Publications

See PubMed for a recent list of publications.

 

2017

  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, W. A. “Features of the Chaperone Cellular Network Revealed through Systematic Interaction Mapping” Cell Reports 20(11), 2735–2748 (2017). (PDF file)
  2. Wong, K. S., Bhandari, V., Janga, S. C., & Houry, W. A. “The RavA-ViaA Chaperone-Like System Interacts with and Modulates the Activity of the Fumarate Reductase Respiratory Complex” Journal of Molecular Biology 429(2), 324–344 (2017). (PDF file)
  3. Kumar, A., Rizzolo, K., Babu, M., & Houry, W. A. “Systematic Approaches for the Analysis of Chaperone Interaction Networks” Methods in Molecular Biology 1709, in press (2017). Stuart K. Calderwood and Thomas L. Prince (eds.), Chaperones: Methods and Protocols, Springer Science+Business Media LLC 2018.
  4. Mao, Y.-Q. & Houry, W. A. “The Role of Pontin and Reptin in Cellular Physiology and Cancer Etiology” Frontiers in Molecular Biosciences (section Protein Folding, Misfolding and Degradation) 4:58. doi: 10.3389/fmolb.2017.00058 (2017). (PDF file)

 

2016

  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., Pomès, R., Sharpe, S., & Houry, W. A. “Mechanism of Amyloidogenesis of a Bacterial AAA+ Chaperone” Structure 24(7), 1095–1109 (2016). (PDF file)
  2. Ewens, C. A., Su, M., Zhao,L., Nano, N., Houry, W. A., & Southworth, D. R. “Architecture and Nucleotide-Dependent Conformational States of the Rvb1-Rvb2 AAA+ Complex” Structure 24(5), 657–666 (2016). (PDF file)
  3. Kandiah, E., Carriel, D., Perard, J., Malet, H., Bacia, M., Liu, K., Chan, S. W. S., Houry, W. A., Ollagnier de Choudens, S., Elsen, S., & Gutsche, I. “Lessons from Structures of E. coli Lysine Decarboxylases” Scientific Reports 6:24601 | DOI: 10.1038/srep24601 (2016). (PDF file)
  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, W. A., Batey, R. A. “Development and Characterization of Potent Cyclic Acyldepsipeptide Analogues with Increased Antimicrobial Activity” Journal of Medicinal Chemsitry 59(2), 624-646 (2016). (PDF file)

 

2015

  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, 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. “Inhibition of the Mitochondrial Protease ClpP as a Therapeutic Strategy for Human Acute Myeloid Leukemia” Cancer Cell 27(6), 864-876 (2015). (PDF file)
  2. Jeganathan, A., Leong, V., Zhao, L., Huen, J., Nano, N., Houry, W. A., & Ortega, J. “Yeast Rvb1 and Rvb2 proteins oligomerize as a conformationally variable dodecamer with low frequency” Journal of Molecular Biology 427(10), 1875–1886 (2015). (PDF file)
  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, W. A., Emili, A., Morris, Q., Bader, G., & Babu, M. “Novel function discovery with GeneMANIA: a new integrated resource for gene function prediction in Escherichia coliBioinformatics 31(3), 306-310 (2015). (PDF file)
  4. Matias, P. M., Baek, S. H., Bandeiras, T. M., Dutta, A., Houry, W. A., Llorca, O., Rosenbaum, J. “The AAA+ Proteins Pontin and Reptin Enter Adult Age: From Understanding Their Basic Biology to the Identification of Selective Inhibitors” Frontiers in Molecular Biosciences (section Protein Folding, Misfolding and Degradation) 2:17, 1-7. doi: 10.3389/fmolb.2015.00017 (2015). (PDF file)
  5. Bhandari, V. & Houry, W. A. “Substrate Interaction Networks of the Escherichia coli Chaperones: Trigger Factor, DnaK and GroEL” in the book Prokaryotic Systems Biology, Mohan Babu and Nevan J. Krogan (Editors). Volume 883 of the series Advances in Experimental Medicine and Biology, pages 271-294. Springer International Publishing AG, Cham, Switzerland (2015). (PDF file)

 

2014

  1. Goodreid, J. D., Wong, K., Leung, E., McCaw, S. E., Gray-Owen, S. D., Lough, A., Houry, W. A., & Batey, R. A. “Total Synthesis and Antibacterial Testing of the A54556 Cyclic Acyldepsipeptides Isolated from Streptomyces hawaiiensisJournal of Natural Products 77(10), 2170−2181 (2014). (PDF file)
  2. Malet, H., Liu, K., El Bakkouri, M., Chan, S. W. S., Effantin, G., Bacia, M., Houry*, W. A., & Gutsche*, I. “Assembly Principles of a Unique Cage Formed by Hexameric and Decameric E. coli Proteins” eLife 3: e03653, 1-11. doi: 10.7554/eLife.03653 (2014). *Co-corresponding authors. (PDF file)
  3. Kakihara, Y., Makhnevych, T., Zhao, L., Tang, W., & Houry, W. A. “Nutritional Status Modulates Box C/D snoRNP Biogenesis by Regulated Subcellular Relocalization of the R2TP Complex” Genome Biology 15(7): 404, 1-20 (2014). (PDF file)
  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, W. A., Parkinson, J., & Emili, A. “Quantitative Genome-Wide Genetic Interaction Screens Reveal Global Epistatic Relationships of Protein Complexes in Escherichia coliPLOS Genetics 10(2): e1004120, 1-15. doi: 10.1371/journal.pgen.1004120 (2014). (PDF file)
  5. Wong, K. S., Snider, J. D., Graham, C., Greenblatt, J. F., Emili, A., Babu, M., & Houry, W. A. “The MoxR ATPase RavA and its Cofactor ViaA Interact with the NADH:Ubiquinone Oxidoreductase I in Escherichia coliPLOS ONE 9(1): e85529, 1-15. doi:10.1371/journal.pone.0085529 (2014). (PDF file)
  6. Liu, K., Ologbenla, A., & Houry, W. A. “Dynamics of the ClpP Serine Protease: A Model for Self-Compartmentalized Proteases” Critical Reviews in Biochemistry and Molecular Biology 49(5), 400-412 (2014). (PDF file)
  7. Rizzolo, K., Wong, P., Tillier, E. R. M., & Houry, 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)
  8. Liu, K. & Houry, W. A. “Chaperones and Proteases of Plasmodium falciparum” in the book Heat Shock Proteins of Malaria, Addmore Shonhai and Gregory L. Blatch (Editors). Springer Science + Business Media Dordrecht (2014). (PDF file)

 

2013

  1. Kamano, Y., Saeki, M., Egusa, H., Kakihara, Y., Houry, W. A., Yatani, H., & Kamisaki, Y. “PIH1D1 Interacts with mTOR Complex 1 and Enhances Ribosome RNA Transcription” FEBS Letters 587(20), 3303-3308 (2013). (PDF file)
  2. Saeki, M., Egusa, H., Kamano, Y., Kakihara, Y., Houry, W. A., Yatani, H., Noguchi, S., & Kamisaki, Y. “Exosome-Bound WD Repeat Protein Monad Inhibits Breast Cancer Cell Invasion by Degrading Amphiregulin mRNA” PLOS ONE 8(7): e67326, 1-11. doi:10.1371/journal.pone.0067326 (2013). (PDF file)
  3. El Bakkouri, M., Rathore, S., Calmettes, C., Wernimont, A. K., Liu, K., Sinha, D., Asad, M., Jung, P., Hui, R., Mohmmed, A., & Houry, W. A. “Structural Insights into the Inactive Subunit of the Apicoplast-Localized Caseinolytic Protease Complex of Plasmodium falciparum” The Journal of Biological Chemistry 288(2), 1022-1031 (2013). (PDF file)
  4. Kanjee, U. & Houry, W. A. “Mechanisms of Acid Resistance in Escherichia coliAnnual Review of Microbiology 67, 65-81 (2013). (PDF file)
  5. Makhnevych, T. & Houry, W. A. “The Control of Spindle Length by Hsp70 and Hsp110 Molecular Chaperones” FEBS Letters 587(8), 1067-1072 (2013). (PDF file)
  6. Nano, N. & Houry, W. A. “Chaperone-Like Activity of the AAA+ Proteins Rvb1 and Rvb2 in the Assembly of Various Complexes” Philosophical Transactions of the Royal Society B 368(1617):20110399, 1-12. doi: 10.1098/rstb.2011.0399 (2013). (PDF file)
  7. Rosenbaum, J., Baek, S. H., Dutta, A., Houry, W. A., Huber, O., Hupp, T. R., & Matias, P. M. “The Emergence of the Conserved AAA+ ATPases Pontin and Reptin on the Signaling Landscape” Science Signaling 6(266) mr1, 1-6 (2013). (PDF file)

 

2012

  1. Paci, A., Liu, X. H., Huang, H., Lim, A., Houry, 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 287(52), 43205–43214 (2012). (PDF file)
  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 198(4), 623-636 (2012). (PDF file)
  3. Thibault, G. & Houry, 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 6(23), 6717-6724 (2012). (PDF file)
  4. Jiméneza, B., Ugwu, F., Zhao, R., Ortía, L., Makhnevych, T., Pineda-Lucena, A., & Houry, 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 287(8), 5698-5709 (2012). (PDF file)
  5. Kanjee, U., Ogata, K., & Houry, W. A. “Direct Binding Targets of the Stringent Response Alarmone (p)ppGpp” Molecular Microbiology 85(6), 1029-1043 (2012). (PDF file)
  6. Wong, K. S. & Houry, W. A. “Novel Structural and Functional Insights into the MoxR Family of AAA+ ATPases” Journal of Structural Biology 179(2), 211-221 (2012). (PDF file)
  7. Makhnevych, T. & Houry, W. A. “The Role of Hsp90 in Protein Complex Assembly” Biochimica et Biophysica Acta – Molecular Cell Research 1823(3), 674-682 (2012). (PDF file)
  8. Kakihara, Y. & Houry, W. A. “The R2TP Complex: Discovery and Functions” Biochimica et Biophysica Acta – Molecular Cell Research 1823(1), 101-107 (2012). (PDF file)
  9. Houry, 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.

 

2011

  1. Kanjee, U., Gutsche, I., Ramachandran, S., & Houry, 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 50(43), 9388-9398 (2011). (PDF file)
  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, W. A. “Activators of Cylindrical Proteases as Antimicrobials: Identification and Development of Novel Small Molecule Activators of the ClpP Protease” Chemistry & Biology 18(9), 1167–1178 (2011). (PDF file)
  3. Kanjee, U., Gutsche, I., Alexopoulos, E., Zhao, B., El Bakkouri, M., Thibault, G., Liu, K., Ramachandran, S., Snider, J., Pai, E. F., & Houry, W. A. “Linkage between the Bacterial Acid Stress and Stringent Responses Revealed by the Structure of the Inducible Lysine Decarboxylase” The EMBO Journal 30(5), 931-944 (2011). (PDF file)
  4. Gong, Y, Zhang, Z., & Houry. W. A. “Bioinformatic Approach to Identify Chaperone Pathway Relationship from Large-Scale Interaction Networks” Methods in Molecular Biology 787, 189-203 (2011). (PDF file)

2010

  1. El Bakkouri, M., Gutsche, I., Kanjee, U., Zhao, B., Yu, M., Goret, G., Schoehn, G., Burmeister, W. P., & Houry, 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 107(52), 22499-22504 (2010). (PDF file)
  2. Cheung, K. L. Y., Huen, J., Kakihara, Y., Houry, W. A., & Ortega, J. “Alternative Oligomeric States of the Yeast Rvb1/Rvb2 Complex Induced by Histidine Tags” Journal of Molecular Biology 404(3), 478-492 (2010). (PDF file)
  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, W. A. “The Clp Chaperones and Proteases of the Human Malaria Parasite Plasmodium falciparumJournal of Molecular Biology 404(3), 456-477 (2010). (PDF file)
  4. Kimber, M. S., Yu, A. Y. H., Borg, M., Chan, H. S., & Houry, W. A. “The Structure of a Disulfide Cross-Linked ClpP Protease: Implications for ClpP Dynamics” Structure 18(7), 798-808 (2010). (PDF file)
  5. Zhao, R., Leung, E., Gruener, S., Schapira, M., & Houry, W. A. “Tamoxifen Enhances the Hsp90 Molecular Chaperone ATPase Activity” PLoS ONE 5(4):e9934, 1-8 (2010). (PDF file)
  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, W. A., Brudno, M., Ragibizadeh, S., Papp, B., Pál, 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 327(5964), 425-431 (2010). (PDF file)
  7. Kanjee, U. & Houry, W. A. “An Assay for Measuring the Activity of Escherichia coli Inducible Lysine Decarboxyase” http://www.jove.com/details.stp?id=2094 doi: 10.3791/2094 Journal of Visualized Experiments 46 (2010). (PDF file)
  8. Zhao, B. & Houry, W. A. “Acid Stress Response in Enteropathogenic Gammaproteobacteria: An Aptitude for Survival” Biochemistry and Cell Biology 88(2), 301–314 (2010). (PDF file)
  9. Cheung, K., Huen, J., Houry, W. A., & Ortega, J. “Comparison of the Multiple Oligomeric Structures Observed for the Rvb1 and Rvb2 Proteins” Biochemistry and Cell Biology 88(1), 77-88 (2010). (PDF file)
  10. Huen, J., Kakihara, Y., Ugwu, F., Cheung, K. L. Y., Ortega, J., & Houry, W. A. “Rvb1-Rvb2: Essential ATP-Dependent Helicases for Critical Complexes” Biochemistry and Cell Biology 88(1), 29-40 (2010). (PDF file)
  11. Houry, W. A. & Ortega, J. “AAA Proteins: Movers and Shakers” (2010) Biochemistry and Cell Biology 88(1), i-iv (2010). (PDF file)

 

2009

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

 

2008

  1. Alexopoulos, E., Kanjee, U., Snider, J., Houry, 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 64(8),700-706 (2008). (PDF file)
  2. Gribun, A., Cheung, K. L. Y., Huen, J., Ortega, J., & Houry, W. A. “Yeast Rvb1 and Rvb2 are ATP-Dependent DNA Helicases that Form a Heterohexameric Complex” Journal of Molecular Biology 376(5), 1320-1333 (2008). (PDF file)
  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, W. A. “Molecular Chaperone Hsp90 Stabilizes Pih1/Nop17 to Maintain R2TP Complex Activity that Regulates snoRNA Accumulation” Journal of Cell Biology 180(3), 563-578 (2008). (PDF file)
  4. Snider, J., Thibault, G., & Houry, W. A. “The AAA+ superfamily of Functionally Diverse Proteins”, Genome Biology 9(4), article 216, 1-8 (2008). (PDF file)
  5. Snider, J. & Houry, W. A. “AAA+ Proteins: Diversity in Function Similarity in Structure”, Biochemical Society Transactions 36(1), 72-77 (2008). (PDF file)

 

2007

  1. Houry, 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, Walid A. Houry, Editor (2007).
  2. Yu, A. Y.-H., & Houry, W. A. “ClpP: A Distinctive Family of Cylindrical Energy-Dependent Serine Proteases” FEBS Letters 581(19), 3749-3757 (2007). (PDF file)
  3. Zhao, R., & Houry, 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, Vol 594 (2007). (PDF file)

 

2006

  1. Thibault, G., Yudin, J., Wong, P., Tsitrin, V., Sprangers, R., Zhao, R., & Houry, W. A. “Specificity in Substrate and Cofactor Recognition by the N-Terminal Domain of the Chaperone ClpX” Proceedings of the National Academy of Sciences 103 (47), 17724-17729 (2006). (PDF file)
  2. Thibault, G., Tsitrin, Y., Davidson, T., Gribun, A., & Houry, W. A. “Large Nucleotide-Dependent Movement of the N-Terminal Domain of the ClpX Chaperone” The EMBO Journal 25 (14), 3367-3376 (2006). (PDF file)
  3. Snider, J., & Houry, W. A. “MoxR AAA+ ATPases: A Novel Family of Molecular Chaperones?” Journal of Structural Biology 156 (1), 200–209 (2006). (PDF file)
  4. Snider, J., Gutsche, I. , Lin, M., Baby, S., Cox, B., Butland, G., Greenblatt, J., Emili, A., & Houry, W. A. “Formation of a Distinctive Complex Between the Inducible Bacterial Lysine Decarboxylase and a Novel AAA+ ATPase” Journal of Biological Chemistry 281(3), 1532-1546 (2006). (PDF file)
  5. Wong, K. S. K., & Houry, W. A. “Hsp90 at the Crossroads of Genetics and Epigenetics” Cell Research 16 (9), 742-749 (2006). (PDF file)

 

2005

  1. Sprangers, R., Gribun, A., Hwang, P. M., Houry, 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 102(46), 16678-16683 (2005). (PDF file)
  2. Gribun, A., Kimber, M. S., Ching, R., Spranger, R., Fiebig, K. M., & Houry, 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 280 (16), 16185-16196 (2005). (PDF file)
  3. Zhao, R., & Houry, W. A. “Hsp90: A Chaperone for Protein Folding and Gene Regulation” Biochemistry and Cell Biology 83 (6), 703-710 (2005). (PDF file)
  4. 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, W. A. “Navigating the Chaperone Network: An Integrative Map of Physical and Genetic Interactions Mediated by the Hsp90 Chaperone” Cell 120 (5), 715-727 (2005). (PDF file)

 

2004

  1. Wong, P., & Houry, W. A. “Chaperone Networks in Bacteria: Analysis of Protein Homeostasis in Minimal Cells” Journal of Structural Biology 146 (1-2), 79-89 (2004). (PDF file)

 

2003

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

 

2001

  1. Houry, W. A. “Mechanism of Substrate Recognition by the Chaperonin GroEL” Biochemistry and Cell Biology, 79(5) , 569-577 (2001). (PDF file)
  2. Houry, W. A. “Chaperone-Assisted Protein Folding in the Cell Cytoplasm” Current Protein and Peptide Science, 2(3), 227-244 (2001). (PDF file)

 

1999

  1. Houry, W. A., Frishman, D., Eckerskorn, C., Lottspeich, F., & Hartl, F. U. “Identification of the In Vivo Substrates of the Chaperonin GroEL” Nature 402(11), 147-154 (1999). (PDF file)
  2. Teter, S. A., Houry, 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 97(6), 755-765 (1999). (PDF file)

 

1998

  1. Houry, 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), 4299-4302 (1998). (PDF file)

 

1997

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

 

1996

  1. Sendak, R. A., Rothwarf, D. M., Wedemeyer, W. J., Houry, W. A., & Scheraga, H. A. “Kinetic and Thermodynamic Studies of the Folding/Unfolding of a Tryptophan-Containing Mutant of Ribonuclease A” Biochemistry 35(39), 12978-12992 (1996). (PDF file)
  2. Houry, 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 35(36), 11734-11746 (1996). (PDF file)
  3. Houry, W. A., & Scheraga, H. A. “Nature of the Unfolded State of Ribonuclease A: Effect of Cis-Trans X-Pro Peptide Bond Isomerization” Biochemistry 35(36), 11719-11733 (1996). (PDF file)
  4. Houry, 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 35(31), 10125-10133 (1996). (PDF file)

 

1995

  1. Houry, 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 2(6), 495-503 (1995). (PDF file)

 

1994

  1. Houry, 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 33(9), 2516-2530 (1994). (PDF file)
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