Relevant bibliographies by topics / Protein folding machinery

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'Protein folding machinery'

Author: Grafiati
Published: 6 September 2023
Last updated: 31 July 2025

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Journal articles on the topic "Protein folding machinery"

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Chiu, Wah. "Center for protein folding machinery." Nanomedicine: Nanotechnology, Biology and Medicine 2, no. 4 (2006): 289. http://dx.doi.org/10.1016/j.nano.2006.10.069.

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Zhang, Xiaodong, Fabienne Beuron, and Paul S. Freemont. "Machinery of protein folding and unfolding." Current Opinion in Structural Biology 12, no. 2 (2002): 231–38. http://dx.doi.org/10.1016/s0959-440x(02)00315-9.

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Buchner, J. "Introduction: the cellular protein folding machinery." Cellular and Molecular Life Sciences 59, no. 10 (2002): 1587–88. http://dx.doi.org/10.1007/pl00012484.

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Fink, Anthony L. "Chaperone-Mediated Protein Folding." Physiological Reviews 79, no. 2 (1999): 425–49. http://dx.doi.org/10.1152/physrev.1999.79.2.425.

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The folding of most newly synthesized proteins in the cell requires the interaction of a variety of protein cofactors known as molecular chaperones. These molecules recognize and bind to nascent polypeptide chains and partially folded intermediates of proteins, preventing their aggregation and misfolding. There are several families of chaperones; those most involved in protein folding are the 40-kDa heat shock protein (HSP40; DnaJ), 60-kDa heat shock protein (HSP60; GroEL), and 70-kDa heat shock protein (HSP70; DnaK) families. The availability of high-resolution structures has facilitated a mo
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Rassow, 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 (1995): 2654–62. http://dx.doi.org/10.1128/mcb.15.5.2654.

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We studied the role of mitochondrial cyclophilin 20 (CyP20), a peptidyl-prolyl cis-trans isomerase, in preprotein translocation across the mitochondrial membranes and protein folding inside the organelle. The inhibitory drug cyclosporin A did not impair membrane translocation of preproteins, but it delayed the folding of an imported protein in wild-type mitochondria. Similarly, Neurospora crassa mitochondria lacking CyP20 efficiently imported preproteins into the matrix, but folding of an imported protein was significantly delayed, indicating that CyP20 is involved in protein folding in the ma
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Melikov, Aleksandr, and Petr Novák. "Heat Shock Protein Network: the Mode of Action, the Role in Protein Folding and Human Pathologies." Folia Biologica 70, no. 3 (2024): 152–65. https://doi.org/10.14712/fb2024070030152.

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Protein folding is an extremely complicated process, which has been extensively tackled during the last decades. In vivo, a certain molecular machinery is responsible for assisting the correct folding of proteins and maintaining protein homeostasis: the members of this machinery are the heat shock proteins (HSPs), which belong among molecular chaperones. Mutations in HSPs are associated with several inherited diseases, and members of this group were also proved to be involved in neurodegenerative pathologies (e.g., Alzheimer and Parkinson diseases), cancer, viral infections, and antibiotic res
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Hartl, F. Ulrich. "Unfolding the chaperone story." Molecular Biology of the Cell 28, no. 22 (2017): 2919–23. http://dx.doi.org/10.1091/mbc.e17-07-0480.

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Protein folding in the cell was originally assumed to be a spontaneous process, based on Anfinsen’s discovery that purified proteins can fold on their own after removal from denaturant. Consequently cell biologists showed little interest in the protein folding process. This changed only in the mid and late 1980s, when the chaperone story began to unfold. As a result, we now know that in vivo, protein folding requires assistance by a complex machinery of molecular chaperones. To ensure efficient folding, members of different chaperone classes receive the nascent protein chain emerging from the
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Pedone, Emilia, Danila Limauro, and Simonetta Bartolucci. "The Machinery for Oxidative Protein Folding in Thermophiles." Antioxidants & Redox Signaling 10, no. 1 (2008): 157–70. http://dx.doi.org/10.1089/ars.2007.1855.

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Aller, Isabel, and Andreas J. Meyer. "The oxidative protein folding machinery in plant cells." Protoplasma 250, no. 4 (2012): 799–816. http://dx.doi.org/10.1007/s00709-012-0463-x.

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Sorokina, 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 (2022): 521. http://dx.doi.org/10.3390/ijms23010521.

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The prevailing current view of protein folding is the thermodynamic hypothesis, under which the native folded conformation of a protein corresponds to the global minimum of Gibbs free energy G. We question this concept and show that the empirical evidence behind the thermodynamic hypothesis of folding is far from strong. Furthermore, physical theory-based approaches to the prediction of protein folds and their folding pathways so far have invariably failed except for some very small proteins, despite decades of intensive theory development and the enormous increase of computer power. The recen
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Dissertations / Theses on the topic "Protein folding machinery"

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Talmon, Esther [Verfasser]. "The periplasmic domain of the barrel assembly machinery protein A (BamA) from Escherichia coli assists folding of outer membrane protein A / Esther Talmon." Kassel : Universitätsbibliothek Kassel, 2016. http://d-nb.info/1124028420/34.

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Alnahi, Haitham G. "A machine induction approach to the protein folding problem." Thesis, Brunel University, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.326864.

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Ashok, Anupama 1985. "TANGO1 asembles a machine for collagen folding and export." Doctoral thesis, Universitat Pompeu Fabra, 2019. http://hdl.handle.net/10803/666036.

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COPII vesicles of 60-90nm diameter are known to export secretory cargoes from endoplasmic reticulum (ER). However, they cannot be employed to export bulky cargoes like the collagens that can reach up to 400 nm in length. Collagens, the most abundant secretory proteins, make up 25% of our dry body weight and required for building extracellular matrix, and to produce mineralized bones. The discovery TANGO1 has made the process of collagen export at the ER amenable to molecular analysis. I set out to identify its interactors through a proximity biotinylation coupled with mass spectrometry approac
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Ishikawa, Yoshihiro. "A molecular chaperone complex as a protein folding machine involved in collagen biosynthesis." 京都大学 (Kyoto University), 2010. http://hdl.handle.net/2433/120704.

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Mauricio-Sanchez, David, Andrade Lopes Alneu de, and higuihara Juarez Pedro Nelson. "Approaches based on tree-structures classifiers to protein fold prediction." Institute of Electrical and Electronics Engineers Inc, 2017. http://hdl.handle.net/10757/622536.

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El texto completo de este trabajo no está disponible en el Repositorio Académico UPC por restricciones de la casa editorial donde ha sido publicado.<br>Protein fold recognition is an important task in the biological area. Different machine learning methods such as multiclass classifiers, one-vs-all and ensemble nested dichotomies were applied to this task and, in most of the cases, multiclass approaches were used. In this paper, we compare classifiers organized in tree structures to classify folds. We used a benchmark dataset containing 125 features to predict folds, comparing different superv
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NEGRI, MATTEO. "Is Evolution an Algorithm? Effects of local entropy in unsupervised learning and protein evolution." Doctoral thesis, Politecnico di Torino, 2022. http://hdl.handle.net/11583/2972307.

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Guan, Wei. "New support vector machine formulations and algorithms with application to biomedical data analysis." Diss., Georgia Institute of Technology, 2011. http://hdl.handle.net/1853/41126.

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The Support Vector Machine (SVM) classifier seeks to find the separating hyperplane wx=r that maximizes the margin distance 1/||w||2^2. It can be formalized as an optimization problem that minimizes the hinge loss Ʃ[subscript i](1-y[subscript i] f(x[subscript i]))₊ plus the L₂-norm of the weight vector. SVM is now a mainstay method of machine learning. The goal of this dissertation work is to solve different biomedical data analysis problems efficiently using extensions of SVM, in which we augment the standard SVM formulation based on the application requirements. The biomedical applications
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"Investtigating the stability of protein folding machinery GroEl." Thesis, 2018. http://localhost:8080/xmlui/handle/12345678/7724.

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Goswami, Arvind Vittal. "Role of Grp 75 Chaperone Folding Machinery in the Maintenance of Mitochondrial Protien Quality Control." Thesis, 2013. http://etd.iisc.ac.in/handle/2005/3333.

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My research focuses on understanding the importance of human mitochondrial Hsp70 (Grp75) chaperone machinery for the maintenance of protein quality control inside the mitochondrial matrix. The investigations carried out during this study have been addressed towards gaining better insights into the working of Grp75 chaperone folding machinery in association with its diverse set of co-chaperones residing in human mitochondria. Additionally, the research also focuses on explaining the various modes of Grp75 participation leading to multiple disease conditions. The thesis has been divided into the
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Goswami, Arvind Vittal. "Role of Grp 75 Chaperone Folding Machinery in the Maintenance of Mitochondrial Protien Quality Control." Thesis, 2013. http://etd.iisc.ernet.in/2005/3333.

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My research focuses on understanding the importance of human mitochondrial Hsp70 (Grp75) chaperone machinery for the maintenance of protein quality control inside the mitochondrial matrix. The investigations carried out during this study have been addressed towards gaining better insights into the working of Grp75 chaperone folding machinery in association with its diverse set of co-chaperones residing in human mitochondria. Additionally, the research also focuses on explaining the various modes of Grp75 participation leading to multiple disease conditions. The thesis has been divided into the
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Books on the topic "Protein folding machinery"

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Nakamura, Tomohiro, and Stuart A. Lipton. Neurodegenerative Diseases as Protein Misfolding Disorders. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190233563.003.0002.

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Neurodegenerative diseases (NDDs) often represent disorders of protein folding. Rather than large aggregates, recent evidence suggests that soluble oligomers of misfolded proteins are the most neurotoxic species. Emerging evidence points to small, soluble oligomers of misfolded proteins as the cause of synaptic dysfunction and loss, the major pathological correlate to disease progression in many NDDs including Alzheimer’s disease. The protein quality control machinery of the cell, which includes molecular chaperones as found in the endoplasmic reticulum (ER), the ubiquitin-proteasome system (U
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Structure and Action of Molecular Chaperones: Machines That Assist Protein Folding in the Cell. World Scientific Publishing Co Pte Ltd, 2016.

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Book chapters on the topic "Protein folding machinery"

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Hartman, D., and M. J. Gething. "Normal protein folding machinery." In Stress-Inducible Cellular Responses. Birkhäuser Basel, 1996. http://dx.doi.org/10.1007/978-3-0348-9088-5_2.

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Jena, Bhanu P. "Chaperonin: Protein Folding Machinery in Cells." In Cellular Nanomachines. Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-44496-9_3.

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Theocharopoulou, Georgia, and Panayiotis Vlamos. "Modeling the Critical Activation of Chaperone Machinery in Protein Folding." In Advances in Experimental Medicine and Biology. Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-32622-7_33.

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Pratt, William B., Yoshihiro Morishima, and Yoichi Osawa. "The Hsp90 Chaperone Machinery Acts at Protein Folding Clefts to Regulate Both Signaling Protein Function and Protein Quality Control." In Heat Shock Proteins in Cancer. Springer Netherlands, 2007. http://dx.doi.org/10.1007/978-1-4020-6401-2_1.

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Hildenbrand, Zacariah L., and Ricardo A. Bernal. "Chaperonin-Mediated Folding of Viral Proteins." In Viral Molecular Machines. Springer US, 2011. http://dx.doi.org/10.1007/978-1-4614-0980-9_13.

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Chawhan, Paridhi, and Ishita Singh. "A Hybrid Quantum Machine Learning for the Prediction of Protein Folding." In Studies in Autonomic, Data-driven and Industrial Computing. Springer Nature Singapore, 2024. http://dx.doi.org/10.1007/978-981-97-5862-3_2.

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Nanni, Luca. "Computational Inference of DNA Folding Principles: From Data Management to Machine Learning." In Special Topics in Information Technology. Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-030-85918-3_7.

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AbstractDNA is the molecular basis of life and would total about three meters if linearly untangled. To fit in the cell nucleus at the micrometer scale, DNA has, therefore, to fold itself into several layers of hierarchical structures, which are thought to be associated with functional compartmentalization of genomic features like genes and their regulatory elements. For this reason, understanding the mechanisms of genome folding is a major biological research problem. Studying chromatin conformation requires high computational resources and complex data analyses pipelines. In this chapter, we
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Singh, Lavneet, Girija Chetty, and Dharmendra Sharma. "A Hybrid Approach to Increase the Performance of Protein Folding Recognition Using Support Vector Machines." In Machine Learning and Data Mining in Pattern Recognition. Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-31537-4_51.

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Leroux, Michel R., and F. Ulrich Hartl. "Cellular functions of molecular chaperones." In Mechanisms of Protein Folding. Oxford University PressOxford, 2000. http://dx.doi.org/10.1093/oso/9780199637898.003.0014.

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Abstract Proteins are faced with the potential problems of aggregation and denaturation throughout their existence. First, they are synthesized on ribosomes as unfolded polypeptide chains that must reach their stably folded conformations, either as monomers or oligorneric species, or else be eliminated on the basis that they cannot serve useful purposes in the cell. This is no easy task, given that the aggregation-prone nascent polypeptide chain cannot fold to its native state until the complete protein (or individual protein domain) is freed from the ribosome. Secondly, the cellular environme
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Simons, J. F., and A. Helenius. "Quality control in the endoplasmic reticulum." In Guidebook to Molecular Chaperones and Protein-Folding Catalysts. Oxford University PressOxford, 1997. http://dx.doi.org/10.1093/oso/9780198599494.003.00192.

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Abstract The reasons for quality control are at least threefold. First, it makes sense to keep newly synthesized proteins in the ER until folding is completed because the ER contains a rich variety of chaperones and folding enzymes at high concentrations. The ER also has an ionic and redox milieu optimized for folding and disulfide formation. In the extracellular space, or other final compartments of residence, no folding machinery is available.
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Conference papers on the topic "Protein folding machinery"

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R., Vijay Arvind, Haribharathi S, and Brindha R. "End-to-End Optimized Pipeline for Prediction of Protein Folding Kinetics." In 2023 International Conference on Machine Learning and Applications (ICMLA). IEEE, 2023. http://dx.doi.org/10.1109/icmla58977.2023.00275.

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Dong, Siyao, Xinge Liu, Yuanlin Qiu, and Shan Li. "Protein Folding Recognition Based on Particle Swarm Optimization and Optimal Interval Distribution Machine." In 2024 36th Chinese Control and Decision Conference (CCDC). IEEE, 2024. http://dx.doi.org/10.1109/ccdc62350.2024.10588127.

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Lin, Guan Ning, Zheng Wang, Dong Xu, and Jianlin Cheng. "Sequence-Based Prediction of Protein Folding Rates Using Contacts, Secondary Structures and Support Vector Machines." In 2009 IEEE International Conference on Bioinformatics and Biomedicine (BIBM). IEEE, 2009. http://dx.doi.org/10.1109/bibm.2009.21.

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