Artículos de revistas sobre el tema "Protein folding machinery"
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Chiu, Wah. "Center for protein folding machinery". Nanomedicine: Nanotechnology, Biology and Medicine 2, n.º 4 (diciembre de 2006): 289. http://dx.doi.org/10.1016/j.nano.2006.10.069.
Texto completoZhang, Xiaodong, Fabienne Beuron y Paul S. Freemont. "Machinery of protein folding and unfolding". Current Opinion in Structural Biology 12, n.º 2 (abril de 2002): 231–38. http://dx.doi.org/10.1016/s0959-440x(02)00315-9.
Texto completoBuchner, J. "Introduction: the cellular protein folding machinery". Cellular and Molecular Life Sciences 59, n.º 10 (octubre de 2002): 1587–88. http://dx.doi.org/10.1007/pl00012484.
Texto completoFink, Anthony L. "Chaperone-Mediated Protein Folding". Physiological Reviews 79, n.º 2 (1 de abril de 1999): 425–49. http://dx.doi.org/10.1152/physrev.1999.79.2.425.
Texto completoRassow, J., K. Mohrs, S. Koidl, I. B. Barthelmess, N. Pfanner y M. Tropschug. "Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60." Molecular and Cellular Biology 15, n.º 5 (mayo de 1995): 2654–62. http://dx.doi.org/10.1128/mcb.15.5.2654.
Texto completoHartl, F. Ulrich. "Unfolding the chaperone story". Molecular Biology of the Cell 28, n.º 22 (noviembre de 2017): 2919–23. http://dx.doi.org/10.1091/mbc.e17-07-0480.
Texto completoSorokina, Irina, Arcady R. Mushegian y Eugene V. Koonin. "Is Protein Folding a Thermodynamically Unfavorable, Active, Energy-Dependent Process?" International Journal of Molecular Sciences 23, n.º 1 (4 de enero de 2022): 521. http://dx.doi.org/10.3390/ijms23010521.
Texto completoChoudhury, P., Y. Liu y RN Sifers. "Quality Control of Protein Folding: Participation in Human Disease". Physiology 12, n.º 4 (1 de agosto de 1997): 162–66. http://dx.doi.org/10.1152/physiologyonline.1997.12.4.162.
Texto completoPedone, Emilia, Danila Limauro y Simonetta Bartolucci. "The Machinery for Oxidative Protein Folding in Thermophiles". Antioxidants & Redox Signaling 10, n.º 1 (enero de 2008): 157–70. http://dx.doi.org/10.1089/ars.2007.1855.
Texto completoAller, Isabel y Andreas J. Meyer. "The oxidative protein folding machinery in plant cells". Protoplasma 250, n.º 4 (23 de octubre de 2012): 799–816. http://dx.doi.org/10.1007/s00709-012-0463-x.
Texto completoSantos, João D., Sara Canato, Ana S. Carvalho, Hugo M. Botelho, Kerman Aloria, Margarida D. Amaral, Rune Matthiesen, Andre O. Falcao y Carlos M. Farinha. "Folding Status Is Determinant over Traffic-Competence in Defining CFTR Interactors in the Endoplasmic Reticulum". Cells 8, n.º 4 (14 de abril de 2019): 353. http://dx.doi.org/10.3390/cells8040353.
Texto completoAlonzi, Dominic S., Kathryn A. Scott, Raymond A. Dwek y Nicole Zitzmann. "Iminosugar antivirals: the therapeutic sweet spot". Biochemical Society Transactions 45, n.º 2 (13 de abril de 2017): 571–82. http://dx.doi.org/10.1042/bst20160182.
Texto completoKang, Ji An y 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, n.º 4 (19 de febrero de 2021): 2078. http://dx.doi.org/10.3390/ijms22042078.
Texto completoMak, Wai Shun, Tsz Ming Tsang, Tsz Yin Chan y 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, n.º 4 (2 de octubre de 2021): 40. http://dx.doi.org/10.3390/proteomes9040040.
Texto completoChristian Wigley, W., Rosalind P. Fabunmi, Min Goo Lee, Christopher R. Marino, Shmuel Muallem, George N. DeMartino y Philip J. Thomas. "Dynamic Association of Proteasomal Machinery with the Centrosome". Journal of Cell Biology 145, n.º 3 (3 de mayo de 1999): 481–90. http://dx.doi.org/10.1083/jcb.145.3.481.
Texto completoMeimaridou, Eirini, Sakina B. Gooljar y J. Paul Chapple. "From hatching to dispatching: the multiple cellular roles of the Hsp70 molecular chaperone machinery". Journal of Molecular Endocrinology 42, n.º 1 (13 de octubre de 2008): 1–9. http://dx.doi.org/10.1677/jme-08-0116.
Texto completoRoy, Joydeep, Sahana Mitra, Kaushik Sengupta y Atin K. Mandal. "Hsp70 clears misfolded kinases that partitioned into distinct quality-control compartments". Molecular Biology of the Cell 26, n.º 9 (mayo de 2015): 1583–600. http://dx.doi.org/10.1091/mbc.e14-08-1262.
Texto completoHadden, M. Kyle, Lakshmi Galam, Jason E. Gestwicki, Robert L. Matts y Brian S. J. Blagg. "Derrubone, an Inhibitor of the Hsp90 Protein Folding Machinery". Journal of Natural Products 70, n.º 12 (diciembre de 2007): 2014–18. http://dx.doi.org/10.1021/np070190s.
Texto completoBrownrigg, George P., James Johnson y Elizabeth J. Rideout. "80 - Sex Differences in β-Cell Protein Folding Machinery". Canadian Journal of Diabetes 44, n.º 7 (octubre de 2020): S32. http://dx.doi.org/10.1016/j.jcjd.2020.08.086.
Texto completoChambers, Joseph E. y 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, n.º 8 (15 de octubre de 2014): C657—C670. http://dx.doi.org/10.1152/ajpcell.00183.2014.
Texto completoZhao, Rongmin y Walid A. Houry. "Hsp90: a chaperone for protein folding and gene regulation". Biochemistry and Cell Biology 83, n.º 6 (1 de diciembre de 2005): 703–10. http://dx.doi.org/10.1139/o05-158.
Texto completoParray, Zahoor Ahmad, Mohammad Shahid y Asimul Islam. "Insights into Fluctuations of Structure of Proteins: Significance of Intermediary States in Regulating Biological Functions". Polymers 14, n.º 8 (11 de abril de 2022): 1539. http://dx.doi.org/10.3390/polym14081539.
Texto completoGandhi, Jason, Anthony C. Antonelli, Adil Afridi, Sohrab Vatsia, Gunjan Joshi, Victor Romanov, Ian V. J. Murray y 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, n.º 4 (27 de mayo de 2019): 339–58. http://dx.doi.org/10.1515/revneuro-2016-0035.
Texto completoScheuner, Donalyn y Randal J. Kaufman. "The Unfolded Protein Response: A Pathway That Links Insulin Demand with β-Cell Failure and Diabetes". Endocrine Reviews 29, n.º 3 (24 de abril de 2008): 317–33. http://dx.doi.org/10.1210/er.2007-0039.
Texto completoZhang, Yongli y Frederick M. Hughson. "Chaperoning SNARE Folding and Assembly". Annual Review of Biochemistry 90, n.º 1 (20 de junio de 2021): 581–603. http://dx.doi.org/10.1146/annurev-biochem-081820-103615.
Texto completoLim, Shion A., Kathryn M. Hart, Michael J. Harms y Susan Marqusee. "Evolutionary trend toward kinetic stability in the folding trajectory of RNases H". Proceedings of the National Academy of Sciences 113, n.º 46 (31 de octubre de 2016): 13045–50. http://dx.doi.org/10.1073/pnas.1611781113.
Texto completoShepherd, Colin, Ojore B. V. Oka y Neil J. Bulleid. "Inactivation of mammalian Ero1α is catalysed by specific protein disulfide-isomerases". Biochemical Journal 461, n.º 1 (13 de junio de 2014): 107–13. http://dx.doi.org/10.1042/bj20140234.
Texto completoBenham, Adam M., Marcel van Lith, Roberto Sitia y 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, n.º 1617 (5 de mayo de 2013): 20110403. http://dx.doi.org/10.1098/rstb.2011.0403.
Texto completoBerner, Nicole, Karl-Richard Reutter y 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, n.º 1 (20 de junio de 2018): 751–82. http://dx.doi.org/10.1146/annurev-biochem-062917-012749.
Texto completoSchlebach, Jonathan P. y Charles R. Sanders. "The safety dance: biophysics of membrane protein folding and misfolding in a cellular context". Quarterly Reviews of Biophysics 48, n.º 1 (25 de noviembre de 2014): 1–34. http://dx.doi.org/10.1017/s0033583514000110.
Texto completoHood, David A. y Anna-Maria Joseph. "Mitochondrial assembly: protein import". Proceedings of the Nutrition Society 63, n.º 2 (mayo de 2004): 293–300. http://dx.doi.org/10.1079/pns2004342.
Texto completoDaverkausen-Fischer, Lea, Margarethe Draga y Felicitas Pröls. "Regulation of Translation, Translocation, and Degradation of Proteins at the Membrane of the Endoplasmic Reticulum". International Journal of Molecular Sciences 23, n.º 10 (17 de mayo de 2022): 5576. http://dx.doi.org/10.3390/ijms23105576.
Texto completoStubenrauch, Christopher J., Gordon Dougan, Trevor Lithgow y Eva Heinz. "Constraints on lateral gene transfer in promoting fimbrial usher protein diversity and function". Open Biology 7, n.º 11 (noviembre de 2017): 170144. http://dx.doi.org/10.1098/rsob.170144.
Texto completoZhu, Lu, H. Ronald Kaback y Ross E. Dalbey. "YidC Protein, a Molecular Chaperone for LacY Protein Folding via the SecYEG Protein Machinery". Journal of Biological Chemistry 288, n.º 39 (8 de agosto de 2013): 28180–94. http://dx.doi.org/10.1074/jbc.m113.491613.
Texto completoShen, Gang y Brian S. J. Blagg. "Radester, a Novel Inhibitor of the Hsp90 Protein Folding Machinery". Organic Letters 7, n.º 11 (mayo de 2005): 2157–60. http://dx.doi.org/10.1021/ol050580a.
Texto completoHamazaki, Jun y Shigeo Murata. "ER-Resident Transcription Factor Nrf1 Regulates Proteasome Expression and Beyond". International Journal of Molecular Sciences 21, n.º 10 (23 de mayo de 2020): 3683. http://dx.doi.org/10.3390/ijms21103683.
Texto completoPety de Thozée, Cédric y 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.
Texto completoYoo, Yoon Seon, Hye Gyeong Han y Young Joo Jeon. "Unfolded Protein Response of the Endoplasmic Reticulum in Tumor Progression and Immunogenicity". Oxidative Medicine and Cellular Longevity 2017 (21 de diciembre de 2017): 1–18. http://dx.doi.org/10.1155/2017/2969271.
Texto completoLatorre, Victor, Florian Mattenberger y Ron Geller. "Chaperoning the Mononegavirales: Current Knowledge and Future Directions". Viruses 10, n.º 12 (8 de diciembre de 2018): 699. http://dx.doi.org/10.3390/v10120699.
Texto completoVoss-Andreae, Julian. "Protein Sculptures: Life's Building Blocks Inspire Art". Leonardo 38, n.º 1 (febrero de 2005): 41–45. http://dx.doi.org/10.1162/leon.2005.38.1.41.
Texto completoLiu, Yi-Chang, Danica Galonić Fujimori y 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, n.º 28 (28 de junio de 2016): E4015—E4024. http://dx.doi.org/10.1073/pnas.1608795113.
Texto completoBöttinger, Lena, Agnieszka Gornicka, Tomasz Czerwik, Piotr Bragoszewski, Adrianna Loniewska-Lwowska, Agnes Schulze-Specking, Kaye N. Truscott, Bernard Guiard, Dusanka Milenkovic y Agnieszka Chacinska. "In vivo evidence for cooperation of Mia40 and Erv1 in the oxidation of mitochondrial proteins". Molecular Biology of the Cell 23, n.º 20 (15 de octubre de 2012): 3957–69. http://dx.doi.org/10.1091/mbc.e12-05-0358.
Texto completoHerrmann, Johannes M. y Roman Köhl. "Catch me if you can! Oxidative protein trapping in the intermembrane space of mitochondria". Journal of Cell Biology 176, n.º 5 (20 de febrero de 2007): 559–63. http://dx.doi.org/10.1083/jcb.200611060.
Texto completoSaris, Nina, Heidi Holkeri, Rachel A. Craven, Colin J. Stirling y 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, n.º 4 (19 de mayo de 1997): 813–24. http://dx.doi.org/10.1083/jcb.137.4.813.
Texto completoVelasco, Dublang, Moro y Muga. "The Complex Phosphorylation Patterns that Regulate the Activity of Hsp70 and Its Cochaperones". International Journal of Molecular Sciences 20, n.º 17 (23 de agosto de 2019): 4122. http://dx.doi.org/10.3390/ijms20174122.
Texto completoKojer, Kerstin, Valentina Peleh, Gaetano Calabrese, Johannes M. Herrmann y Jan Riemer. "Kinetic control by limiting glutaredoxin amounts enables thiol oxidation in the reducing mitochondrial intermembrane space". Molecular Biology of the Cell 26, n.º 2 (15 de enero de 2015): 195–204. http://dx.doi.org/10.1091/mbc.e14-10-1422.
Texto completoRabhi, Nabil, Elisabet Salas, Philippe Froguel y 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.
Texto completoRaj, Kritika, Soram Idiyasan Chanu y Surajit Sarkar. "Protein Misfolding and Aggregation in Neurodegenerative Disorders: Focus on Chaperone-Mediated Protein Folding Machinery". International Journal of Neurology Research 1, n.º 2 (2015): 72–78. http://dx.doi.org/10.17554/j.issn.2313-5611.2015.01.14.
Texto completoNaganathan, Athi N. "Molecular origins of folding rate differences in the thioredoxin family". Biochemical Journal 477, n.º 6 (18 de marzo de 2020): 1083–87. http://dx.doi.org/10.1042/bcj20190864.
Texto completoAnas, Mohammad, Ankita Shukla, Aradhya Tripathi, Varsha Kumari, Chetan Prakash, Priyabrata Nag, L. Sathish Kumar, Sandeep K. Sharma, Ravishankar Ramachandran y 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, n.º 18 (28 de septiembre de 2020): 3625–43. http://dx.doi.org/10.1042/bcj20200434.
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