참고문헌 (70)

1. Doyle, Shannon M., Genest, Olivier, Wickner, Sue. Protein rescue from aggregates by powerful molecular chaperone machines. Nature reviews. Molecular cell biology, vol.14, no.10, 617-629.

   상세보기

2. Hayer-Hartl, MK, Martin, J, Hartl, FU. Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding. Science, vol.269, no.5225, 836-841.

   상세보기

3. Todd, MJ, Viitanen, PV, Lorimer, GH. Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. Science, vol.265, no.5172, 659-666.

   상세보기

4. Thomas, Jeffrey G., Baneyx, François. ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells. Molecular microbiology, vol.36, no.6, 1360-1370.

   상세보기

5. Hartl, F. Ulrich, Bracher, Andreas, Hayer-Hartl, Manajit. Molecular chaperones in protein folding and proteostasis. Nature, vol.475, no.7356, 324-332.

   상세보기

6. Corrales, F J, Fersht, A R. Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage.. Proceedings of the National Academy of Sciences of the United States of America, vol.93, no.9, 4509-4512.

   상세보기

7. 10.1038/s41580‐019‐0183‐6 

   

8. Zolkiewski, M., Zhang, T., Nagy, M.. Aggregate reactivation mediated by the Hsp100 chaperones. Archives of biochemistry and biophysics, vol.520, no.1, 1-6.

   상세보기

9. Saibil, Helen. Chaperone machines for protein folding, unfolding and disaggregation. Nature reviews. Molecular cell biology, vol.14, no.10, 630-642.

   상세보기

10. Duran, Elizabeth C., Weaver, Clarissa L., Lucius, Aaron L.. Comparative Analysis of the Structure and Function of AAA+ Motors ClpA, ClpB, and Hsp104: Common Threads and Disparate Functions. Frontiers in molecular biosciences, vol.4, 54-.

    상세보기

11. 10.1046/j.1365‐2443.2001.00447.x 

    

12. Doyle, S.M., Wickner, S.. Hsp104 and ClpB: protein disaggregating machines. Trends in biochemical sciences, vol.34, no.1, 40-48.

    상세보기

13. Wang, Feng, Mei, Ziqing, Qi, Yutao, Yan, Chuangye, Hu, Qi, Wang, Jiawei, Shi, Yigong. Structure and mechanism of the hexameric MecA？?ClpC molecular machine. Nature, vol.471, no.7338, 331-335.

    상세보기

14. Kirstein, Janine, Molière, Noël, Dougan, David A., Turgay, Kür？ad. Adapting the machine: adaptor proteins for Hsp100/Clp and AAA+ proteases. Nature reviews. Microbiology, vol.7, no.8, 589-599.

    상세보기

15. Sweeny, E.A., Shorter, J.. Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104. Journal of molecular biology, vol.428, no.9, 1870-1885.

    상세보기

16. 10.1186/s12866‐020‐1719‐9 

    

17. 10.1038/s41594‐020‐0409‐5 

    

18. Zolkiewski, Michal. ClpB Cooperates with DnaK, DnaJ, and GrpE in Suppressing Protein Aggregation. The Journal of biological chemistry, vol.274, no.40, 28083-28086.

    상세보기

19. Lee, Sukyeong, Sowa, Mathew E, Watanabe, Yo-hei, Sigler, Paul B, Chiu, Wah, Yoshida, Masasuke, Tsai, Francis T.F. The Structure of ClpB : A Molecular Chaperone that Rescues Proteins from an Aggregated State. Cell, vol.115, no.2, 229-240.

    상세보기

20. Kim, K.I., Cheong, G.W., Park, S.C., Ha, J.S., Woo, K.M., Choi, S.J., Chung, C.H.. Heptameric ring structure of the heat-shock protein ClpB, a protein-activated ATPase in Escherichia coli. Journal of molecular biology, vol.303, no.5, 655-666.

    상세보기

21. Carroni, Marta, Franke, Kamila B, Maurer, Michael, Jäger, Jasmin, Hantke, Ingo, Gloge, Felix, Linder, Daniela, Gremer, Sebastian, Turgay, Kürşad, Bukau, Bernd, Mogk, Axel. Regulatory coiled-coil domains promote head-to-head assemblies of AAA+ chaperones essential for tunable activity control. eLife, vol.6, e30120-.

    상세보기

22. Biter, Amadeo B., Lee, Sukyeong, Sung, Nuri, Tsai, Francis T.F.. Structural basis for intersubunit signaling in a protein disaggregating machine. Proceedings of the National Academy of Sciences of the United States of America, vol.109, no.31, 12515-12520.

    상세보기

23. Yamasaki, Takashi, Oohata, Yukiko, Nakamura, Toshiki, Watanabe, Yo-hei. Analysis of the Cooperative ATPase Cycle of the AAA+ Chaperone ClpB from Thermus thermophilus by Using Ordered Heterohexamers with an Alternating Subunit Arrangement. The Journal of biological chemistry, vol.290, no.15, 9789-9800.

    상세보기

24. Li, Tao, Weaver, Clarissa L., Lin, Jiabei, Duran, Elizabeth C., Miller, Justin M., Lucius, Aaron L.. Escherichia coli ClpB is a non-processive polypeptide translocase. The Biochemical journal, vol.470, no.1, 39-52.

    상세보기

25. Kedzierska, S., Akoev, V., Barnett, M. E., Zolkiewski, M.. Structure and Function of the Middle Domain of ClpB from Escherichia coli. Biochemistry, vol.42, no.48, 14242-14248.

    상세보기

26. Lee, Sukyeong, Sowa, Mathew E., Choi, Jae-Mun, Tsai, Francis T.F.. The ClpB/Hsp104 molecular chaperone—a protein disaggregating machine. Journal of structural biology, vol.146, no.1, 99-105.

    상세보기

27. Yokom, Adam L, Gates, Stephanie N, Jackrel, Meredith E, Mack, Korrie L, Su, Min, Shorter, James, Southworth, Daniel R. Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocation. Nature structural & molecular biology, vol.23, no.9, 830-837.

    상세보기

28. Gates, Stephanie N., Yokom, Adam L., Lin, JiaBei, Jackrel, Meredith E., Rizo, Alexandrea N., Kendsersky, Nathan M., Buell, Courtney E., Sweeny, Elizabeth A., Mack, Korrie L., Chuang, Edward, Torrente, Mariana P., Su, Min, Shorter, James, Southworth, Daniel R.. Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104. Science, vol.357, no.6348, 273-279.

    상세보기

29. Deville, Célia, Carroni, Marta, Franke, Kamila B., Topf, Maya, Bukau, Bernd, Mogk, Axel, Saibil, Helen R.. Structural pathway of regulated substrate transfer and threading through an Hsp100 disaggregase. Science advances, vol.3, no.8, e1701726-.

    상세보기

30. 10.1038/s41467‐019‐10150‐y 

    

31. Shorter, James, Southworth, Daniel R.. Spiraling in Control: Structures and Mechanisms of the Hsp104 Disaggregase. Cold Spring Harbor perspectives in biology, vol.11, no.8, a034033-a034033.

    상세보기

32. Miller, Justin M., Chaudhary, Hamza, Marsee, Justin D.. Phylogenetic analysis predicts structural divergence for proteobacterial ClpC proteins. Journal of structural biology, vol.201, no.1, 52-62.

    상세보기

33. Park, Sang‐Sang, Kwon, Hyog‐Young, Tran, Thao Dang‐Hien, Choi, Moo‐Hyun, Jung, Seung‐Ha, Lee, Sangho, Briles, David E., Rhee, Dong‐Kwon. ClpL is a chaperone without auxiliary factors. The FEBS journal, vol.282, no.8, 1352-1367.

    상세보기

34. Zhang, Xiaodong, Wigley, Dale B. The 'glutamate switch' provides a link between ATPase activity and ligand binding in AAA+ proteins. Nature structural & molecular biology, vol.15, no.11, 1223-1227.

    상세보기

35. Schuck, Peter, Gillis, Richard B., Besong, Tabot M. D., Almutairi, Fahad, Adams, Gary G., Rowe, Arthur J., Harding, Stephen E.. SEDFIT–MSTAR: molecular weight and molecular weight distribution analysis of polymers by sedimentation equilibrium in the ultracentrifuge. The Analyst : An International Journal of Analytical and Bioanalytical Science, vol.139, no.1, 79-92.

    상세보기

36. 1992 Royal Society of Chemistry London T Laue B Shah T Ridgeway PS En SE Harding HC Horton AJ Rowe Analytical ultracentrifugation in biochemistry & polymer science 90 125 

37. Scheres, Sjors H.W.. RELION: Implementation of a Bayesian approach to cryo-EM structure determination. Journal of structural biology, vol.180, no.3, 519-530.

    상세보기

38. Li, Xueming, Mooney, Paul, Zheng, Shawn, Booth, Chris, Braunfeld, Michael B., Gubbens, Sander, Agard, David A., Cheng, Yifan. Electron counting and beam-induced motion correction enable near atomic resolution single particle cryoEM. Nature methods, vol.10, no.6, 584-590.

    상세보기

39. Rohou, A., Grigorieff, N.. CTFFIND4: Fast and accurate defocus estimation from electron micrographs. Journal of structural biology, vol.192, no.2, 216-221.

    상세보기

40. Heymann, J. Bernard, Belnap, David M.. Bsoft: Image processing and molecular modeling for electron microscopy. Journal of structural biology, vol.157, no.1, 3-18.

    상세보기

41. Grant, Timothy, Rohou, Alexis, Grigorieff, Nikolaus. cis TEM, user-friendly software for single-particle image processing. eLife, vol.7, e35383-.

    상세보기

42. Pettersen, Eric F., Goddard, Thomas D., Huang, Conrad C., Couch, Gregory S., Greenblatt, Daniel M., Meng, Elaine C., Ferrin, Thomas E.. UCSF Chimera—A visualization system for exploratory research and analysis. Journal of computational chemistry, vol.25, no.13, 1605-1612.

    상세보기

43. Emsley, Paul, Cowtan, Kevin. Coot: model-building tools for molecular graphics. Acta crystallographica. Section D, Biological crystallography, vol.60, no.12, 2126-2132.

    상세보기

44. Adams, Paul D., Afonine, Pavel V., Bunkóczi, Gábor, Chen, Vincent B., Davis, Ian W., Echols, Nathaniel, Headd, Jeffrey J., Hung, Li-Wei, Kapral, Gary J., Grosse-Kunstleve, Ralf W., McCoy, Airlie J., Moriarty, Nigel W., Oeffner, Robert, Read, Randy J., Richardson, David C., Richardson, Jane S., Terwilliger, Thomas C., Zwart, Peter H.. PHENIX : a comprehensive Python-based system for macromolecular structure solution. Acta crystallographica. Section D, Biological crystallography, vol.66, no.2, 213-221.

    상세보기

45. Wang, Ray Yu-Ruei, Song, Yifan, Barad, Benjamin A, Cheng, Yifan, Fraser, James S, DiMaio, Frank. Automated structure refinement of macromolecular assemblies from cryo-EM maps using Rosetta. eLife, vol.5, e17219-.

    상세보기

46. 10.1107/S0021889892001663 

    

47. Franke, D., Petoukhov, M. V., Konarev, P. V., Panjkovich, A., Tuukkanen, A., Mertens, H. D. T., Kikhney, A. G., Hajizadeh, N. R., Franklin, J. M., Jeffries, C. M., Svergun, D. I.. ATSAS 2.8 : a comprehensive data analysis suite for small-angle scattering from macromolecular solutions. Journal of applied crystallography, vol.50, no.4, 1212-1225.

    상세보기

48. Franke, Daniel, Svergun, Dmitri I.. DAMMIF , a program for rapid ab-initio shape determination in small-angle scattering. Journal of applied crystallography, vol.42, no.2, 342-346.

    상세보기

49. Volkov, Vladimir V., Svergun, Dmitri I.. Uniqueness of ab initio shape determination in small-angle scattering. Journal of applied crystallography, vol.36, no.3, 860-864.

    상세보기

50. 10.1016/S0006‐3495(99)77443‐6 

    

51. Kozin, M. B., Svergun, D. I.. Automated matching of high- and low-resolution structural models. Journal of applied crystallography, vol.34, no.1, 33-41.

    상세보기

52. Saeed, I.A., Ashraf, S.S.. Denaturation studies reveal significant differences between GFP and blue fluorescent protein. International journal of biological macromolecules, vol.45, no.3, 236-241.

    상세보기

53. Liu, Jing, Mei, Ziqing, Li, Ningning, Qi, Yutao, Xu, Yanji, Shi, Yigong, Wang, Feng, Lei, Jianlin, Gao, Ning. Structural Dynamics of the MecA-ClpC Complex : A TYPE II AAA⁺ PROTEIN UNFOLDING MACHINE. The Journal of biological chemistry, vol.288, no.24, 17597-17608.

    상세보기

54. Zolkiewski, Michal, Kessel, Martin, Ginsburg, Ann, Maurizi, Michael R.. Nucleotide‐dependent oligomerization of C1pB from Escherichia coli. Protein science : a publication of the Protein Society, vol.8, no.9, 1899-1903.

    상세보기

55. Shiau, Andrew K., Harris, Seth F., Southworth, Daniel R., Agard, David A.. Structural Analysis of E. coli hsp90 Reveals Dramatic Nucleotide-Dependent Conformational Rearrangements. Cell, vol.127, no.2, 329-340.

    상세보기

56. Ewens, Caroline A., Su, M., Zhao, L., Nano, N., Houry, Walid A., Southworth, Daniel R.. Architecture and Nucleotide-Dependent Conformational Changes of the Rvb1-Rvb2 AAA+ Complex Revealed by Cryoelectron Microscopy. Structure, vol.24, no.5, 657-666.

    상세보기

57. Yu, Hongjun, Lupoli, Tania J., Kovach, Amanda, Meng, Xing, Zhao, Gongpu, Nathan, Carl F., Li, Huilin. ATP hydrolysis-coupled peptide translocation mechanism of Mycobacterium tuberculosis ClpB. Proceedings of the National Academy of Sciences of the United States of America, vol.115, no.41, E9560-E9569.

    상세보기

58. Lipińska, Natalia, Ziętkiewicz, Szymon, Sobczak, Alicja, Jurczyk, Agnieszka, Potocki, Wojciech, Morawiec, Ewa, Wawrzycka, Aleksandra, Gumowski, Krzysztof, Ślusarz, Magdalena, Rodziewicz-Motowidło, Sylwia, Chruściel, Elżbieta, Liberek, Krzysztof. Disruption of Ionic Interactions between the Nucleotide Binding Domain 1 (NBD1) and Middle (M) Domain in Hsp100 Disaggregase Unleashes Toxic Hyperactivity and Partial Independence from Hsp70. The Journal of biological chemistry, vol.288, no.4, 2857-2869.

    상세보기

59. DeSantis, Morgan E., Sweeny, Elizabeth A., Snead, David, Leung, Eunice H., Go, Michelle S., Gupta, Kushol, Wendler, Petra, Shorter, James. Conserved Distal Loop Residues in the Hsp104 and ClpB Middle Domain Contact Nucleotide-binding Domain 2 and Enable Hsp70-dependent Protein Disaggregation. The Journal of biological chemistry, vol.289, no.2, 848-867.

    상세보기

60. Carroni, Marta, Kummer, Eva, Oguchi, Yuki, Wendler, Petra, Clare, Daniel K, Sinning, Irmgard, Kopp, Jürgen, Mogk, Axel, Bukau, Bernd, Saibil, Helen R. Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation. eLife, vol.3, e02481-.

    상세보기

61. Rambo, Robert P., Tainer, John A.. Characterizing flexible and intrinsically unstructured biological macromolecules by SAS using the Porod‐Debye law. Biopolymers, vol.95, no.8, 559-571.

    상세보기

62. Barnett, Micheal E., Zolkiewska, Anna, Zolkiewski, Michal. Structure and Activity of ClpB from Escherichia coli. The Journal of biological chemistry, vol.275, no.48, 37565-37571.

    상세보기

63. Akoev, Vladimir, Gogol, Edward P., Barnett, Micheal E., Zolkiewski, Michal. Nucleotide‐induced switch in oligomerization of the AAA⁺ ATPase ClpB. Protein science : a publication of the Protein Society, vol.13, no.3, 567-574.

    상세보기

64. Rohrwild, Markus, Pfeifer, Günter, Santarius, Ute, Müller, Shirley A., Huang, H.-C., Engel, Andreas, Baumeister, Wolfgang, Goldberg, Alfred L.. The ATP-dependent HslVU protease from Escherichia coli is a four-ring structure resembling the proteasome. Nature structural biology, vol.4, no.2, 133-139.

    상세보기

65. Miyata, T., Yamada, K., Iwasaki, H., Shinagawa, H., Morikawa, K., Mayanagi, K.. Two Different Oligomeric States of the RuvB Branch Migration Motor Protein as Revealed by Electron Microscopy. Journal of structural biology, vol.131, no.2, 83-89.

    상세보기

66. Ishikawa, Takashi, Beuron, Fabienne, Kessel, Martin, Wickner, Sue, Maurizi, Michael R., Steven, Alasdair C.. Translocation pathway of protein substrates in ClpAP protease. Proceedings of the National Academy of Sciences of the United States of America, vol.98, no.8, 4328-4333.

    상세보기

67. Ripstein, Zev A, Vahidi, Siavash, Houry, Walid A, Rubinstein, John L, Kay, Lewis E. A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery. eLife, vol.9, e52158-.

    상세보기

68. 10.1038/s41594‐019‐0304‐0 

    

69. Kater, Lukas, Wagener, Nikola, Berninghausen, Otto, Becker, Thomas, Neupert, Walter, Beckmann, Roland. Structure of the Bcs1 AAA-ATPase suggests an airlock-like translocation mechanism for folded proteins. Nature structural & molecular biology, vol.27, no.2, 142-149.

    상세보기

70. 10.1186/s12859‐015‐0545‐9 

    

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