Artículos de revistas sobre el tema "Prone proteins"
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De Baets, Greet, Joost Schymkowitz y Frederic Rousseau. "Predicting aggregation-prone sequences in proteins". Essays in Biochemistry 56 (18 de agosto de 2014): 41–52. http://dx.doi.org/10.1042/bse0560041.
Texto completoLebendiker, Mario y Tsafi Danieli. "Production of prone-to-aggregate proteins". FEBS Letters 588, n.º 2 (6 de noviembre de 2013): 236–46. http://dx.doi.org/10.1016/j.febslet.2013.10.044.
Texto completoGalves, Margarita, Ritu Rathi, Gali Prag y Avraham Ashkenazi. "Ubiquitin Signaling and Degradation of Aggregate-Prone Proteins". Trends in Biochemical Sciences 44, n.º 10 (octubre de 2019): 872–84. http://dx.doi.org/10.1016/j.tibs.2019.04.007.
Texto completoTartaglia, Gian Gaetano, Amol P. Pawar, Silvia Campioni, Christopher M. Dobson, Fabrizio Chiti y Michele Vendruscolo. "Prediction of Aggregation-Prone Regions in Structured Proteins". Journal of Molecular Biology 380, n.º 2 (julio de 2008): 425–36. http://dx.doi.org/10.1016/j.jmb.2008.05.013.
Texto completoBerger, Zdenek, Brinda Ravikumar, Fiona M. Menzies, Lourdes Garcia Oroz, Benjamin R. Underwood, Menelas N. Pangalos, Ina Schmitt et al. "Rapamycin alleviates toxicity of different aggregate-prone proteins". Human Molecular Genetics 15, n.º 3 (20 de diciembre de 2005): 433–42. http://dx.doi.org/10.1093/hmg/ddi458.
Texto completoChennamsetty, Naresh, Vladimir Voynov, Veysel Kayser, Bernhard Helk y Bernhardt L. Trout. "Prediction of Aggregation Prone Regions of Therapeutic Proteins". Journal of Physical Chemistry B 114, n.º 19 (20 de mayo de 2010): 6614–24. http://dx.doi.org/10.1021/jp911706q.
Texto completoSalomons, Florian A., Victoria Menéndez-Benito, Claudia Böttcher, Brett A. McCray, J. Paul Taylor y Nico P. Dantuma. "Selective Accumulation of Aggregation-Prone Proteasome Substrates in Response to Proteotoxic Stress". Molecular and Cellular Biology 29, n.º 7 (21 de enero de 2009): 1774–85. http://dx.doi.org/10.1128/mcb.01485-08.
Texto completoRavikumar, Brinda, Abraham Acevedo-Arozena, Sara Imarisio, Zdenek Berger, Coralie Vacher, Cahir J. O'Kane, Steve D. M. Brown y David C. Rubinsztein. "Dynein mutations impair autophagic clearance of aggregate-prone proteins". Nature Genetics 37, n.º 7 (26 de junio de 2005): 771–76. http://dx.doi.org/10.1038/ng1591.
Texto completoKnaevelsrud, Helene y Anne Simonsen. "Fighting disease by selective autophagy of aggregate-prone proteins". FEBS Letters 584, n.º 12 (20 de abril de 2010): 2635–45. http://dx.doi.org/10.1016/j.febslet.2010.04.041.
Texto completoKällquist, Linda, Markus Hansson, Ann-Maj Persson, Hans Janssen, Jero Calafat, Hans Tapper y Inge Olsson. "The tetraspanin CD63 is involved in granule targeting of neutrophil elastase". Blood 112, n.º 8 (15 de octubre de 2008): 3444–54. http://dx.doi.org/10.1182/blood-2007-10-116285.
Texto completoBitran, Amir, William M. Jacobs, Xiadi Zhai y Eugene Shakhnovich. "Cotranslational folding allows misfolding-prone proteins to circumvent deep kinetic traps". Proceedings of the National Academy of Sciences 117, n.º 3 (7 de enero de 2020): 1485–95. http://dx.doi.org/10.1073/pnas.1913207117.
Texto completoRoyster, Austin, Sheema Mir y Mohammad Ayoub Mir. "A novel approach for the purification of aggregation prone proteins". PLOS ONE 16, n.º 11 (22 de noviembre de 2021): e0260143. http://dx.doi.org/10.1371/journal.pone.0260143.
Texto completoGrosch, Hans-Wilhelm y Andrej Hasilik. "Protection of Proteolysis-Prone Recombinant Proteins in Baculovirus Expression Systems". BioTechniques 24, n.º 6 (junio de 1998): 930–34. http://dx.doi.org/10.2144/98246bm05.
Texto completoMenzies, Fiona M., Raphael Hourez, Sara Imarisio, Marcel Raspe, Oana Sadiq, Dhia Chandraratna, Cahir O'Kane et al. "Puromycin-sensitive aminopeptidase protects against aggregation-prone proteins via autophagy". Human Molecular Genetics 19, n.º 23 (9 de septiembre de 2010): 4573–86. http://dx.doi.org/10.1093/hmg/ddq385.
Texto completoRavikumar, Brinda y David C. Rubinsztein. "Can autophagy protect against neurodegeneration caused by aggregate-prone proteins?" NeuroReport 15, n.º 16 (noviembre de 2004): 2443–45. http://dx.doi.org/10.1097/00001756-200411150-00001.
Texto completoSanders, Charles R. "The Scarlet Letter: Cellular Recognition of Misfolding-Prone Membrane Proteins". Biophysical Journal 112, n.º 3 (febrero de 2017): 329a. http://dx.doi.org/10.1016/j.bpj.2016.11.1780.
Texto completoLee, Yaelim, Tong Zhou, Gian Gaetano Tartaglia, Michele Vendruscolo y Claus O. Wilke. "Translationally optimal codons associate with aggregation-prone sites in proteins". PROTEOMICS 10, n.º 23 (2 de noviembre de 2010): 4163–71. http://dx.doi.org/10.1002/pmic.201000229.
Texto completoSironi, Luigi, Elena Tremoli, Ingrid Miller, Uliano Guerrini, Anna Maria Calvio, Ivano Eberini, Manfred Gemeiner, Maria Asdente, Rodolfo Paoletti y Elisabetta Gianazza. "Acute-Phase Proteins Before Cerebral Ischemia in Stroke-Prone Rats". Stroke 32, n.º 3 (marzo de 2001): 753–60. http://dx.doi.org/10.1161/01.str.32.3.753.
Texto completoBernstein, Joel M., Paul M. Bronson y Mark E. Wilson. "Immunoglobulin G Subclass Response to Major outer Membrane Proteins of Nontypable Haemophilus Influenzae in Children with Acute Otitis Media". Otolaryngology–Head and Neck Surgery 116, n.º 3 (marzo de 1997): 363–71. http://dx.doi.org/10.1016/s0194-59989770275-4.
Texto completoZhou, Ren-Bin, Xiao-Li Lu, Chen Dong, Fiaz Ahmad, Chen-Yan Zhang y Da-Chuan Yin. "Application of protein crystallization methodologies to enhance the solubility, stability and monodispersity of proteins". CrystEngComm 20, n.º 14 (2018): 1923–27. http://dx.doi.org/10.1039/c7ce02189e.
Texto completoPoboinev, V. V., V. V. Khrustalev, T. A. Khrustaleva y A. N. Stojarov. "Structural transitions in mixed classes of proteins". Proceedings of the National Academy of Sciences of Belarus, Biological Series 64, n.º 3 (17 de agosto de 2019): 326–37. http://dx.doi.org/10.29235/1029-8940-2019-64-3-326-337.
Texto completoBock, Josephine, Nathalie Kühnle, Julia D. Knopf, Nina Landscheidt, Jin-Gu Lee, Yihong Ye y Marius K. Lemberg. "Rhomboid protease RHBDL4 promotes retrotranslocation of aggregation-prone proteins for degradation". Cell Reports 40, n.º 6 (agosto de 2022): 111175. http://dx.doi.org/10.1016/j.celrep.2022.111175.
Texto completoBranco dos Santos, J., G. Staniforth, C. Breda, F. Herrera, T. Outeiro, M. Tuite y F. Giorgini. "B07 Aggregation-prone Proteins Exacerbate Huntingtin Toxicity In Yeast And Drosophila". Journal of Neurology, Neurosurgery & Psychiatry 85, Suppl 1 (1 de septiembre de 2014): A11. http://dx.doi.org/10.1136/jnnp-2014-309032.35.
Texto completoMittag, Tanja y Melissa R. Marzahn. "Short Aggregation-Prone Peptide Detectives: Finding Proteins and Truths about Aggregation". Journal of Molecular Biology 427, n.º 2 (enero de 2015): 221–24. http://dx.doi.org/10.1016/j.jmb.2014.10.017.
Texto completoLee, Minjung y Jaekyoon Shin. "Triage of oxidation-prone proteins by Sqstm1/p62 within the mitochondria". Biochemical and Biophysical Research Communications 413, n.º 1 (septiembre de 2011): 122–27. http://dx.doi.org/10.1016/j.bbrc.2011.08.067.
Texto completoFang, Yaping y Jianwen Fang. "Discrimination of soluble and aggregation-prone proteins based on sequence information". Molecular BioSystems 9, n.º 4 (2013): 806. http://dx.doi.org/10.1039/c3mb70033j.
Texto completoKarabiyik, Cansu, Min Jae Lee y David C. Rubinsztein. "Autophagy impairment in Parkinson’s disease". Essays in Biochemistry 61, n.º 6 (12 de diciembre de 2017): 711–20. http://dx.doi.org/10.1042/ebc20170023.
Texto completoHan, K. Y., J. A. Song, K. Y. Ahn, J. S. Park, H. S. Seo y J. Lee. "Solubilization of aggregation-prone heterologous proteins by covalent fusion of stress-responsive Escherichia coli protein, SlyD". Protein Engineering Design and Selection 20, n.º 11 (30 de octubre de 2007): 543–49. http://dx.doi.org/10.1093/protein/gzm055.
Texto completoAuth, Mariann, Tünde Nyikó, Andor Auber y Dániel Silhavy. "The role of RST1 and RIPR proteins in plant RNA quality control systems". Plant Molecular Biology 106, n.º 3 (17 de abril de 2021): 271–84. http://dx.doi.org/10.1007/s11103-021-01145-9.
Texto completoCiryam, Prajwal, Isabella A. Lambert-Smith, Daniel M. Bean, Rosie Freer, Fernando Cid, Gian Gaetano Tartaglia, Darren N. Saunders et al. "Spinal motor neuron protein supersaturation patterns are associated with inclusion body formation in ALS". Proceedings of the National Academy of Sciences 114, n.º 20 (10 de abril de 2017): E3935—E3943. http://dx.doi.org/10.1073/pnas.1613854114.
Texto completoDas Roy, Rishi, Manju Bhardwaj, Vasudha Bhatnagar, Kausik Chakraborty y Debasis Dash. "How do eubacterial organisms manage aggregation-prone proteome?" F1000Research 3 (27 de junio de 2014): 137. http://dx.doi.org/10.12688/f1000research.4307.1.
Texto completoNichols, Michael R. "Disentangling aggregation‐prone proteins: a new method for isolating α‐synuclein species". Journal of Neurochemistry 153, n.º 1 (10 de febrero de 2020): 7–9. http://dx.doi.org/10.1111/jnc.14973.
Texto completoCarvalho, Sofia B., Hugo M. Botelho, Sónia S. Leal, Isabel Cardoso, Günter Fritz y Cláudio M. Gomes. "Intrinsically Disordered and Aggregation Prone Regions Underlie β-Aggregation in S100 Proteins". PLoS ONE 8, n.º 10 (1 de octubre de 2013): e76629. http://dx.doi.org/10.1371/journal.pone.0076629.
Texto completoUchio, Naohiro, Yoko Oma, Kazuya Toriumi, Noboru Sasagawa, Isei Tanida, Eriko Fujita, Yoriko Kouroku, Reiko Kuroda, Takashi Momoi y Shoichi Ishiura. "Endoplasmic reticulum stress caused by aggregate-prone proteins containing homopolymeric amino acids". FEBS Journal 274, n.º 21 (8 de octubre de 2007): 5619–27. http://dx.doi.org/10.1111/j.1742-4658.2007.06085.x.
Texto completoLok, Chun-Nam, Lai-King Sy, Fuli Liu y Chi-Ming Che. "Activation of Autophagy of Aggregation-prone Ubiquitinated Proteins by Timosaponin A-III". Journal of Biological Chemistry 286, n.º 36 (8 de julio de 2011): 31684–96. http://dx.doi.org/10.1074/jbc.m110.202531.
Texto completoKang, S. H., D. M. Kim, H. J. Kim, S. Y. Jun, K. Y. Lee y H. J. Kim. "Cell-Free Production of Aggregation-Prone Proteins in Soluble and Active Forms". Biotechnology Progress 21, n.º 5 (7 de octubre de 2005): 1412–19. http://dx.doi.org/10.1021/bp050087y.
Texto completoMelnik, Andre, Valentina Cappelletti, Federico Vaggi, Ilaria Piazza, Marco Tognetti, Carmen Schwarz, Gea Cereghetti et al. "Comparative analysis of the intracellular responses to disease-related aggregation-prone proteins". Journal of Proteomics 225 (agosto de 2020): 103862. http://dx.doi.org/10.1016/j.jprot.2020.103862.
Texto completoRavikumar, B. "Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy". Human Molecular Genetics 11, n.º 9 (1 de mayo de 2002): 1107–17. http://dx.doi.org/10.1093/hmg/11.9.1107.
Texto completoMurakumo, Yoshiki, Yukiko Ogura, Hideshi Ishii, Shin-ichiro Numata, Masatoshi Ichihara, Carlo M. Croce, Richard Fishel y Masahide Takahashi. "Interactions in the Error-prone Postreplication Repair Proteins hREV1, hREV3, and hREV7". Journal of Biological Chemistry 276, n.º 38 (2 de agosto de 2001): 35644–51. http://dx.doi.org/10.1074/jbc.m102051200.
Texto completoYacoubian, Talene A. y David G. Standaert. "Reaping what you sow: Cross-seeding between aggregation-prone proteins in neurodegeneration". Movement Disorders 29, n.º 3 (2 de enero de 2014): 306. http://dx.doi.org/10.1002/mds.25766.
Texto completoHiguchi, Kae, Takashi Yabuki, Masahiro Ito y Takanori Kigawa. "Cold shock proteins improve E. coli cell‐free synthesis in terms of soluble yields of aggregation‐prone proteins". Biotechnology and Bioengineering 117, n.º 6 (26 de marzo de 2020): 1628–39. http://dx.doi.org/10.1002/bit.27326.
Texto completoKleppe, April Snofrid y Erich Bornberg-Bauer. "Robustness by intrinsically disordered C-termini and translational readthrough". Nucleic Acids Research 46, n.º 19 (22 de septiembre de 2018): 10184–94. http://dx.doi.org/10.1093/nar/gky778.
Texto completoOnwezen, Marleen C., Muriel C. D. Verain y Hans Dagevos. "Social Norms Support the Protein Transition: The Relevance of Social Norms to Explain Increased Acceptance of Alternative Protein Burgers over 5 Years". Foods 11, n.º 21 (28 de octubre de 2022): 3413. http://dx.doi.org/10.3390/foods11213413.
Texto completoDavis, John N. y Anthony N. van den Pol. "Viral Mutagenesis as a Means for Generating Novel Proteins". Journal of Virology 84, n.º 3 (11 de noviembre de 2009): 1625–30. http://dx.doi.org/10.1128/jvi.01747-09.
Texto completoSánchez-Pérez, Ana María, Berta Claramonte-Clausell, Juan Vicente Sánchez-Andrés y María Trinidad Herrero. "Parkinson’s Disease and Autophagy". Parkinson's Disease 2012 (2012): 1–6. http://dx.doi.org/10.1155/2012/429524.
Texto completoKaur, Ravinder, Janet R. Casey y Michael E. Pichichero. "Serum Antibody Response to Five Streptococcus pneumoniae Proteins During Acute Otitis Media in Otitis-prone and Non–otitis-prone Children". Pediatric Infectious Disease Journal 30, n.º 8 (agosto de 2011): 645–50. http://dx.doi.org/10.1097/inf.0b013e31821c2d8b.
Texto completoMetskas, Lauren Ann y Elizabeth Rhoades. "Single-Molecule FRET of Intrinsically Disordered Proteins". Annual Review of Physical Chemistry 71, n.º 1 (20 de abril de 2020): 391–414. http://dx.doi.org/10.1146/annurev-physchem-012420-104917.
Texto completoSun, Xiaolin, William T. Jones y Erik H. A. Rikkerink. "GRAS proteins: the versatile roles of intrinsically disordered proteins in plant signalling". Biochemical Journal 442, n.º 1 (27 de enero de 2012): 1–12. http://dx.doi.org/10.1042/bj20111766.
Texto completoMonti, Paola, Vaclav Brazda, Natália Bohálová, Otília Porubiaková, Paola Menichini, Andrea Speciale, Renata Bocciardi, Alberto Inga y Gilberto Fronza. "Evaluating the Influence of a G-Quadruplex Prone Sequence on the Transactivation Potential by Wild-Type and/or Mutant P53 Family Proteins through a Yeast-Based Functional Assay". Genes 12, n.º 2 (15 de febrero de 2021): 277. http://dx.doi.org/10.3390/genes12020277.
Texto completoDumas, Louis, Francesca Zito, Pascaline Auroy, Xenie Johnson, Gilles Peltier y Jean Alric. "Structure-Function Analysis of Chloroplast Proteins via Random Mutagenesis Using Error-Prone PCR". Plant Physiology 177, n.º 2 (27 de abril de 2018): 465–75. http://dx.doi.org/10.1104/pp.17.01618.
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