cSorafenib as an Inhibitor of RUVBL2\u201d Biomolecules<\/em> 10<\/u>(4), article number 605, 1-15; doi:10.3390\/biom10040605 (2020). (<\/span>PDF file<\/a>)<\/span><\/li>\n\n\n\n
          4. Ripstein, Z. A., Vahidi, S., Houry<\/strong>, W. A., Rubinstein, J. L., & Kay, L. E. \u201cA Processive Rotary Mechanism Couples Substrate Unfolding and Proteolysis in the ClpXP Degradation Machinery\u201d eLife<\/em> 9<\/u>:e52158, 1-25 (2020). (<\/span>PDF file<\/a>)<\/span><\/li>\n\n\n\n
          5. Seraphim, T. V. & Houry<\/strong>, W. A. \u201cPrimer on AAA+ Proteins\u201d <\/span>Current Biology<\/em> 30<\/u>(6), R251-R257, (2020). (<\/span>PDF file<\/a>)<\/span><\/li>\n<\/ol>\n\n\n\n

            2019<\/strong><\/h3>\n\n\n\n
              \n
            1. Mabanglo, M. F., Leung, E., Vahidi, S., Seraphim, T. V., Eger, B. T., Bryson, S., Bhandari, V., Zhou, J. L., Mao, Y.-Q., Rizzolo, K., Barghash, M. M., Goodreid, J. D., Phanse, S., Babu, M., Barbosa, L. R. S., Ramos, C. H. I., Batey, R. A., Kay, L. E., Pai, E. F., & Houry<\/strong>, W. A. \u201cClpP Protease Activation Results from the Reorganization of the Electrostatic Interaction Networks at the Entrance Pores\u201d Communications Biology<\/em> 2<\/u>(1), article number 410 (2019). (PDF file<\/a>)<\/li>\n\n\n\n
            2. Ishizawa, J., Zarabi, S. F., Davis, R. E., Halgas, O., Nii, T., Jitkova, Y., Zhao, R., St-Germain, J., Heese, L. E., Egan, G., Ruvolo, V. R., Barghout, S. H., Nishida, Y., Hurren, R., Ma, W., Gronda, M., Link, T., Wong, K. S., Mabanglo, M., Kojima, K., Borthakur, G., MacLean, N., Ma, M. C. J., Leber, A. B., Minden, M. D., Houry<\/strong>, W. A., Kantarjian, H., Stogniew, M., Raught, B., Pai, E. F., Schimmer, A. D., & Andreeff, M. \u201cMitochondrial ClpP-Mediated Proteolysis Induces Selective Cancer Cell Lethality\u201d 35<\/u>(5), 721-737 Cancer Cell<\/em> (2019). (PDF file<\/a>)<\/li>\n\n\n\n
            3. Weiditch, S. A., Seraphim, T. V., Houry<\/strong>, W. A., & Kanelis, V. \u201cStrategies for Purification of the Bacteriophage HK97 Small and Large Terminase Subunits that Yield Pure and Homogeneous Samples that are Functional\u201d 160<\/u>, 45-55 Protein Expression and Purification<\/em> (2019). (PDF file<\/a>)<\/li>\n\n\n\n
            4. Seraphim, T. V., Chakafana, G., Shonhai, A., & Houry<\/strong>, W. A. \u201cPlasmodium falciparum<\/i> R2TP complex\u201d Biophysical Reviews<\/em> 11<\/u>(46), 1007-1015 (2019). <\/span>(PDF file<\/a>)<\/li>\n\n\n\n
            5. Wong, K. S. & Houry<\/strong>, W. A. \u201cChemical Modulation of the Human Mitochondrial ClpP: Potential Application in Cancer Therapeutics\u201d ACS Chemical Biology<\/em> 14<\/u>(11), 2349-2360 (2019). (PDF file<\/a>)<\/li>\n\n\n\n
            6. Lin, F., Mabanglo, M. F., Houry<\/strong>, W. A., & Batey, R. A. \u201cDevelopment of Small Molecules to Modulate the Activity of the ATP-Dependent ClpP Protease as a Novel Antibacterial and Anticancer Drug Target\u201d 2019<\/em> Medicinal Chemistry Reviews<\/em>, Joanne J. Bronson (Editor-In-Chief), Volume 54, Chapter 18, pages 379 \u2013 404. (2019). (PDF file<\/a>)<\/li>\n\n\n\n
            7. Wong, K. S. & Houry<\/strong>, W. A. \u201cRecent Advances in Targeting Human Mitochondrial AAA+ Proteases to Develop Novel Cancer Therapeutics\u201d in the book Mitochondrial Health and Disease, Mohan Babu and Andrea Urbani (Editors). Volume 1158 of the series Advances in Experimental Medicine and Biology<\/em>, pages 119-142. Springer, Singapore (2019). (PDF file<\/a>)<\/li>\n\n\n\n
            8. Rizzolo, K. & Houry<\/strong>, W. A. \u201cMultiple Functionalities of Molecular Chaperones Revealed Through Systematic Mapping of their Interaction Networks\u201d Journal of Biological Chemistry<\/em> 294<\/u>(6), 2142-2150 (2019). (PDF file<\/a>)<\/li>\n<\/ol>\n\n\n\n

              2018<\/strong><\/h3>\n\n\n\n
                \n
              1. Vahidi, S., Ripstein, Z. A., Bonomi, M., Yuwen, T., Mabanglo, M. F., Juravsky, J. B., Rizzolo, K., Velyvis, A., Houry<\/strong>, W. A., Vendruscolo, M., Rubinstein, J. L., & Kay, L. E. \u201cReversible Inhibition of the ClpP Protease via an N-Terminal Conformational Switch\u201d Proceedings of the National Academy of Sciences<\/em> 115<\/u>(28), E6447-E6456 (2018). (PDF file<\/a>)<\/li>\n\n\n\n
              2. Wong, K. S., Mabanglo, M. F., Seraphim, T. V., Mollica, A., Mao, Y.-Q., Rizzolo, K., Leung, E., Moutaoufik, M. T., Hoell, L., Phanse, S., Goodreid, J., Barbosa, L. R. S., Ramos, C. H. I., Babu, M., Mennella, V., Batey, R. A., Schimmer A. D., & Houry<\/strong>, W. A. \u201cAcyldepsipeptide Analogs Dysregulate Human Mitochondrial ClpP Protease Activity and Cause Apoptotic Cell Death\u201d Cell Chemical Biology<\/em> 25<\/u>(8), 1017-1030 (2018). (PDF file<\/a>)<\/li>\n\n\n\n
              3. Rizzolo, K., Kumar, A., Kakihara, Y., Phanse, S., Minic, Z., Snider, J., Stagljar, I., Zilles, S., Babu, M., & Houry<\/strong>, W. A. \u201cSystems Analysis of the Genetic Interaction Network of Yeast Molecular Chaperones\u201d Molecular Omics<\/em> 14<\/u>(2), 82\u201394 (2018). (PDF file<\/a>)<\/li>\n\n\n\n
              4. Editor of the eBook \u201cThe Role of AAA+ Proteins in Protein Repair and Degradation\u201d Frontiers Media. doi: 10.3389\/978-2-88945-656-7 (2018). Shorter, J. & Houry<\/strong>, W. A. editors. (https:\/\/www.frontiersin.org\/research-topics\/4803\/the-role-of-aaa-proteins-in-protein-repair-and-degradation)<\/li>\n\n\n\n
              5. Shorter, J. & Houry<\/strong>, W. A. \u201cEditorial: The Role of AAA+ Proteins in Protein Repair and Degradation\u201d Frontiers in Molecular Biosciences<\/em> (section Protein Folding, Misfolding and Degradation) 5:85. doi: 10.3389\/fmolb.2018.00085 (2018). (PDF file<\/a>)<\/li>\n\n\n\n
              6. Lynham, J. & Houry<\/strong>, W. A. \u201cThe multiple functions of the PAQosome: an R2TP- and URI1 prefoldin-based chaperone complex\u201d in the book Prefoldins: The New Chaperones, Nabil Djouber (Editor). Volume 1106 of the series Advances in Experimental Medicine and Biology<\/em>, pages 37-72. Springer International Publishing AG, Cham, Switzerland (2018). (PDF file<\/a>)<\/li>\n\n\n\n
              7. Bhandari, V., Wong, K. S., Zhou, J. L., Mabanglo, M. F., Batey, R. A., & Houry<\/strong>, W. A. \u201cThe Role of ClpP Protease in Bacterial Pathogenesis and Human Diseases\u201d ACS Chemical Biology<\/em> 13<\/u>(6), 1413\u22121425 (2018). (PDF file<\/a>)<\/li>\n\n\n\n
              8. Houry<\/strong>, W. A., Bertrand, E., & Coulombe, B. \u201cThe PAQosome, an R2TP-Based Chaperone for Quaternary Structure Formation\u201d Trends in Biochemical Sciences<\/em> 43<\/u>(1), 4-9 (2018). (PDF file<\/a>)<\/li>\n\n\n\n
              9. Kumar, A., Rizzolo, K., Zilles, S., Babu, M., & Houry<\/strong>, W. A. \u201cComputational Analysis of the Chaperone Interaction Networks\u201d Methods in Molecular Biology<\/em> 1709<\/u>, 275-291 (2018). Stuart K. Calderwood and Thomas L. Prince (eds.), Chaperones: Methods and Protocols, Springer Science+Business Media LLC 2018. (PDF file<\/a>)<\/li>\n<\/ol>\n\n\n\n

                2017<\/strong><\/h3>\n\n\n\n
                  \n
                1. Rizzolo, K., Huen, J., Kumar, A., Phanse, S., Vlasblom, J., Kakihara, Y., Zeineddine, H. A., Minic, Z., Snider, J., Wang, W., Pons, C., Seraphim, T. V., Boczek, E. E., Alberti, S., Costanzo, M., Myers, C. L., Stagljar, I., Boone, C., Babu, M., & Houry<\/strong>, W. A. \u201cFeatures of the Chaperone Cellular Network Revealed through Systematic Interaction Mapping\u201d Cell Reports<\/em> 20<\/u>(11), 2735\u20132748 (2017). (PDF file<\/a>)<\/li>\n\n\n\n
                2. Wong, K. S., Bhandari, V., Janga, S. C., & Houry<\/strong>, W. A. \u201cThe RavA-ViaA Chaperone-Like System Interacts with and Modulates the Activity of the Fumarate Reductase Respiratory Complex\u201d Journal of Molecular Biology<\/em> 429<\/u>(2), 324\u2013344 (2017). (PDF file<\/a>)<\/li>\n\n\n\n
                3. Mao, Y.-Q. & Houry<\/strong>, W. A. \u201cThe Role of Pontin and Reptin in Cellular Physiology and Cancer Etiology\u201d Frontiers in Molecular Biosciences<\/em> (section Protein Folding, Misfolding and Degradation) 4<\/strong>:58. doi: 10.3389\/fmolb.2017.00058 (2017). (PDF file<\/a>)<\/li>\n<\/ol>\n\n\n\n

                   <\/h3>\n\n\n\n

                  2016<\/strong><\/h3>\n\n\n\n
                    \n
                  1. Chan, S. W. S., Yau, J., Ing, C., Liu, K., Farber, P., Won, A., Bhandari, V., Kara-Yacoubian, N., Seraphim, T. V., Chakrabarti, N., Kay, L. E., Yip, C. M., Pom\u00e8s, R., Sharpe, S., & Houry<\/strong>, W. A. \u201cMechanism of Amyloidogenesis of a Bacterial AAA+ Chaperone\u201d Structure<\/em> 24<\/u>(7), 1095\u20131109 (2016). (PDF file<\/a>)<\/li>\n\n\n\n
                  2. Ewens, C. A., Su, M., Zhao,L., Nano, N., Houry<\/strong>, W. A., & Southworth, D. R. \u201cArchitecture and Nucleotide-Dependent Conformational States of the Rvb1-Rvb2 AAA+ Complex\u201d Structure<\/em> 24<\/u>(5), 657\u2013666 (2016). (PDF file)<\/a><\/li>\n\n\n\n
                  3. Kandiah, E., Carriel, D., Perard, J., Malet, H., Bacia, M., Liu, K., Chan, S. W. S., Houry<\/strong>, W. A., Ollagnier de Choudens, S., Elsen, S., & Gutsche, I. \u201cLessons from Structures of E. coli<\/em> Lysine Decarboxylases\u201d Scientific Reports<\/em> 6:24601 | DOI: 10.1038\/srep24601 (2016). (PDF file)<\/a><\/li>\n\n\n\n
                  4. Goodreid, J. D., Janetzko, J., Santa Maria Jr., J. P., Wong, K. S., Leung, E., Eger, B. T., Bryson, S., Pai, E. F., Gray-Owen, S. D., Walker, S., Houry<\/strong>, W. A., Batey, R. A. \u201cDevelopment and Characterization of Potent Cyclic Acyldepsipeptide Analogues with Increased Antimicrobial Activity\u201d Journal of Medicinal Chemsitry<\/em> 59<\/u>(2), 624-646 (2016). (PDF file)<\/a><\/li>\n<\/ol>\n\n\n\n

                    2015<\/strong><\/h3>\n\n\n\n
                      \n
                    1. 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, D., Sukhai, M. A., Prabha, S., Bashir, S., Ramakrishnan, A., Leung, E., Qia, Y. H.,, Zhang, N., Combes, K. R., Ketela, T., Lin, F., Houry<\/strong>, W. A., Aman, A., Al-Awar, R., Zheng, W., Wienholds, E., Xu, C. J., Dick, J., Wang, J. C., Moffat, J., Minden, M. D., Eaves, C. J., Bader, G. D., Hao, Z., Kornblau, S. M., Raught, B., & Schimmer, A. D. \u201cInhibition of the Mitochondrial Protease ClpP as a Therapeutic Strategy for Human Acute Myeloid Leukemia\u201d Cancer Cell<\/em> 27<\/u>(6), 864-876 (2015). (PDF file)<\/a><\/li>\n\n\n\n
                    2. Jeganathan, A., Leong, V., Zhao, L., Huen, J., Nano, N., Houry<\/strong>, W. A., & Ortega, J. \u201cYeast Rvb1 and Rvb2 proteins oligomerize as a conformationally variable dodecamer with low frequency\u201d Journal of Molecular Biology<\/em> 427<\/u>(10), 1875\u20131886 (2015). (PDF file)<\/a><\/li>\n\n\n\n
                    3. 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, J. F., Houry<\/strong>, W. A., Emili, A., Morris, Q., Bader, G., & Babu, M. \u201cNovel function discovery with GeneMANIA: a new integrated resource for gene function prediction in Escherichia coli<\/em>\u201d Bioinformatics<\/em> 31<\/u>(3), 306-310 (2015). (PDF file)<\/a><\/li>\n\n\n\n
                    4. Matias, P. M., Baek, S. H., Bandeiras, T. M., Dutta, A., Houry<\/strong>, W. A., Llorca, O., Rosenbaum, J. \u201cThe AAA+ Proteins Pontin and Reptin Enter Adult Age: From Understanding Their Basic Biology to the Identification of Selective Inhibitors\u201d Frontiers in Molecular Biosciences<\/em> (section Protein Folding, Misfolding and Degradation) 2<\/strong>:17, 1-7. doi: 10.3389\/fmolb.2015.00017 (2015). (PDF file)<\/a><\/li>\n\n\n\n
                    5. Bhandari, V. & Houry<\/strong>, W. A. \u201cSubstrate Interaction Networks of the Escherichia coli Chaperones: Trigger Factor, DnaK and GroEL\u201d in the book Prokaryotic Systems Biology, Mohan Babu and Nevan J. Krogan (Editors). Volume 883 of the series Advances in Experimental Medicine and Biology<\/em>, pages 271-294. Springer International Publishing AG, Cham, Switzerland (2015). (PDF file)<\/a><\/li>\n<\/ol>\n\n\n\n

                      2014<\/strong><\/h3>\n\n\n\n
                        \n
                      1. Goodreid, J. D., Wong, K., Leung, E., McCaw, S. E., Gray-Owen, S. D., Lough, A., Houry<\/strong>, W. A., & Batey, R. A. “Total Synthesis and Antibacterial Testing of the A54556 Cyclic Acyldepsipeptides Isolated from Streptomyces hawaiiensis<\/em>” Journal of Natural Products<\/em> 77<\/span>(10), 2170\u22122181 (2014). (PDF file)<\/a><\/li>\n\n\n\n
                      2. Malet, H., Liu, K., El Bakkouri, M., Chan, S. W. S., Effantin, G., Bacia, M., Houry<\/strong>*, W. A., & Gutsche*, I. “Assembly Principles of a Unique Cage Formed by Hexameric and Decameric E. coli<\/em> Proteins” eLife<\/em> 3<\/span>: e03653, 1-11. doi: 10.7554\/eLife.03653 (2014). *Co-corresponding authors. (PDF file)<\/a><\/li>\n\n\n\n
                      3. Kakihara, Y., Makhnevych, T., Zhao, L., Tang, W., & Houry<\/strong>, W. A. “Nutritional Status Modulates Box C\/D snoRNP Biogenesis by Regulated Subcellular Relocalization of the R2TP Complex” Genome Biology<\/em> 15<\/span>(7): 404, 1-20 (2014). (PDF file)<\/a><\/li>\n\n\n\n
                      4. Babu, M, Arnold, R., Bundalovic-Torma, C., Gagarinova, A., Wong, K. S., Kumar, A., Stewart, G., Samanfar, B., Aoki, H., Wagih, O., Vlasblom, J., Phanse, S., Lad, K., Yu, A. Y. H., Graham, C., Jin, K., Brown, E., Golshani, A., Kim, P., Moreno-Hagelsieb, G., Greenblatt, J., Houry<\/strong>, W. A., Parkinson, J., & Emili, A. “Quantitative Genome-Wide Genetic Interaction Screens Reveal Global Epistatic Relationships of Protein Complexes in Escherichia coli<\/em>” PLOS Genetics<\/em> 10<\/span>(2): e1004120, 1-15. doi: 10.1371\/journal.pgen.1004120 (2014). (PDF file)<\/a><\/li>\n\n\n\n
                      5. Wong, K. S., Snider, J. D., Graham, C., Greenblatt, J. F., Emili, A., Babu, M., & Houry<\/strong>, W. A. “The MoxR ATPase RavA and its Cofactor ViaA Interact with the NADH:Ubiquinone Oxidoreductase I in Escherichia coli<\/em>” PLOS ONE<\/em> 9<\/span>(1): e85529, 1-15. doi:10.1371\/journal.pone.0085529 (2014). (PDF file)<\/a><\/li>\n\n\n\n
                      6. Editor of the book \u201cInteractomics & Systems Biology: The Molecular Chaperones Interaction Networks in Protein Folding and Degradation\u201d, Springer Science + Business Media, New York, USA (2014). Houry<\/strong>, W.A. editor.<\/li>\n\n\n\n
                      7. Liu, K., Ologbenla, A., & Houry<\/strong>, W. A. “Dynamics of the ClpP Serine Protease: A Model for Self-Compartmentalized Proteases” Critical Reviews in Biochemistry and Molecular Biology<\/em> 49<\/span>(5), 400-412 (2014). (PDF file)<\/a><\/li>\n\n\n\n
                      8. Rizzolo, K., Wong, P., Tillier, E. R. M., & Houry<\/strong>, W. A. “The Interaction Network of the Hsp90 Molecular Chaperone” in the book Interactomics & Systems Biology: The Molecular Chaperones Interaction Networks in Protein Folding and Degradation, Walid A. Houry (Editor). Springer Science + Business Media New York (2014). DOI 10.1007\/978-1-4939-1130-1_5. (PDF file)<\/a><\/li>\n\n\n\n
                      9. Liu, K. & Houry<\/strong>, W. A. “Chaperones and Proteases of Plasmodium falciparum<\/em>” in the book Heat Shock Proteins of Malaria, Addmore Shonhai and Gregory L. Blatch (Editors). Springer Science + Business Media Dordrecht (2014). (PDF file)<\/a><\/li>\n<\/ol>\n\n\n\n

                        2013<\/strong><\/h3>\n\n\n\n
                          \n
                        1. Kamano, Y., Saeki, M., Egusa, H., Kakihara, Y., Houry<\/strong>, W. A., Yatani, H., & Kamisaki, Y. \u201cPIH1D1 Interacts with mTOR Complex 1 and Enhances Ribosome RNA Transcription\u201d FEBS Letters<\/em> 587<\/span>(20), 3303-3308 (2013). (PDF file)<\/a><\/li>\n\n\n\n
                        2. Saeki, M., Egusa, H., Kamano, Y., Kakihara, Y., Houry<\/strong>, W. A., Yatani, H., Noguchi, S., & Kamisaki, Y. \u201cExosome-Bound WD Repeat Protein Monad Inhibits Breast Cancer Cell Invasion by Degrading Amphiregulin mRNA\u201d PLOS ONE<\/em> 8<\/span>(7): e67326, 1-11. doi:10.1371\/journal.pone.0067326 (2013). (PDF file)<\/a><\/li>\n\n\n\n
                        3. El Bakkouri, M., Rathore, S., Calmettes, C., Wernimont, A. K., Liu, K., Sinha, D., Asad, M., Jung, P., Hui, R., Mohmmed, A., & Houry<\/strong>, W. A. \u201cStructural Insights into the Inactive Subunit of the Apicoplast-Localized Caseinolytic Protease Complex of Plasmodium falciparum\u201d The Journal of Biological Chemistry<\/em> 288<\/span>(2), 1022-1031 (2013). (PDF file)<\/a><\/li>\n\n\n\n
                        4. Kanjee, U. & Houry<\/strong>, W. A. \u201cMechanisms of Acid Resistance in Escherichia coli<\/em>\u201d Annual Review of Microbiology<\/em> 67<\/span>, 65-81 (2013). (PDF file)<\/a><\/li>\n\n\n\n
                        5. Makhnevych, T. & Houry<\/strong>, W. A. \u201cThe Control of Spindle Length by Hsp70 and Hsp110 Molecular Chaperones\u201d FEBS Letters<\/em> 587<\/span>(8), 1067-1072 (2013). (PDF file)<\/a><\/li>\n\n\n\n
                        6. Nano, N. & Houry<\/strong>, W. A. \u201cChaperone-Like Activity of the AAA+ Proteins Rvb1 and Rvb2 in the Assembly of Various Complexes\u201d Philosophical Transactions of the Royal Society B<\/em> 368<\/span>(1617):20110399, 1-12. doi: 10.1098\/rstb.2011.0399 (2013). (PDF file)<\/a><\/li>\n\n\n\n
                        7. Rosenbaum, J., Baek, S. H., Dutta, A., Houry<\/strong>, W. A., Huber, O., Hupp, T. R., & Matias, P. M. \u201cThe Emergence of the Conserved AAA+ ATPases Pontin and Reptin on the Signaling Landscape\u201d Science Signaling<\/em> 6<\/span>(266) mr1, 1-6 (2013). (PDF file)<\/a><\/li>\n<\/ol>\n\n\n\n

                          2012<\/strong><\/h3>\n\n\n\n
                            \n
                          1. Paci, A., Liu, X. H., Huang, H., Lim, A., Houry<\/strong>, W. A., & 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<\/em> 287<\/span>(52), 43205\u201343214 (2012). (PDF file)<\/a><\/li>\n\n\n\n
                          2. Makhnevych, T., Wong, P., Pogoutse, O., Vizeacoumar, F. J., Greenblatt, J. F., Emili, A., & Houry, W. A. “Hsp110 is Required for Spindle Length Control” Journal of Cell Biology<\/em> 198<\/span>(4), 623-636 (2012). (PDF file)<\/a><\/li>\n\n\n\n
                          3. Thibault, G. & Houry<\/strong>, W. A. “The 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<\/em> 6<\/span>(23), 6717-6724 (2012). (PDF file)<\/a><\/li>\n\n\n\n
                          4. Jim\u00e9neza, B., Ugwu, F., Zhao, R., Ort\u00eda, L., Makhnevych, T., Pineda-Lucena, A., & Houry<\/strong>, W. A. “The Structure of the Minimal TPR Domain Protein Tah1 Reveals the Mechanism of Its Interaction with Pih1 and Hsp90” The Journal of Biological Chemistry<\/em> 287<\/span>(8), 5698-5709 (2012). (PDF file)<\/a><\/li>\n\n\n\n
                          5. Kanjee, U., Ogata, K., & Houry<\/strong>, W. A. “Direct Binding Targets of the Stringent Response Alarmone (p)ppGpp” Molecular Microbiology<\/em> 85<\/span>(6), 1029-1043 (2012). (PDF file)<\/a><\/li>\n\n\n\n
                          6. Wong, K. S. & Houry<\/strong>, W. A. “Novel Structural and Functional Insights into the MoxR Family of AAA+ ATPases” Journal of Structural Biology<\/em> 179<\/span>(2), 211-221 (2012). (PDF file)<\/a><\/li>\n\n\n\n
                          7. Makhnevych, T. & Houry<\/strong>, W. A. “The Role of Hsp90 in Protein Complex Assembly” Biochimica et Biophysica Acta – Molecular Cell Research<\/em> 1823<\/span>(3), 674-682 (2012). (PDF file)<\/a><\/li>\n\n\n\n
                          8. Kakihara, Y. & Houry<\/strong>, W. A. “The R2TP Complex: Discovery and Functions” Biochimica et Biophysica Acta – Molecular Cell Research<\/em> 1823<\/span>(1), 101-107 (2012). (PDF file)<\/a><\/li>\n\n\n\n
                          9. Houry<\/strong>, W. A. “Mapping the Molecular Chaperone Interaction Network in Yeast” (http:\/\/hstalks.com\/lib.php?t=HST142.3170_1_2&c=252), in The Biomedical & Life Sciences Collection, Henry Stewart Talks Series on “Protein Homeostasis” (http:\/\/hstalks.com\/main\/browse_talks.php?father_id=641&c=252). Walid A. Houry, Editor (2012). Henry Stewart Talks Ltd, London.<\/li>\n<\/ol>\n\n\n\n

                            2011<\/strong><\/h3>\n\n\n\n
                              \n
                            1. Kanjee, U., Gutsche, I., Ramachandran, S., & Houry<\/strong>, W. A. “Regulation of the activity of the Escherichia coli basic aliphatic amino acid decarboxylases by nucleotides and oligomerization reveals the presence of a pH zone of inhibition” Biochemistry<\/em> 50<\/span>(43), 9388-9398 (2011). (PDF file)<\/a><\/li>\n\n\n\n
                            2. Leung, E., Datti, A., Cossette, M., Goodreid, J., McCaw, S. E., Mah, M., Nakhamchik, A., Ogata, K., El Bakkouri, M., Cheng, Y.-Q., Wodak, S. J., Eger, B. T., Pai, E. F., Liu, J., Gray-Owen, S., Batey, R. A., & Houry<\/strong>, W. A. “Activators of Cylindrical Proteases as Antimicrobials: Identification and Development of Novel Small Molecule Activators of the ClpP Protease” Chemistry & Biology<\/em> 18<\/span>(9), 1167\u20131178 (2011). (PDF file)<\/a><\/li>\n\n\n\n
                            3. Kanjee, U., Gutsche, I., Alexopoulos, E., Zhao, B., El Bakkouri, M., Thibault, G., Liu, K., Ramachandran, S., Snider, J., Pai, E. F., & Houry<\/strong>, W. A. “Linkage between the Bacterial Acid Stress and Stringent Responses Revealed by the Structure of the Inducible Lysine Decarboxylase” The EMBO Journal<\/em> 30<\/span>(5), 931-944 (2011). (PDF file)<\/a><\/li>\n\n\n\n
                            4. Gong, Y, Zhang, Z., & Houry<\/strong>. W. A. “Bioinformatic Approach to Identify Chaperone Pathway Relationship from Large-Scale Interaction Networks” Methods in Molecular Biology<\/em> 787<\/span>, 189-203 (2011). (PDF file)<\/a><\/li>\n<\/ol>\n\n\n\n

                              2010<\/strong><\/h3>\n\n\n\n
                                \n
                              1. El Bakkouri, M., Gutsche, I., Kanjee, U., Zhao, B., Yu, M., Goret, G., Schoehn, G., Burmeister, W. P., & Houry<\/strong>, W. A. “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<\/em> 107<\/span>(52), 22499-22504 (2010). (PDF file)<\/a><\/li>\n\n\n\n
                              2. Cheung, K. L. Y., Huen, J., Kakihara, Y., Houry<\/strong>, W. A., & Ortega, J. “Alternative Oligomeric States of the Yeast Rvb1\/Rvb2 Complex Induced by Histidine Tags” Journal of Molecular Biology<\/em> 404<\/span>(3), 478-492 (2010). (PDF file)<\/a><\/li>\n\n\n\n
                              3. El Bakkouri, M., Pow, A., Mulichak, A., Cheung, K. L. Y., Artz, J. D., Amani, M., Fell, S., de Koning-Ward, T. F., Goodman, C. D., McFadden, G. I., Ortega, J., Hui, R., & Houry<\/strong>, W. A. “The Clp Chaperones and Proteases of the Human Malaria Parasite Plasmodium falciparum<\/em>” Journal of Molecular Biology<\/em> 404<\/span>(3), 456-477 (2010). (PDF file)<\/a><\/li>\n\n\n\n
                              4. Kimber, M. S., Yu, A. Y. H., Borg, M., Chan, H. S., & Houry<\/strong>, W. A. “The Structure of a Disulfide Cross-Linked ClpP Protease: Implications for ClpP Dynamics” Structure<\/em> 18<\/span>(7), 798-808 (2010). (PDF file)<\/a><\/li>\n\n\n\n
                              5. Zhao, R., Leung, E., Gruener, S., Schapira, M., & Houry<\/strong>, W. A. “Tamoxifen Enhances the Hsp90 Molecular Chaperone ATPase Activity” PLoS ONE<\/em> 5(4):e9934, 1-8 (2010). (PDF file)<\/a><\/li>\n\n\n\n
                              6. Costanzo, M., Baryshnikova, A., Bellay, J., Kim, Y., Spear, E. D., Sevier, C. S., Ding, H., Koh, J. L. Y., Toufighi, K., Mostafavi, S., Prinz, J., St. Onge, R. P., VanderSluis, B., Makhnevych, T., Vizeacoumar, F. J., Alizadeh, S., Bahr, S., Brost, R. L., Chen, Y., Cokol, M., Deshpande, R., Li, Z., Li, Z.-Y., Liang, W., Marback, M., Paw, J., San Luis, B.-J., Shuteriqi, E., Tong, A. H. Y., van Dyk, N., Wallace, I. M., Whitney, J. A., Weirauch, M. T., Zhong, G., Zhu, H., Houry<\/strong>, W. A., Brudno, M., Ragibizadeh, S., Papp, B., P\u00e1l, C., Roth, F. P., Giaever, G., Nislow, C., Troyanskaya, O. G., Bussey, H., Bader, G. D., Gingras, A.-C., Morris, Q. D., Kim, P. M., Kaiser, C. A., Myers, C. L., Andrews, B. J., & Boone, C. “The Genetic Landscape of a Cell” Science<\/em> 327<\/span>(5964), 425-431 (2010). (PDF file)<\/a><\/li>\n\n\n\n
                              7. Kanjee, U. & Houry<\/strong>, W. A. “An Assay for Measuring the Activity of Escherichia coli<\/em> Inducible Lysine Decarboxyase” http:\/\/www.jove.com\/details.stp?id=2094 doi: 10.3791\/2094 Journal of Visualized Experiments<\/em> 46<\/span> (2010). (PDF file)<\/a><\/li>\n\n\n\n
                              8. Zhao, B. & Houry<\/strong>, W. A. “Acid Stress Response in Enteropathogenic Gammaproteobacteria: An Aptitude for Survival” Biochemistry and Cell Biology<\/em> 88<\/span>(2), 301\u2013314 (2010). (PDF file)<\/a><\/li>\n\n\n\n
                              9. Cheung, K., Huen, J., Houry<\/strong>, W. A., & Ortega, J. “Comparison of the Multiple Oligomeric Structures Observed for the Rvb1 and Rvb2 Proteins” Biochemistry and Cell Biology<\/em> 88<\/span>(1), 77-88 (2010). (PDF file)<\/a><\/li>\n\n\n\n
                              10. Huen, J., Kakihara, Y., Ugwu, F., Cheung, K. L. Y., Ortega, J., & Houry<\/strong>, W. A. “Rvb1-Rvb2: Essential ATP-Dependent Helicases for Critical Complexes” Biochemistry and Cell Biology<\/em> 88<\/span>(1), 29-40 (2010). (PDF file)<\/a><\/li>\n\n\n\n
                              11. Houry<\/strong>, W. A. & Ortega, J. “AAA Proteins: Movers and Shakers” (2010) Biochemistry and Cell Biology<\/em> 88<\/span>(1), i-iv (2010). (PDF file)<\/a><\/li>\n<\/ol>\n\n\n\n

                                2009<\/strong><\/h3>\n\n\n\n
                                  \n
                                1. Gong, Y., Kakihara, Y., Krogan, N., Greenblatt, J., Emili, A., Zhang, Z., & Houry<\/strong>, W. A. “An atlas of Chaperone-Protein Interactions in Saccharomyces cerevisiae: Implications to Protein Folding Pathways in the Cell” Molecular Systems Biology<\/em> 5:275, 1-14 (2009). (PDF file)<\/a><\/li>\n<\/ol>\n\n\n\n

                                  2008<\/strong><\/h3>\n\n\n\n
                                    \n
                                  1. Alexopoulos, E., Kanjee, U., Snider, J., Houry<\/strong>, W. A., & Pai, E. F. “Crystallization and Preliminary X-ray Analysis of the Inducible Lysine Decarboxylase from Escherichia coli” Acta Crystallographica Section F: Structural Biology and Crystallization Communications<\/em> 64(8),700-706 (2008). (PDF file)<\/a><\/li>\n\n\n\n
                                  2. Gribun, A., Cheung, K. L. Y., Huen, J., Ortega, J., & Houry<\/strong>, W. A. “Yeast Rvb1 and Rvb2 are ATP-Dependent DNA Helicases that Form a Heterohexameric Complex” Journal of Molecular Biology<\/em> 376(5), 1320-1333 (2008). (PDF file)<\/a><\/li>\n\n\n\n
                                  3. Zhao, R., Kakihara, Y., Gribun, A., Huen, J., Yang, G., Khanna, M., Costanzo, M., Brost, R. L., Boone, C., Hughes, T. R., Yip, C. M., & Houry<\/strong>, W. A. “Molecular Chaperone Hsp90 Stabilizes Pih1\/Nop17 to Maintain R2TP Complex Activity that Regulates snoRNA Accumulation” Journal of Cell Biology<\/em> 180(3), 563-578 (2008). (PDF file)<\/a><\/li>\n\n\n\n
                                  4. Snider, J., Thibault, G., & Houry<\/strong>, W. A. “The AAA+ superfamily of Functionally Diverse Proteins”, Genome Biology<\/em> 9(4), article 216, 1-8 (2008). (PDF file)<\/a><\/li>\n\n\n\n
                                  5. Snider, J. & Houry<\/strong>, W. A. “AAA+ Proteins: Diversity in Function Similarity in Structure”, Biochemical Society Transactions<\/em> 36(1), 72-77 (2008). (PDF file)<\/a><\/li>\n<\/ol>\n\n\n\n

                                    2007<\/strong><\/h3>\n\n\n\n
                                      \n
                                    1. Houry<\/strong>, W. A. “Overview of Prokaryotic Molecular Chaperones” in Henry Stewart Talks Series on “Molecular Chaperones: Principles and Diseases”, http:\/\/www.hstalks.com\/molchap\/index.htm<\/a>, Walid A. Houry<\/strong>, Editor (2007).<\/li>\n\n\n\n
                                    2. Yu, A. Y.-H., & Houry<\/strong>, W. A. “ClpP: A Distinctive Family of Cylindrical Energy-Dependent Serine Proteases” FEBS Letters<\/em> 581<\/span>(19), 3749-3757 (2007). (PDF file)<\/a><\/li>\n\n\n\n
                                    3. Zhao, R., & Houry<\/strong>, W. A. “Molecular Interaction Network of the Hsp90 Chaperone System” in Molecular Aspects of the Stress Response: Chaperones, Membranes, and Networks, Peter Csermely and Laszlo Vigh, eds. (Landes Bioscience) – part of the series Advances in Experimental Medicine and Biology<\/em>, Vol 594 (2007). (PDF file)<\/a><\/li>\n<\/ol>\n\n\n\n

                                      2006<\/strong><\/h3>\n\n\n\n
                                        \n
                                      1. Thibault, G., Yudin, J., Wong, P., Tsitrin, V., Sprangers, R., Zhao, R., & Houry<\/strong>, W. A. “Specificity in Substrate and Cofactor Recognition by the N-Terminal Domain of the Chaperone ClpX” Proceedings of the National Academy of Sciences <\/em>103 (47), 17724-17729 (2006). (PDF file)<\/a><\/li>\n\n\n\n
                                      2. Thibault, G., Tsitrin, Y., Davidson, T., Gribun, A., & Houry<\/strong>, W. A. “Large Nucleotide-Dependent Movement of the N-Terminal Domain of the ClpX Chaperone” The EMBO Journal <\/em>25 (14), 3367-3376 (2006). (PDF file)<\/a><\/li>\n\n\n\n
                                      3. Snider, J., & Houry<\/strong>, W. A. “MoxR AAA+ ATPases: A Novel Family of Molecular Chaperones?” Journal of Structural Biology <\/em>156 (1), 200\u2013209 (2006). (PDF file)<\/a><\/li>\n\n\n\n
                                      4. Snider, J., Gutsche, I. , Lin, M., Baby, S., Cox, B., Butland, G., Greenblatt, J., Emili, A., & Houry<\/strong>, W. A. “Formation of a Distinctive Complex Between the Inducible Bacterial Lysine Decarboxylase and a Novel AAA+ ATPase” Journal of Biological Chemistry <\/em>281(3), 1532-1546 (2006). (PDF file)<\/a><\/li>\n\n\n\n
                                      5. Wong, K. S. K., & Houry, <\/strong>W. A. “Hsp90 at the Crossroads of Genetics and Epigenetics” Cell Research <\/em>16 (9), 742-749 (2006). (PDF file)<\/a><\/li>\n<\/ol>\n\n\n\n

                                        2005<\/strong><\/h3>\n\n\n\n
                                          \n
                                        1. Sprangers, R., Gribun, A., Hwang, P. M., Houry<\/strong>, W. A., & Kay , L. E. “Quantitative NMR Spectroscopy of Supramolecular Complexes: Dynamic Side Pores in ClpP are Important for Product Release” Proceedings of the National Academy of Sciences <\/em>102(46), 16678-16683 (2005). (PDF file)<\/a><\/li>\n\n\n\n
                                        2. Gribun, A., Kimber, M. S., Ching, R., Spranger, R., Fiebig, K. M., & Houry<\/strong>, W. A. “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” Journal of Biological Chemistry <\/em>280 (16), 16185-16196 (2005). (PDF file)<\/a><\/li>\n\n\n\n
                                        3. Zhao , R., Davey, M., Hsu , Y.-C., Kaplanek , P., Tong, A., Parsons, A., Cagney, G., Mai, D., Krogan, N., Greenblatt, J., Boone, C., Emili, A., & Houry<\/strong>, W. A. “Navigating the Chaperone Network: An Integrative Map of Physical and Genetic Interactions Mediated by the Hsp90 Chaperone” Cell <\/em>120 (5), 715-727 (2005). (PDF file)<\/a><\/li>\n\n\n\n
                                        4. Zhao, R., & Houry<\/strong>, W. A. “Hsp90: A Chaperone for Protein Folding and Gene Regulation” Biochemistry and Cell Biology <\/em>83 (6), 703-710 (2005). (PDF file)<\/a><\/li>\n<\/ol>\n\n\n\n

                                          2004<\/strong><\/h3>\n\n\n\n
                                            \n
                                          1. Wong, P., & Houry<\/strong>, W. A. “Chaperone Networks in Bacteria: Analysis of Protein Homeostasis in Minimal Cells” Journal of Structural Biology <\/em>146 (1-2), 79-89 (2004). (PDF file)<\/a><\/li>\n<\/ol>\n\n\n\n

                                            2003<\/strong><\/h3>\n\n\n\n
                                              \n
                                            1. Donaldson, L. W., Wojtyra, U., & Houry<\/strong>, W. A. “Solution Structure of the Dimeric Zinc Binding Domain of the Chaperone ClpX” Journal of Biological Chemistry <\/em>278 (49), 48991-48996 (2003). (PDF file)<\/a><\/li>\n\n\n\n
                                            2. Wojtyra, U., Thibault, G., Tuite, A., & Houry<\/strong>, W. A. “The N-Terminal Zinc Binding Domain of ClpX is a Dimerization Domain that Modulates the Chaperone Function” Journal of Biological Chemistry <\/em>278 (49), 48981-48990 (2003). (PDF file)<\/a><\/li>\n\n\n\n
                                            3. Wong, P., Kolesov, G., Frishman, D., & Houry<\/strong>, W. A. “Phylogenetic Web Profiler” Bioinformatics<\/em> 19(6), 782-783 (2003). (PDF file)<\/a><\/li>\n<\/ol>\n\n\n\n

                                              2001<\/strong><\/h3>\n\n\n\n
                                                \n
                                              1. Houry<\/strong>, W. A. “Mechanism of Substrate Recognition by the Chaperonin GroEL” Biochemistry and Cell Biology<\/em>, 79(5) , 569-577 (2001). (PDF file)<\/a><\/li>\n\n\n\n
                                              2. Houry<\/strong>, W. A. “Chaperone-Assisted Protein Folding in the Cell Cytoplasm” Current Protein and Peptide Science<\/em>, 2(3), 227-244 (2001). (PDF file)<\/a><\/li>\n<\/ol>\n\n\n\n

                                                1999<\/strong><\/h3>\n\n\n\n
                                                  \n
                                                1. Houry<\/strong>, W. A., Frishman, D., Eckerskorn, C., Lottspeich, F., & Hartl, F. U. “Identification of the In Vivo Substrates of the Chaperonin GroEL” Nature<\/em> 402(11), 147-154 (1999). (PDF file)<\/a><\/li>\n\n\n\n
                                                2. Teter, S. A., Houry<\/strong>, W. A., Ang, D., Tradler, T., Rockabrand, D., Fischer, G., Blum, P., Georgopolous, C., & Hartl, F. U. “Polypeptide Flux through Bacterial Hsp70: DnaK Cooperates with Trigger Factor in Chaperoning Nascent Chains” Cell<\/em> 97(6), 755-765 (1999). (PDF file)<\/a><\/li>\n<\/ol>\n\n\n\n

                                                  1998<\/strong><\/h3>\n\n\n\n
                                                    \n
                                                  1. Houry<\/strong>, W. A., Sauder, J. M., Roder, H., & Scheraga, H. A. “Definition of Amide Protection Factors for Early Kinetic Intermediates in Protein Folding” Proceedings of the National Academy of Sciences 95(8)<\/em>, 4299-4302 (1998). (PDF file)<\/a><\/li>\n<\/ol>\n\n\n\n

                                                    1997<\/strong><\/h3>\n\n\n\n
                                                      \n
                                                    1. Ewalt+, K. L., Hendrick+, J. P., Houry<\/strong>+, W. A., & Hartl, F. U. “In vivo Observation of Polypeptide Flux through the Bacterial Chaperonin System” Cell<\/em> 90(3), 491-500 (1997).
                                                      +These authors contributed equally to this work.                                                       (PDF file)<\/a><\/li>\n<\/ol>\n\n\n\n

                                                      1996<\/strong><\/h3>\n\n\n\n
                                                        \n
                                                      1. Sendak, R. A., Rothwarf, D. M., Wedemeyer, W. J., Houry<\/strong>, W. A., & Scheraga, H. A. “Kinetic and Thermodynamic Studies of the Folding\/Unfolding of a Tryptophan-Containing Mutant of Ribonuclease A” Biochemistry<\/em> 35(39), 12978-12992 (1996). (PDF file)<\/a><\/li>\n\n\n\n
                                                      2. Houry<\/strong>, W. A., & Scheraga, H. A. “Structure of a Hydrophobically Collapsed Intermediate on the Conformational Folding Pathway of Ribonuclease A Probed by Hydrogen-Deuterium Exchange” Biochemistry<\/em> 35(36), 11734-11746 (1996). (PDF file)<\/a><\/li>\n\n\n\n
                                                      3. Houry<\/strong>, W. A., & Scheraga, H. A. “Nature of the Unfolded State of Ribonuclease A: Effect of Cis-Trans X-Pro Peptide Bond Isomerization” Biochemistry<\/em> 35(36), 11719-11733 (1996). (PDF file)<\/a><\/li>\n\n\n\n
                                                      4. Houry<\/strong>, W. A., Rothwarf, D. M., & Scheraga, H. A. “Circular Dichroism Evidence for the Presence of Burst-Phase Intermediates on the Conformational Folding Pathway of Ribonuclease A” Biochemistry<\/em> 35(31), 10125-10133 (1996). (PDF file)<\/a><\/li>\n<\/ol>\n\n\n\n

                                                        1995<\/strong><\/h3>\n\n\n\n
                                                          \n
                                                        1. Houry<\/strong>, W. A., Rothwarf, D. M., & Scheraga, H. A. “The Nature of the Initial Step in the Conformational Folding of Disulfide-Intact Ribonuclease A” Nature Structural Biology<\/em> 2(6), 495-503 (1995). (PDF file)<\/a><\/li>\n<\/ol>\n\n\n\n

                                                          1994<\/strong><\/h3>\n\n\n\n
                                                            \n
                                                          1. Houry<\/strong>, W. A., Rothwarf, D. M., & Scheraga, H. A. “A Very Fast Phase in the Refolding of Disulfide-Intact Ribonuclease A: Implications for the Refolding and Unfolding Pathways” Biochemistry<\/em> 33(9), 2516-2530 (1994). (PDF file)<\/a><\/li>\n<\/ol>\n","protected":false},"excerpt":{"rendered":"

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