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Journal articles on the topic 'Protein folding machinery'

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Published: 6 September 2023
Last updated: 31 July 2025

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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Santos, João D., Sara Canato, Ana S. Carvalho, et al. "Folding Status Is Determinant over Traffic-Competence in Defining CFTR Interactors in the Endoplasmic Reticulum." Cells 8, no. 4 (2019): 353. http://dx.doi.org/10.3390/cells8040353.

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The most common cystic fibrosis-causing mutation (F508del, present in ~85% of CF patients) leads to CFTR misfolding, which is recognized by the endoplasmic reticulum (ER) quality control (ERQC), resulting in ER retention and early degradation. It is known that CFTR exit from the ER is mediated by specific retention/sorting signals that include four arginine-framed tripeptide (AFT) retention motifs and a diacidic (DAD) exit code that controls the interaction with the COPII machinery. Here, we aim at obtaining a global view of the protein interactors that regulate CFTR exit from the ER. We used
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12

Alonzi, Dominic S., Kathryn A. Scott, Raymond A. Dwek, and Nicole Zitzmann. "Iminosugar antivirals: the therapeutic sweet spot." Biochemical Society Transactions 45, no. 2 (2017): 571–82. http://dx.doi.org/10.1042/bst20160182.

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Many viruses require the host endoplasmic reticulum protein-folding machinery in order to correctly fold one or more of their glycoproteins. Iminosugars with glucose stereochemistry target the glucosidases which are key for entry into the glycoprotein folding cycle. Viral glycoproteins are thus prevented from interacting with the protein-folding machinery leading to misfolding and an antiviral effect against a wide range of different viral families. As iminosugars target host enzymes, they should be refractory to mutations in the virus. Iminosugars therefore have great potential for developmen
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13

Christian Wigley, W., Rosalind P. Fabunmi, Min Goo Lee, et al. "Dynamic Association of Proteasomal Machinery with the Centrosome." Journal of Cell Biology 145, no. 3 (1999): 481–90. http://dx.doi.org/10.1083/jcb.145.3.481.

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Although the number of pathologies known to arise from the inappropriate folding of proteins continues to grow, mechanisms underlying the recognition and ultimate disposition of misfolded polypeptides remain obscure. For example, how and where such substrates are identified and processed is unknown. We report here the identification of a specific subcellular structure in which, under basal conditions, the 20S proteasome, the PA700 and PA28 (700- and 180-kD proteasome activator complexes, respectively), ubiquitin, Hsp70 and Hsp90 (70- and 90-kD heat shock protein, respectively) concentrate in H
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14

Choudhury, P., Y. Liu, and RN Sifers. "Quality Control of Protein Folding: Participation in Human Disease." Physiology 12, no. 4 (1997): 162–66. http://dx.doi.org/10.1152/physiologyonline.1997.12.4.162.

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15

Kang, 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 (2021): 2078. http://dx.doi.org/10.3390/ijms22042078.

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The endoplasmic reticulum (ER) is an interconnected organelle that plays fundamental roles in the biosynthesis, folding, stabilization, maturation, and trafficking of secretory and transmembrane proteins. It is the largest organelle and critically modulates nearly all aspects of life. Therefore, in the endoplasmic reticulum, an enormous investment of resources, including chaperones and protein folding facilitators, is dedicated to adequate protein maturation and delivery to final destinations. Unfortunately, the folding and assembly of proteins can be quite error-prone, which leads to the gene
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16

Mak, 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 (2021): 40. http://dx.doi.org/10.3390/proteomes9040040.

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This study investigates whether selected WD40 proteins with a 7-bladed β-propeller structure, similar to that of the β subunit of the G protein heterotrimer, interact with the cytosolic chaperonin CCT and its known binding partner, PhLP1. Previous studies have shown that CCT is required for the folding of the Gβ subunit and other WD40 proteins. The role of PhLP1 in the folding of Gβ has also been established, but it is unknown if PhLP1 assists in the folding of other Gβ-like proteins. The binding of three Gβ-like proteins, TBL2, MLST8 and CDC20, to CCT and PhLP1, was demonstrated in this study
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17

Meimaridou, 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 (2008): 1–9. http://dx.doi.org/10.1677/jme-08-0116.

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Molecular chaperones are best recognized for their roles in de novo protein folding and the cellular response to stress. However, many molecular chaperones, and in particular the Hsp70 chaperone machinery, have multiple diverse cellular functions. At the molecular level, chaperones are mediators of protein conformational change. To facilitate conformational change of client/substrate proteins, in manifold contexts, chaperone power must be closely regulated and harnessed to specific cellular locales – this is controlled by cochaperones. This review considers specialized functions of the Hsp70 c
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18

Roy, 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 (2015): 1583–600. http://dx.doi.org/10.1091/mbc.e14-08-1262.

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Hsp70 aids in protein folding and directs misfolded proteins to the cellular degradation machinery. We describe discrete roles of Hsp70,SSA1 as an important quality-control machinery that switches functions to ameliorate the cellular environment. SSA1 facilitates folding/maturation of newly synthesized protein kinases by aiding their phosphorylation process and also stimulates ubiquitylation and degradation of kinases in regular protein turnover or during stress when kinases are denatured or improperly folded. Significantly, while kinases accumulate as insoluble inclusions upon SSA1 inhibition
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19

Hadden, 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 (2007): 2014–18. http://dx.doi.org/10.1021/np070190s.

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20

Brownrigg, George P., James Johnson та Elizabeth J. Rideout. "80 - Sex Differences in β-Cell Protein Folding Machinery". Canadian Journal of Diabetes 44, № 7 (2020): S32. http://dx.doi.org/10.1016/j.jcjd.2020.08.086.

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21

Gandhi, Jason, Anthony C. Antonelli, Adil Afridi, et al. "Protein misfolding and aggregation in neurodegenerative diseases: a review of pathogeneses, novel detection strategies, and potential therapeutics." Reviews in the Neurosciences 30, no. 4 (2019): 339–58. http://dx.doi.org/10.1515/revneuro-2016-0035.

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Abstract Protein folding is a complex, multisystem process characterized by heavy molecular and cellular footprints. Chaperone machinery enables proper protein folding and stable conformation. Other pathways concomitant with the protein folding process include transcription, translation, post-translational modifications, degradation through the ubiquitin-proteasome system, and autophagy. As such, the folding process can go awry in several different ways. The pathogenic basis behind most neurodegenerative diseases is that the disruption of protein homeostasis (i.e. proteostasis) at any level wi
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22

Parray, 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 (2022): 1539. http://dx.doi.org/10.3390/polym14081539.

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Proteins are indispensable to cellular communication and metabolism. The structure on which cells and tissues are developed is deciphered from proteins. To perform functions, proteins fold into a three-dimensional structural design, which is specific and fundamentally determined by their characteristic sequence of amino acids. Few of them have structural versatility, allowing them to adapt their shape to the task at hand. The intermediate states appear momentarily, while protein folds from denatured (D) ⇔ native (N), which plays significant roles in cellular functions. Prolific effort needs to
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23

Scheuner, 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 (2008): 317–33. http://dx.doi.org/10.1210/er.2007-0039.

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Abstract The endoplasmic reticulum (ER) is the entry site into the secretory pathway for newly synthesized proteins destined for the cell surface or released into the extracellular milieu. The study of protein folding and trafficking within the ER is an extremely active area of research that has provided novel insights into many disease processes. Cells have evolved mechanisms to modulate the capacity and quality of the ER protein-folding machinery to prevent the accumulation of unfolded or misfolded proteins. These signaling pathways are collectively termed the unfolded protein response (UPR)
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Lim, 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 (2016): 13045–50. http://dx.doi.org/10.1073/pnas.1611781113.

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Proper folding of proteins is critical to producing the biological machinery essential for cellular function. The rates and energetics of a protein’s folding process, which is described by its energy landscape, are encoded in the amino acid sequence. Over the course of evolution, this landscape must be maintained such that the protein folds and remains folded over a biologically relevant time scale. How exactly a protein’s energy landscape is maintained or altered throughout evolution is unclear. To study how a protein’s energy landscape changed over time, we characterized the folding trajecto
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25

Chambers, 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 (2014): C657—C670. http://dx.doi.org/10.1152/ajpcell.00183.2014.

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The endoplasmic reticulum (ER) is a major site of protein synthesis, most strikingly in the specialized secretory cells of metazoans, which can produce their own weight in proteins daily. Cells possess a diverse machinery to ensure correct folding, assembly, and secretion of proteins from the ER. When this machinery is overwhelmed, the cell is said to experience ER stress, a result of the accumulation of unfolded or misfolded proteins in the lumen of the organelle. Here we discuss the causes of ER stress and the mechanisms by which cells elicit a response, with an emphasis on recent discoverie
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26

Zhao, Rongmin, and Walid A. Houry. "Hsp90: a chaperone for protein folding and gene regulation." Biochemistry and Cell Biology 83, no. 6 (2005): 703–10. http://dx.doi.org/10.1139/o05-158.

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Molecular chaperones are essential components of a quality control machinery present in the cell. They can either aid in the folding and maintenance of newly translated proteins, or they can lead to the degradation of misfolded and destabilized proteins. Hsp90 is a key member of this machinery. It is a ubiquitous molecular chaperone that is found in eubacteria and all branches of eukarya. It plays a central role in cellular signaling since it is essential for maintaining the activity of several signaling proteins, including steroid hormone receptors and protein kinases. Hsp90 is currently a no
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27

Zhang, Yongli, and Frederick M. Hughson. "Chaperoning SNARE Folding and Assembly." Annual Review of Biochemistry 90, no. 1 (2021): 581–603. http://dx.doi.org/10.1146/annurev-biochem-081820-103615.

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SNARE proteins and Sec1/Munc18 (SM) proteins constitute the core molecular engine that drives nearly all intracellular membrane fusion and exocytosis. While SNAREs are known to couple their folding and assembly to membrane fusion, the physiological pathways of SNARE assembly and the mechanistic roles of SM proteins have long been enigmatic. Here, we review recent advances in understanding the SNARE–SM fusion machinery with an emphasis on biochemical and biophysical studies of proteins that mediate synaptic vesicle fusion. We begin by discussing the energetics, pathways, and kinetics of SNARE f
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28

Benham, 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 (2013): 20110403. http://dx.doi.org/10.1098/rstb.2011.0403.

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The protein folding machinery of the endoplasmic reticulum (ER) ensures that proteins entering the eukaryotic secretory pathway acquire appropriate post-translational modifications and reach a stably folded state. An important component of this protein folding process is the supply of disulfide bonds. These are introduced into client proteins by ER resident oxidoreductases, including ER oxidoreductin 1 (Ero1). Ero1 is usually considered to function in a linear pathway, by ‘donating’ a disulfide bond to protein disulfide isomerase (PDI) and receiving electrons that are passed on to the terminal
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29

Berner, 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 (2018): 751–82. http://dx.doi.org/10.1146/annurev-biochem-062917-012749.

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Cells must constantly monitor the integrity of their macromolecular constituents. Proteins are the most versatile class of macromolecules but are sensitive to structural alterations. Misfolded or otherwise aberrant protein structures lead to dysfunction and finally aggregation. Their presence is linked to aging and a plethora of severe human diseases. Thus, misfolded proteins have to be rapidly eliminated. Secretory proteins constitute more than one-third of the eukaryotic proteome. They are imported into the endoplasmic reticulum (ER), where they are folded and modified. A highly elaborated m
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30

Shen, Gang, and Brian S. J. Blagg. "Radester, a Novel Inhibitor of the Hsp90 Protein Folding Machinery." Organic Letters 7, no. 11 (2005): 2157–60. http://dx.doi.org/10.1021/ol050580a.

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31

Daverkausen-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 (2022): 5576. http://dx.doi.org/10.3390/ijms23105576.

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The endoplasmic reticulum (ER) of mammalian cells is the central organelle for the maturation and folding of transmembrane proteins and for proteins destined to be secreted into the extracellular space. The proper folding of target proteins is achieved and supervised by a complex endogenous chaperone machinery. BiP, a member of the Hsp70 protein family, is the central chaperone in the ER. The chaperoning activity of BiP is assisted by ER-resident DnaJ (ERdj) proteins due to their ability to stimulate the low, intrinsic ATPase activity of BiP. Besides their co-chaperoning activity, ERdj protein
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32

Shepherd, Colin, Ojore B. V. Oka та Neil J. Bulleid. "Inactivation of mammalian Ero1α is catalysed by specific protein disulfide-isomerases". Biochemical Journal 461, № 1 (2014): 107–13. http://dx.doi.org/10.1042/bj20140234.

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The formation of disulfides in proteins that enter the endoplasmic reticulum is essential for their folding. We show in the present study that a key component of the machinery for disulfide formation is negatively regulated by the product of its catalytic activity.
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33

Zhu, 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 (2013): 28180–94. http://dx.doi.org/10.1074/jbc.m113.491613.

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34

Schlebach, 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 (2014): 1–34. http://dx.doi.org/10.1017/s0033583514000110.

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AbstractMost biological processes require the production and degradation of proteins, a task that weighs heavily on the cell. Mutations that compromise the conformational stability of proteins place both specific and general burdens on cellular protein homeostasis (proteostasis) in ways that contribute to numerous diseases. Efforts to elucidate the chain of molecular events responsible for diseases of protein folding address one of the foremost challenges in biomedical science. However, relatively little is known about the processes by which mutations prompt the misfolding of α-helical membran
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35

Hood, David A., and Anna-Maria Joseph. "Mitochondrial assembly: protein import." Proceedings of the Nutrition Society 63, no. 2 (2004): 293–300. http://dx.doi.org/10.1079/pns2004342.

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The protein import process of mitochondria is vital for the assembly of the hundreds of nuclear-derived proteins into an expanding organelle reticulum. Most of our knowledge of this complex multisubunit network comes from studies of yeast and fungal systems, with little information known about the protein import process in mammalian cells, particularly skeletal muscle. However, growing evidence indicates that the protein import machinery can respond to changes in the energy status of the cell. In particular, contractile activity, a powerful inducer of mitochondrial biogenesis, has been shown t
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36

Stubenrauch, 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 (2017): 170144. http://dx.doi.org/10.1098/rsob.170144.

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Fimbriae are long, adhesive structures widespread throughout members of the family Enterobacteriaceae. They are multimeric extrusions, which are moved out of the bacterial cell through an integral outer membrane protein called usher. The complex folding mechanics of the usher protein were recently revealed to be catalysed by the membrane-embedded translocation and assembly module (TAM). Here, we examine the diversity of usher proteins across a wide range of extraintestinal (ExPEC) and enteropathogenic (EPEC) Escherichia coli , and further focus on a so far undescribed chaperone–usher system, w
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Hamazaki, Jun, and Shigeo Murata. "ER-Resident Transcription Factor Nrf1 Regulates Proteasome Expression and Beyond." International Journal of Molecular Sciences 21, no. 10 (2020): 3683. http://dx.doi.org/10.3390/ijms21103683.

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Protein folding is a substantively error prone process, especially when it occurs in the endoplasmic reticulum (ER). The highly exquisite machinery in the ER controls secretory protein folding, recognizes aberrant folding states, and retrotranslocates permanently misfolded proteins from the ER back to the cytosol; these misfolded proteins are then degraded by the ubiquitin–proteasome system termed as the ER-associated degradation (ERAD). The 26S proteasome is a multisubunit protease complex that recognizes and degrades ubiquitinated proteins in an ATP-dependent manner. The complex structure of
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38

Pety 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.

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Proteins destined for the secretory pathway are translocated into the endoplasmic reticulum (ER), where they are subjected to a variety of post-translational modifications before they reach their final destination. Newly synthesized proteins that have defect in polypeptide folding or subunit assembly are recognized by quality control systems and eliminated by the 26S proteasome, a cytosolic ATP-dependent proteolytic machinery. Delivery of non-native ER proteins to the proteasome requires retrograde transport across the ER membrane and depends on a protein-unfolding machine consisting of Cdc48p
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Latorre, Victor, Florian Mattenberger, and Ron Geller. "Chaperoning the Mononegavirales: Current Knowledge and Future Directions." Viruses 10, no. 12 (2018): 699. http://dx.doi.org/10.3390/v10120699.

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The order Mononegavirales harbors numerous viruses of significant relevance to human health, including both established and emerging infections. Currently, vaccines are only available for a small subset of these viruses, and antiviral therapies remain limited. Being obligate cellular parasites, viruses must utilize the cellular machinery for their replication and spread. Therefore, targeting cellular pathways used by viruses can provide novel therapeutic approaches. One of the key challenges confronted by both hosts and viruses alike is the successful folding and maturation of proteins. In cel
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Yoo, 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.

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The endoplasmic reticulum (ER) is a pivotal regulator of folding, quality control, trafficking, and targeting of secreted and transmembrane proteins, and accordingly, eukaryotic cells have evolved specialized machinery to ensure that the ER enables these proteins to acquire adequate folding and maturation in the presence of intrinsic and extrinsic insults. This adaptive capacity of the ER to intrinsic and extrinsic perturbations is important for maintaining protein homeostasis, which is termed proteostasis. Failure in adaptation to these perturbations leads to accumulation of misfolded or unas
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41

Perni, Michele, and Benedetta Mannini. "Targeting Protein Aggregation in ALS." Biomolecules 14, no. 10 (2024): 1324. http://dx.doi.org/10.3390/biom14101324.

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Proteinopathies involve the abnormal accumulation of specific proteins. Maintaining the balance of the proteome is a finely regulated process managed by a complex network of cellular machinery responsible for protein synthesis, folding, and degradation. However, stress and ageing can disrupt this balance, leading to widespread protein aggregation. Currently, several therapies targeting protein aggregation are in clinical trials for ALS. These approaches mainly focus on two strategies: addressing proteins that are prone to aggregation due to mutations and targeting the cellular mechanisms that
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42

Voss-Andreae, Julian. "Protein Sculptures: Life's Building Blocks Inspire Art." Leonardo 38, no. 1 (2005): 41–45. http://dx.doi.org/10.1162/leon.2005.38.1.41.

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The author takes a literal look at the foundation of our physical existence by creating sculptures of proteins, the universal parts of the machinery of life. For him, it is less important to copy a molecule accurately in all its details than to find a guiding principle and follow it to see whether it yields artistically interesting results. The main idea underlying these sculptures is the analogy between the technique of mitered cuts and protein folding. The sculptures offer a sensual experience of a world that is usually accessible only through the intellect.
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Böttinger, Lena, Agnieszka Gornicka, Tomasz Czerwik, et al. "In vivo evidence for cooperation of Mia40 and Erv1 in the oxidation of mitochondrial proteins." Molecular Biology of the Cell 23, no. 20 (2012): 3957–69. http://dx.doi.org/10.1091/mbc.e12-05-0358.

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The intermembrane space of mitochondria accommodates the essential mitochondrial intermembrane space assembly (MIA) machinery that catalyzes oxidative folding of proteins. The disulfide bond formation pathway is based on a relay of reactions involving disulfide transfer from the sulfhydryl oxidase Erv1 to Mia40 and from Mia40 to substrate proteins. However, the substrates of the MIA typically contain two disulfide bonds. It was unclear what the mechanisms are that ensure that proteins are released from Mia40 in a fully oxidized form. In this work, we dissect the stage of the oxidative folding
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Saris, 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 (1997): 813–24. http://dx.doi.org/10.1083/jcb.137.4.813.

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Heat stress is an obvious hazard, and mechanisms to recover from thermal damage, largely unknown as of yet, have evolved in all organisms. We have recently shown that a marker protein in the ER of Saccharomyces cerevisiae, denatured by exposure of cells to 50°C after preconditioning at 37°C, was reactivated by an ATP-dependent machinery, when the cells were returned to physiological temperature 24°C. Here we show that refolding of the marker enzyme Hsp150Δ–β-lactamase, inactivated and aggregated by the 50°C treatment, required a novel ER-located homologue of the Hsp70 family, Lhs1p. In the abs
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Liu, 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 (2016): E4015—E4024. http://dx.doi.org/10.1073/pnas.1608795113.

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Our understanding of how the endoplasmic reticulum (ER)-associated protein degradation (ERAD) machinery efficiently targets terminally misfolded proteins while avoiding the misidentification of nascent polypeptides and correctly folded proteins is limited. For luminal N-glycoproteins, demannosylation of their N-glycan to expose a terminal α1,6-linked mannose is necessary for their degradation via ERAD, but whether this modification is specific to misfolded proteins is unknown. Here we report that the complex of the mannosidase Htm1p and the protein disulfide isomerase Pdi1p (Htm1p–Pdi1p) acts
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Velasco, 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 (2019): 4122. http://dx.doi.org/10.3390/ijms20174122.

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Proteins must fold into their native structure and maintain it during their lifespan to display the desired activity. To ensure proper folding and stability, and avoid generation of misfolded conformations that can be potentially cytotoxic, cells synthesize a wide variety of molecular chaperones that assist folding of other proteins and avoid their aggregation, which unfortunately is unavoidable under acute stress conditions. A protein machinery in metazoa, composed of representatives of the Hsp70, Hsp40, and Hsp110 chaperone families, can reactivate protein aggregates. We revised herein the p
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Herrmann, 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 (2007): 559–63. http://dx.doi.org/10.1083/jcb.200611060.

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The intermembrane space (IMS) of mitochondria, the compartment that phylogenetically originated from the periplasm of bacteria, contains machinery to catalyze the oxidative folding of proteins (Mesecke, N., N. Terziyska, C. Kozany, F. Baumann, W. Neupert, K. Hell, and J.M. Herrmann. 2005. Cell. 121:1059–1069; Rissler, M., N. Wiedemann, S. Pfannschmidt, K. Gabriel, B. Guiard, N. Pfanner, and A. Chacinska. 2005. J. Mol. Biol. 353: 485–492; Tokatlidis, K. 2005. Cell. 121:965–96). This machinery introduces disulfide bonds into newly imported precursor proteins, thereby locking them in a folded con
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Raj, 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.

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49

Kojer, 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 (2015): 195–204. http://dx.doi.org/10.1091/mbc.e14-10-1422.

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The mitochondrial intermembrane space (IMS) harbors an oxidizing machinery that drives import and folding of small cysteine-containing proteins without targeting signals. The main component of this pathway is the oxidoreductase Mia40, which introduces disulfides into its substrates. We recently showed that the IMS glutathione pool is maintained as reducing as that of the cytosol. It thus remained unclear how equilibration of protein disulfides with the IMS glutathione pool is prevented in order to allow oxidation-driven protein import. Here we demonstrate the presence of glutaredoxins in the I
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Naganathan, Athi N. "Molecular origins of folding rate differences in the thioredoxin family." Biochemical Journal 477, no. 6 (2020): 1083–87. http://dx.doi.org/10.1042/bcj20190864.

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Thioredoxins are a family of conserved oxidoreductases responsible for maintaining redox balance within cells. They have also served as excellent model systems for protein design and engineering studies particularly through ancestral sequence reconstruction methods. The recent work by Gamiz-Arco et al. [Biochem J (2019) 476, 3631–3647] answers fundamental questions on how specific sequence differences can contribute to differences in folding rates between modern and ancient thioredoxins but also among a selected subset of modern thioredoxins. They surprisingly find that rapid unassisted foldin
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