Статті в журналах з теми "Protein folding machinery"
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Chiu, Wah. "Center for protein folding machinery." Nanomedicine: Nanotechnology, Biology and Medicine 2, no. 4 (December 2006): 289. http://dx.doi.org/10.1016/j.nano.2006.10.069.
Повний текст джерелаZhang, Xiaodong, Fabienne Beuron, and Paul S. Freemont. "Machinery of protein folding and unfolding." Current Opinion in Structural Biology 12, no. 2 (April 2002): 231–38. http://dx.doi.org/10.1016/s0959-440x(02)00315-9.
Повний текст джерелаBuchner, J. "Introduction: the cellular protein folding machinery." Cellular and Molecular Life Sciences 59, no. 10 (October 2002): 1587–88. http://dx.doi.org/10.1007/pl00012484.
Повний текст джерелаFink, Anthony L. "Chaperone-Mediated Protein Folding." Physiological Reviews 79, no. 2 (April 1, 1999): 425–49. http://dx.doi.org/10.1152/physrev.1999.79.2.425.
Повний текст джерелаRassow, J., K. Mohrs, S. Koidl, I. B. Barthelmess, N. Pfanner, and M. Tropschug. "Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60." Molecular and Cellular Biology 15, no. 5 (May 1995): 2654–62. http://dx.doi.org/10.1128/mcb.15.5.2654.
Повний текст джерелаHartl, F. Ulrich. "Unfolding the chaperone story." Molecular Biology of the Cell 28, no. 22 (November 2017): 2919–23. http://dx.doi.org/10.1091/mbc.e17-07-0480.
Повний текст джерелаSorokina, Irina, Arcady R. Mushegian, and Eugene V. Koonin. "Is Protein Folding a Thermodynamically Unfavorable, Active, Energy-Dependent Process?" International Journal of Molecular Sciences 23, no. 1 (January 4, 2022): 521. http://dx.doi.org/10.3390/ijms23010521.
Повний текст джерелаChoudhury, P., Y. Liu, and RN Sifers. "Quality Control of Protein Folding: Participation in Human Disease." Physiology 12, no. 4 (August 1, 1997): 162–66. http://dx.doi.org/10.1152/physiologyonline.1997.12.4.162.
Повний текст джерелаPedone, Emilia, Danila Limauro, and Simonetta Bartolucci. "The Machinery for Oxidative Protein Folding in Thermophiles." Antioxidants & Redox Signaling 10, no. 1 (January 2008): 157–70. http://dx.doi.org/10.1089/ars.2007.1855.
Повний текст джерелаAller, Isabel, and Andreas J. Meyer. "The oxidative protein folding machinery in plant cells." Protoplasma 250, no. 4 (October 23, 2012): 799–816. http://dx.doi.org/10.1007/s00709-012-0463-x.
Повний текст джерелаSantos, João D., Sara Canato, Ana S. Carvalho, Hugo M. Botelho, Kerman Aloria, Margarida D. Amaral, Rune Matthiesen, Andre O. Falcao, and Carlos M. Farinha. "Folding Status Is Determinant over Traffic-Competence in Defining CFTR Interactors in the Endoplasmic Reticulum." Cells 8, no. 4 (April 14, 2019): 353. http://dx.doi.org/10.3390/cells8040353.
Повний текст джерелаAlonzi, Dominic S., Kathryn A. Scott, Raymond A. Dwek, and Nicole Zitzmann. "Iminosugar antivirals: the therapeutic sweet spot." Biochemical Society Transactions 45, no. 2 (April 13, 2017): 571–82. http://dx.doi.org/10.1042/bst20160182.
Повний текст джерелаKang, Ji An, and Young Joo Jeon. "How Is the Fidelity of Proteins Ensured in Terms of Both Quality and Quantity at the Endoplasmic Reticulum? Mechanistic Insights into E3 Ubiquitin Ligases." International Journal of Molecular Sciences 22, no. 4 (February 19, 2021): 2078. http://dx.doi.org/10.3390/ijms22042078.
Повний текст джерелаMak, Wai Shun, Tsz Ming Tsang, Tsz Yin Chan, and Georgi L. Lukov. "Novel Binding Partners for CCT and PhLP1 Suggest a Common Folding Mechanism for WD40 Proteins with a 7-Bladed Beta-Propeller Structure." Proteomes 9, no. 4 (October 2, 2021): 40. http://dx.doi.org/10.3390/proteomes9040040.
Повний текст джерелаChristian Wigley, W., Rosalind P. Fabunmi, Min Goo Lee, Christopher R. Marino, Shmuel Muallem, George N. DeMartino, and Philip J. Thomas. "Dynamic Association of Proteasomal Machinery with the Centrosome." Journal of Cell Biology 145, no. 3 (May 3, 1999): 481–90. http://dx.doi.org/10.1083/jcb.145.3.481.
Повний текст джерелаMeimaridou, Eirini, Sakina B. Gooljar, and J. Paul Chapple. "From hatching to dispatching: the multiple cellular roles of the Hsp70 molecular chaperone machinery." Journal of Molecular Endocrinology 42, no. 1 (October 13, 2008): 1–9. http://dx.doi.org/10.1677/jme-08-0116.
Повний текст джерелаRoy, Joydeep, Sahana Mitra, Kaushik Sengupta, and Atin K. Mandal. "Hsp70 clears misfolded kinases that partitioned into distinct quality-control compartments." Molecular Biology of the Cell 26, no. 9 (May 2015): 1583–600. http://dx.doi.org/10.1091/mbc.e14-08-1262.
Повний текст джерелаHadden, M. Kyle, Lakshmi Galam, Jason E. Gestwicki, Robert L. Matts, and Brian S. J. Blagg. "Derrubone, an Inhibitor of the Hsp90 Protein Folding Machinery." Journal of Natural Products 70, no. 12 (December 2007): 2014–18. http://dx.doi.org/10.1021/np070190s.
Повний текст джерелаBrownrigg, George P., James Johnson та Elizabeth J. Rideout. "80 - Sex Differences in β-Cell Protein Folding Machinery". Canadian Journal of Diabetes 44, № 7 (жовтень 2020): S32. http://dx.doi.org/10.1016/j.jcjd.2020.08.086.
Повний текст джерелаChambers, Joseph E., and Stefan J. Marciniak. "Cellular Mechanisms of Endoplasmic Reticulum Stress Signaling in Health and Disease. 2. Protein misfolding and ER stress." American Journal of Physiology-Cell Physiology 307, no. 8 (October 15, 2014): C657—C670. http://dx.doi.org/10.1152/ajpcell.00183.2014.
Повний текст джерелаZhao, Rongmin, and Walid A. Houry. "Hsp90: a chaperone for protein folding and gene regulation." Biochemistry and Cell Biology 83, no. 6 (December 1, 2005): 703–10. http://dx.doi.org/10.1139/o05-158.
Повний текст джерелаParray, Zahoor Ahmad, Mohammad Shahid, and Asimul Islam. "Insights into Fluctuations of Structure of Proteins: Significance of Intermediary States in Regulating Biological Functions." Polymers 14, no. 8 (April 11, 2022): 1539. http://dx.doi.org/10.3390/polym14081539.
Повний текст джерелаGandhi, Jason, Anthony C. Antonelli, Adil Afridi, Sohrab Vatsia, Gunjan Joshi, Victor Romanov, Ian V. J. Murray, and Sardar Ali Khan. "Protein misfolding and aggregation in neurodegenerative diseases: a review of pathogeneses, novel detection strategies, and potential therapeutics." Reviews in the Neurosciences 30, no. 4 (May 27, 2019): 339–58. http://dx.doi.org/10.1515/revneuro-2016-0035.
Повний текст джерелаScheuner, Donalyn, та Randal J. Kaufman. "The Unfolded Protein Response: A Pathway That Links Insulin Demand with β-Cell Failure and Diabetes". Endocrine Reviews 29, № 3 (24 квітня 2008): 317–33. http://dx.doi.org/10.1210/er.2007-0039.
Повний текст джерелаZhang, Yongli, and Frederick M. Hughson. "Chaperoning SNARE Folding and Assembly." Annual Review of Biochemistry 90, no. 1 (June 20, 2021): 581–603. http://dx.doi.org/10.1146/annurev-biochem-081820-103615.
Повний текст джерелаLim, Shion A., Kathryn M. Hart, Michael J. Harms, and Susan Marqusee. "Evolutionary trend toward kinetic stability in the folding trajectory of RNases H." Proceedings of the National Academy of Sciences 113, no. 46 (October 31, 2016): 13045–50. http://dx.doi.org/10.1073/pnas.1611781113.
Повний текст джерелаShepherd, Colin, Ojore B. V. Oka та Neil J. Bulleid. "Inactivation of mammalian Ero1α is catalysed by specific protein disulfide-isomerases". Biochemical Journal 461, № 1 (13 червня 2014): 107–13. http://dx.doi.org/10.1042/bj20140234.
Повний текст джерелаBenham, Adam M., Marcel van Lith, Roberto Sitia, and Ineke Braakman. "Ero1–PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum." Philosophical Transactions of the Royal Society B: Biological Sciences 368, no. 1617 (May 5, 2013): 20110403. http://dx.doi.org/10.1098/rstb.2011.0403.
Повний текст джерелаBerner, Nicole, Karl-Richard Reutter, and Dieter H. Wolf. "Protein Quality Control of the Endoplasmic Reticulum and Ubiquitin–Proteasome-Triggered Degradation of Aberrant Proteins: Yeast Pioneers the Path." Annual Review of Biochemistry 87, no. 1 (June 20, 2018): 751–82. http://dx.doi.org/10.1146/annurev-biochem-062917-012749.
Повний текст джерелаSchlebach, Jonathan P., and Charles R. Sanders. "The safety dance: biophysics of membrane protein folding and misfolding in a cellular context." Quarterly Reviews of Biophysics 48, no. 1 (November 25, 2014): 1–34. http://dx.doi.org/10.1017/s0033583514000110.
Повний текст джерелаHood, David A., and Anna-Maria Joseph. "Mitochondrial assembly: protein import." Proceedings of the Nutrition Society 63, no. 2 (May 2004): 293–300. http://dx.doi.org/10.1079/pns2004342.
Повний текст джерелаDaverkausen-Fischer, Lea, Margarethe Draga, and Felicitas Pröls. "Regulation of Translation, Translocation, and Degradation of Proteins at the Membrane of the Endoplasmic Reticulum." International Journal of Molecular Sciences 23, no. 10 (May 17, 2022): 5576. http://dx.doi.org/10.3390/ijms23105576.
Повний текст джерелаStubenrauch, Christopher J., Gordon Dougan, Trevor Lithgow, and Eva Heinz. "Constraints on lateral gene transfer in promoting fimbrial usher protein diversity and function." Open Biology 7, no. 11 (November 2017): 170144. http://dx.doi.org/10.1098/rsob.170144.
Повний текст джерелаZhu, Lu, H. Ronald Kaback, and Ross E. Dalbey. "YidC Protein, a Molecular Chaperone for LacY Protein Folding via the SecYEG Protein Machinery." Journal of Biological Chemistry 288, no. 39 (August 8, 2013): 28180–94. http://dx.doi.org/10.1074/jbc.m113.491613.
Повний текст джерелаShen, Gang, and Brian S. J. Blagg. "Radester, a Novel Inhibitor of the Hsp90 Protein Folding Machinery." Organic Letters 7, no. 11 (May 2005): 2157–60. http://dx.doi.org/10.1021/ol050580a.
Повний текст джерелаHamazaki, Jun, and Shigeo Murata. "ER-Resident Transcription Factor Nrf1 Regulates Proteasome Expression and Beyond." International Journal of Molecular Sciences 21, no. 10 (May 23, 2020): 3683. http://dx.doi.org/10.3390/ijms21103683.
Повний текст джерелаPety de Thozée, Cédric, and Michel Ghislain. "ER-Associated Degradation of Membrane Proteins in Yeast." Scientific World JOURNAL 6 (2006): 967–83. http://dx.doi.org/10.1100/tsw.2006.191.
Повний текст джерелаYoo, Yoon Seon, Hye Gyeong Han, and Young Joo Jeon. "Unfolded Protein Response of the Endoplasmic Reticulum in Tumor Progression and Immunogenicity." Oxidative Medicine and Cellular Longevity 2017 (December 21, 2017): 1–18. http://dx.doi.org/10.1155/2017/2969271.
Повний текст джерелаLatorre, Victor, Florian Mattenberger, and Ron Geller. "Chaperoning the Mononegavirales: Current Knowledge and Future Directions." Viruses 10, no. 12 (December 8, 2018): 699. http://dx.doi.org/10.3390/v10120699.
Повний текст джерелаVoss-Andreae, Julian. "Protein Sculptures: Life's Building Blocks Inspire Art." Leonardo 38, no. 1 (February 2005): 41–45. http://dx.doi.org/10.1162/leon.2005.38.1.41.
Повний текст джерелаLiu, Yi-Chang, Danica Galonić Fujimori, and Jonathan S. Weissman. "Htm1p–Pdi1p is a folding-sensitive mannosidase that marks N-glycoproteins for ER-associated protein degradation." Proceedings of the National Academy of Sciences 113, no. 28 (June 28, 2016): E4015—E4024. http://dx.doi.org/10.1073/pnas.1608795113.
Повний текст джерелаBöttinger, Lena, Agnieszka Gornicka, Tomasz Czerwik, Piotr Bragoszewski, Adrianna Loniewska-Lwowska, Agnes Schulze-Specking, Kaye N. Truscott, Bernard Guiard, Dusanka Milenkovic, and Agnieszka Chacinska. "In vivo evidence for cooperation of Mia40 and Erv1 in the oxidation of mitochondrial proteins." Molecular Biology of the Cell 23, no. 20 (October 15, 2012): 3957–69. http://dx.doi.org/10.1091/mbc.e12-05-0358.
Повний текст джерелаHerrmann, Johannes M., and Roman Köhl. "Catch me if you can! Oxidative protein trapping in the intermembrane space of mitochondria." Journal of Cell Biology 176, no. 5 (February 20, 2007): 559–63. http://dx.doi.org/10.1083/jcb.200611060.
Повний текст джерелаSaris, Nina, Heidi Holkeri, Rachel A. Craven, Colin J. Stirling, and Marja Makarow. "The Hsp70 Homologue Lhs1p Is Involved in a Novel Function of the Yeast Endoplasmic Reticulum, Refolding and Stabilization of Heat-denatured Protein Aggregates." Journal of Cell Biology 137, no. 4 (May 19, 1997): 813–24. http://dx.doi.org/10.1083/jcb.137.4.813.
Повний текст джерелаVelasco, Dublang, Moro, and Muga. "The Complex Phosphorylation Patterns that Regulate the Activity of Hsp70 and Its Cochaperones." International Journal of Molecular Sciences 20, no. 17 (August 23, 2019): 4122. http://dx.doi.org/10.3390/ijms20174122.
Повний текст джерелаKojer, Kerstin, Valentina Peleh, Gaetano Calabrese, Johannes M. Herrmann, and Jan Riemer. "Kinetic control by limiting glutaredoxin amounts enables thiol oxidation in the reducing mitochondrial intermembrane space." Molecular Biology of the Cell 26, no. 2 (January 15, 2015): 195–204. http://dx.doi.org/10.1091/mbc.e14-10-1422.
Повний текст джерелаRabhi, Nabil, Elisabet Salas, Philippe Froguel та Jean-Sébastien Annicotte. "Role of the Unfolded Protein Response inβCell Compensation and Failure during Diabetes". Journal of Diabetes Research 2014 (2014): 1–11. http://dx.doi.org/10.1155/2014/795171.
Повний текст джерелаRaj, Kritika, Soram Idiyasan Chanu, and Surajit Sarkar. "Protein Misfolding and Aggregation in Neurodegenerative Disorders: Focus on Chaperone-Mediated Protein Folding Machinery." International Journal of Neurology Research 1, no. 2 (2015): 72–78. http://dx.doi.org/10.17554/j.issn.2313-5611.2015.01.14.
Повний текст джерелаNaganathan, Athi N. "Molecular origins of folding rate differences in the thioredoxin family." Biochemical Journal 477, no. 6 (March 18, 2020): 1083–87. http://dx.doi.org/10.1042/bcj20190864.
Повний текст джерелаAnas, Mohammad, Ankita Shukla, Aradhya Tripathi, Varsha Kumari, Chetan Prakash, Priyabrata Nag, L. Sathish Kumar, Sandeep K. Sharma, Ravishankar Ramachandran, and Niti Kumar. "Structural–functional diversity of malaria parasite's PfHSP70-1 and PfHSP40 chaperone pair gives an edge over human orthologs in chaperone-assisted protein folding." Biochemical Journal 477, no. 18 (September 28, 2020): 3625–43. http://dx.doi.org/10.1042/bcj20200434.
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