Relevant bibliographies by topics / Chaperony

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Academic literature on the topic 'Chaperony'

Author: Grafiati
Published: 24 April 2022

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Journal articles on the topic "Chaperony"

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Scalia, Federica, Alessandra Maria Vitale, Radha Santonocito, Everly Conway de Macario, Alberto J. L. Macario, and Francesco Cappello. "The Neurochaperonopathies: Anomalies of the Chaperone System with Pathogenic Effects in Neurodegenerative and Neuromuscular Disorders." Applied Sciences 11, no. 3 (January 20, 2021): 898. http://dx.doi.org/10.3390/app11030898.

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The chaperone (or chaperoning) system (CS) constitutes molecular chaperones, co-chaperones, and chaperone co-factors, interactors and receptors, and its canonical role is protein quality control. A malfunction of the CS may cause diseases, known as the chaperonopathies. These are caused by qualitatively and/or quantitatively abnormal molecular chaperones. Since the CS is ubiquitous, chaperonopathies are systemic, affecting various tissues and organs, playing an etiologic-pathogenic role in diverse conditions. In this review, we focus on chaperonopathies involved in the pathogenic mechanisms of diseases of the central and peripheral nervous systems: the neurochaperonopathies (NCPs). Genetic NCPs are linked to pathogenic variants of chaperone genes encoding, for example, the small Hsp, Hsp10, Hsp40, Hsp60, and CCT-BBS (chaperonin-containing TCP-1- Bardet–Biedl syndrome) chaperones. Instead, the acquired NCPs are associated with malfunctional chaperones, such as Hsp70, Hsp90, and VCP/p97 with aberrant post-translational modifications. Awareness of the chaperonopathies as the underlying primary or secondary causes of disease will improve diagnosis and patient management and open the possibility of investigating and developing chaperonotherapy, namely treatment with the abnormal chaperone as the main target. Positive chaperonotherapy would apply in chaperonopathies by defect, i.e., chaperone insufficiency, and consist of chaperone replacement or boosting, whereas negative chaperonotherapy would be pertinent when a chaperone actively participates in the initiation and progression of the disease and must be blocked and eliminated.
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Hervás, Rubén, and Javier Oroz. "Mechanistic Insights into the Role of Molecular Chaperones in Protein Misfolding Diseases: From Molecular Recognition to Amyloid Disassembly." International Journal of Molecular Sciences 21, no. 23 (December 2, 2020): 9186. http://dx.doi.org/10.3390/ijms21239186.

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Age-dependent alterations in the proteostasis network are crucial in the progress of prevalent neurodegenerative diseases, such as Alzheimer’s, Parkinson’s, or amyotrophic lateral sclerosis, which are characterized by the presence of insoluble protein deposits in degenerating neurons. Because molecular chaperones deter misfolded protein aggregation, regulate functional phase separation, and even dissolve noxious aggregates, they are considered major sentinels impeding the molecular processes that lead to cell damage in the course of these diseases. Indeed, members of the chaperome, such as molecular chaperones and co-chaperones, are increasingly recognized as therapeutic targets for the development of treatments against degenerative proteinopathies. Chaperones must recognize diverse toxic clients of different orders (soluble proteins, biomolecular condensates, organized protein aggregates). It is therefore critical to understand the basis of the selective chaperone recognition to discern the mechanisms of action of chaperones in protein conformational diseases. This review aimed to define the selective interplay between chaperones and toxic client proteins and the basis for the protective role of these interactions. The presence and availability of chaperone recognition motifs in soluble proteins and in insoluble aggregates, both functional and pathogenic, are discussed. Finally, the formation of aberrant (pro-toxic) chaperone complexes will also be disclosed.
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Zuehlke, Abbey D., Michael A. Moses, and Len Neckers. "Heat shock protein 90: its inhibition and function." Philosophical Transactions of the Royal Society B: Biological Sciences 373, no. 1738 (December 4, 2017): 20160527. http://dx.doi.org/10.1098/rstb.2016.0527.

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The molecular chaperone heat shock protein 90 (Hsp90) facilitates metastable protein maturation, stabilization of aggregation-prone proteins, quality control of misfolded proteins and assists in keeping proteins in activation-competent conformations. Proteins that rely on Hsp90 for function are delivered to Hsp90 utilizing a co-chaperone–assisted cycle. Co-chaperones play a role in client transfer to Hsp90, Hsp90 ATPase regulation and stabilization of various Hsp90 conformational states. Many of the proteins chaperoned by Hsp90 (Hsp90 clients) are essential for the progression of various diseases, including cancer, Alzheimer's disease and other neurodegenerative diseases, as well as viral and bacterial infections. Given the importance of these clients in different diseases and their dynamic interplay with the chaperone machinery, it has been suggested that targeting Hsp90 and its respective co-chaperones may be an effective method for combating a large range of illnesses. This article is part of the theme issue ‘Heat shock proteins as modulators and therapeutic targets of chronic disease: an integrated perspective’.
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Chen, Chih-Ling, Chien-Nan Lee, Yin-Hsiu Chien, Wuh-Liang Hwu, Tung-Ming Chang, and Ni-Chung Lee. "Novel Compound Heterozygous Variants in TBCD Gene Associated with Infantile Neurodegenerative Encephalopathy." Children 8, no. 12 (December 5, 2021): 1140. http://dx.doi.org/10.3390/children8121140.

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Mutations in tubulin-specific chaperon D (TBCD), the gene encoding one of the co-chaperons required for the assembly and disassembly of the α/β-tubulin heterodimers, have been reported to cause perturbed microtubule dynamics, resulting in debilitating early-onset progressive neurodegenerative disorder. Here, we identified two novel TBCD variants, c.1340C>T (p.Ala447Val), and c.817+2T>C, presented as compound heterozygotes in two affected siblings born to unaffected carrier parents. Clinical features included early-onset neurodegeneration, failure to thrive, respiratory failure, hypotonia, muscle weakness and atrophy and seizures. We established the genotype–phenotype relationship of these TBCD pathogenic variants and provided insight into the protein structural alteration that may contribute to this chaperone-associated tubulinopathy.
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Wang, Lisha, Liza Bergkvist, Rajnish Kumar, Bengt Winblad, and Pavel F. Pavlov. "Targeting Chaperone/Co-Chaperone Interactions with Small Molecules: A Novel Approach to Tackle Neurodegenerative Diseases." Cells 10, no. 10 (September 29, 2021): 2596. http://dx.doi.org/10.3390/cells10102596.

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The dysfunction of the proteostasis network is a molecular hallmark of neurodegenerative diseases such as Alzheimer’s disease, Parkinson’s disease, Huntington’s disease, and amyotrophic lateral sclerosis. Molecular chaperones are a major component of the proteostasis network and maintain cellular homeostasis by folding client proteins, assisting with intracellular transport, and interfering with protein aggregation or degradation. Heat shock protein 70 kDa (Hsp70) and 90 kDa (Hsp90) are two of the most important chaperones whose functions are dependent on ATP hydrolysis and collaboration with their co-chaperones. Numerous studies implicate Hsp70, Hsp90, and their co-chaperones in neurodegenerative diseases. Targeting the specific protein–protein interactions between chaperones and their particular partner co-chaperones with small molecules provides an opportunity to specifically modulate Hsp70 or Hsp90 function for neurodegenerative diseases. Here, we review the roles of co-chaperones in Hsp70 or Hsp90 chaperone cycles, the impacts of co-chaperones in neurodegenerative diseases, and the development of small molecules modulating chaperone/co-chaperone interactions. We also provide a future perspective of drug development targeting chaperone/co-chaperone interactions for neurodegenerative diseases.
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Stemp, Markus J., Suranjana Guha, F. Ulrich Hartl, and José M. Barral. "Efficient production of native actin upon translation in a bacterial lysate supplemented with the eukaryotic chaperonin TRiC." Biological Chemistry 386, no. 8 (August 1, 2005): 753–57. http://dx.doi.org/10.1515/bc.2005.088.

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Abstract Recombinant expression of actin in bacteria results in non-native species that aggregate into inclusion bodies. Actin is a folding substrate of TRiC, the chaperonin of the eukaryotic cytosol. By employing bacterial in vitro translation lysates supplemented with purified chaperones, we have found that TRiC is the only eukaryotic chaperone necessary for correct folding of newly translated actin. The actin thus produced binds deoxyribonuclease I and polymerizes into filaments, hallmarks of its native state. In contrast to its rapid folding in the eukaryotic cytosol, actin translated in TRiC-supplemented bacterial lysate folds with slower kinetics, resembling the kinetics upon refolding from denaturant. Lysate supplementation with the bacterial chaperonin GroEL/ES or the DnaK/DnaJ/GrpE chaperones leads to prevention of actin aggregation, yet fails to support its correct folding. This combination of in vitro bacterial translation and TRiC-assisted folding allows a detailed analysis of the mechanisms necessary for efficient actin folding in vivo. In addition, it provides a robust alternative for the production of substantial amounts of eukaryotic proteins that otherwise misfold or lead to cellular toxicity upon expression in heterologous hosts.
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Lin, Jiusheng, and Mark A. Wilson. "Escherichia coli Thioredoxin-like Protein YbbN Contains an Atypical Tetratricopeptide Repeat Motif and Is a Negative Regulator of GroEL." Journal of Biological Chemistry 286, no. 22 (April 15, 2011): 19459–69. http://dx.doi.org/10.1074/jbc.m111.238741.

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Many proteins contain a thioredoxin (Trx)-like domain fused with one or more partner domains that diversify protein function by the modular construction of new molecules. The Escherichia coli protein YbbN is a Trx-like protein that contains a C-terminal domain with low homology to tetratricopeptide repeat motifs. YbbN has been proposed to act as a chaperone or co-chaperone that aids in heat stress response and DNA synthesis. We report the crystal structure of YbbN, which is an elongated molecule with a mobile Trx domain and four atypical tetratricopeptide repeat motifs. The Trx domain lacks a canonical CXXC active site architecture and is not a functional oxidoreductase. A variety of proteins in E. coli interact with YbbN, including multiple ribosomal protein subunits and a strong interaction with GroEL. YbbN acts as a mild inhibitor of GroESL chaperonin function and ATPase activity, suggesting that it is a negative regulator of the GroESL system. Combined with previous observations that YbbN enhances the DnaK-DnaJ-GrpE chaperone system, we propose that YbbN coordinately regulates the activities of these two prokaryotic chaperones, thereby helping to direct client protein traffic initially to DnaK. Therefore, YbbN may play a role in integrating the activities of different chaperone pathways in E. coli and related bacteria.
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Griffith, Alijah A., and William Holmes. "Fine Tuning: Effects of Post-Translational Modification on Hsp70 Chaperones." International Journal of Molecular Sciences 20, no. 17 (August 28, 2019): 4207. http://dx.doi.org/10.3390/ijms20174207.

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The discovery of heat shock proteins shaped our view of protein folding in the cell. Since their initial discovery, chaperone proteins were identified in all domains of life, demonstrating their vital and conserved functional roles in protein homeostasis. Chaperone proteins maintain proper protein folding in the cell by utilizing a variety of distinct, characteristic mechanisms to prevent aberrant intermolecular interactions, prevent protein aggregation, and lower entropic costs to allow for protein refolding. Continued study has found that chaperones may exhibit alternative functions, including maintaining protein folding during endoplasmic reticulum (ER) import and chaperone-mediated degradation, among others. Alternative chaperone functions are frequently controlled by post-translational modification, in which a given chaperone can switch between functions through covalent modification. This review will focus on the Hsp70 class chaperones and their Hsp40 co-chaperones, specifically highlighting the importance of post-translational control of chaperones. These modifications may serve as a target for therapeutic intervention in the treatment of diseases of protein misfolding and aggregation.
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Ellis, R. John. "Assembly chaperones: a perspective." Philosophical Transactions of the Royal Society B: Biological Sciences 368, no. 1617 (May 5, 2013): 20110398. http://dx.doi.org/10.1098/rstb.2011.0398.

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The historical origins and current interpretation of the molecular chaperone concept are presented, with the emphasis on the distinction between folding chaperones and assembly chaperones. Definitions of some basic terms in this field are offered and misconceptions pointed out. Two examples of assembly chaperone are discussed in more detail: the role of numerous histone chaperones in fundamental nuclear processes and the co-operation of assembly chaperones with folding chaperones in the production of the world's most important enzyme.
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Matsukura, L., and N. Miyashita. "Simulation study of the function of domain swapping in the HSP90 chaperone cycle." Journal of Physics: Conference Series 2207, no. 1 (March 1, 2022): 012024. http://dx.doi.org/10.1088/1742-6596/2207/1/012024.

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Abstract HSP90 is one of the molecular chaperones, and it is known as an anti-cancer drug target. In the HSP90 chaperone cycle, when the ATP binds to the HSP90NTD, the HSP90 dimer forms a domain swapping in NTD. The stability of the HSP90 dimer is essential to the HSP90 chaperon cycle process. We have performed several molecular dynamics simulations of the HSP90 dimer to investigate how ATP binding and domain swapping have affected the stability. We analysed the fluctuation of critical residues for ATP binding and ATP hydrolysis in the HSP90NTD dimer conformation. As a result, we found that domain swapping is essential to the stability of the HSP90 dimer, while ATP is not so essential for the stability of the dimer conformation.
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Dissertations / Theses on the topic "Chaperony"

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Ignatyeva, Maria. "Identification et caractérisation de HIRIP3 comme nouveau chaperon d'histone H2A." Thesis, Strasbourg, 2017. http://www.theses.fr/2017STRAJ028.

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Le génome des cellules eucaryotes est empaqueté dans la chromatine, dont l’établissement et la maintenance nécessitent des processus d’assemblage et de remodelage. Ce travail de thèse a été consacré à la caractérisation de deux facteurs de la machinerie d’assemblage de la chromatine. Le premier facteur étudié dans ce travail était HIRIP3, un homologue mammifère de la levure H2A.Z chaperon Chz1. Nous voulions vérifier si HIRIP3 est une chaperon d'histone par elle-même. Pour commencer, nous avons décrit l'interaction de HIRIP3 avec les histones in vivo. Ensuite, nous avons étudié la spécificité structurale de cette interaction in vitro. Nous avons caractérisé HIRIP3 comme une nouvelle chaperon d'histone H2A qui utilise le motif CHZ pour sa fonction. La deuxième partie de ce travail a été axée sur le complexe de remodelage de la chromatine SRCAP. Nous avons cherché à décoder son réseau d'interaction et à décrire ses sous-complexes. Nous avons reconstitué le complexe de base YL1, SRCAP, TIP49A, TIP49B et H2A.Z / H2B en utilisant le système d'expression chez baculovirus. Notre protocole nous a permis de purifier un complexe de base adapté aux futures études structurelles par microscopie cryo-électronique
The genome of eukaryotic cells is packaged into chromatin, which establishment and maintenance require mechanisms of assembly and remodelling. This thesis work was dedicated to the characterization of two factors of chromatin assembly machinery. The first factor studied in this work was HIRIP3, a mammalian homologue of yeast H2A.Z chaperone Chz1. We aimed to test whether HIRIP3 is a histone chaperone by itself. At first, we established HIRIP3 interaction with histones in vivo. After then, we studied the structural specificity of this interaction in vitro. We have characterized HIRIP3 as a novel H2A histone chaperone that utilizes the CHZ motif for its function. The second part of this work was focused on SRCAP chromatin remodelling complex. We aimed to decipher its interaction network and to describe its sub-complexes. We have reconstituted YL1, SRCAP, TIP49A, TIP49B and H2A.Z/H2B core complex using baculovirus expression system. Our protocol allowed us to purify core complex suitable for future structural studies by cryo-electron microscopy
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Junior, Sergio Luiz Ramos. "Caracterização da chaperona Hsp100 de Leishmania braziliensis: estudos estruturais e funcionais." Universidade de São Paulo, 2018. http://www.teses.usp.br/teses/disponiveis/75/75133/tde-10102018-162854/.

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A leishmaniose é uma doença tropical negligenciada que afeta milhares de pessoas podendo até levar a óbito em sua forma visceral. Durante o seu ciclo de vida, o parasita passa por diversas mudanças ambientais como mudança de temperatura e pH, principalmente quando da transfecção do inseto vetor para o hospedeiro mamífero. Tais mudanças geram estresse celular que pode levar proteínas ao enovelamento incorreto assim como a processos agregativos, sendo necessários sistemas de controle de qualidade proteico para manter a homeostase celular, do qual fazem parte as chaperonas moleculares. Chaperonas como a Hsp100, ajudam a manter a homeostase celular e a adaptação desempenhando um papel importante para protozoários como a Leishmania braziliensis, causador da leishmaniose. A Hsp100 tem papel desagregase, atuando com outras chaperonas moleculares para a extração de polipeptídios de agregados proteicos possibilitando seu desenovelamento e posterior reenovelamento, evitando seu efeito tóxico sobre a célula. A Hsp100 parece ser essencial para esses microrganismos, no entanto não há muito dados disponíveis para Hsp100 em Leishmania sp. e Plasmodium sp. Neste trabalho está descrito o protocolo para expressão e purificação da Hsp100 recombinante de L. braziliensis (rLbHsp100), assim como sua caracterização estrutural e funcional inicial in vitro. A proteína foi analisada por espectropolarimetria de dicroísmo circular, apresentando estrutura típica de proteínas ricas em hélices α, a fluorescência estática de triptofano demonstrou que a proteína possui estrutura terciária local com seus triptofanos parcialmente expostos ao solvente. Por cromatografia de exclusão molecular analítica, observou-se que a LbHsp100 se comporta como um oligômero cujo estado é influenciado tanto pela concentração proteica como pela presença de nucleotídeos adenosina. Análises por ultracentrifugação analítica evidenciaram que a rLbHsp100 em solução apresenta um equilíbrio de diversas espécies havendo deslocamento para um hexâmero de maneira concentração dependente. Análises de SAXS confirmaram a estrutura hexamérica e proporcionaram a obtenção de um modelo ab initio da proteína. Através de microscopia eletrônica de transmissão pode-se observar a forma toróide e a dispersividade do sistema. Por fim, atestou-se que a proteína foi obtida funcional com fraca atividade ATPásica, apresentando também interações com nucleotídeos adenosina (ATP e ADP) assim como com a suramina.
Leishmaniasis is a neglected tropical disease that affects thousands of people and may even lead to death in its visceral form. During its life cycle, the parasite undergoes several environmental changes such as temperature and pH changes, especially when transfecting from the vector insect into the mammalian host. Such changes generate a cellular stress that can lead to misfolding as well as to aggregative processes, therefore a protein quality control system is necessary to maintain cell homeostasis, which includes molecular chaperones. Chaperones such as Hsp100 can help maintain cellular homeostasis and adaptation playing an important role for protozoa such as Leishmania braziliensis, which causes leishmaniasis. The Hsp100 has a disaggregase action, acting with other proteins of the chaperone system to extract polypeptides from protein aggregates, allowing their unfolding and subsequent refolding, avoiding their toxic effect on the cell. Hsp100 appears to be essential for these microorganisms, however there is not much data available for Hsp100 in Leishmania sp. and Plasmodium sp. This work describes the protocol for expression and purification of the recombinant Hsp100 of Leishmania braziliensis (rLbHsp100), as well as its initial in vitro characterization. The protein was analyzed by circular dichroism spectropolarimetry, presenting a typical structure of ?-helix rich protein as well as a concentration-dependent structure gain, static fluorescence of tryptophan demonstrated that the protein has local tertiary structure with its tryptophans partially exposed to the solvent. Analytical size exclusion chromatography showed that LbHsp100 behaves as an oligomer whose state is influenced by both the concentration and the presence of adenosine nucleotides. Analysis by analytical ultracentrifugation has shown that the rLbHsp100 in solution exhibits an equilibrium of several species shifting towards a hexamer in a concentration dependent manner. SAXS analyzes confirm the hexameric structure and had provide an ab initio model for the protein. Transmission electron microscopy shows the toroidal form and dispersivity of the system. Finally, the obtained protein had showed catalytic function, and also interacted with adenosine nucleotides (ATP and ADP) as well as suramine.
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Richter, Klaus. "Die ATP-Hydrolyse des molekularen Chaperons Hsp90 und ihre Regulation durch Co-Chaperone." [S.l. : s.n.], 2003. http://deposit.ddb.de/cgi-bin/dokserv?idn=970225741.

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Etchells, Stephanie Anne. "Examination of eukaryotic chaperonin-mediated nascent chain folding in the cytosol: a photocrosslinking approach." Texas A&M University, 2003. http://hdl.handle.net/1969.1/1170.

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TRiC (TCP-1 ring complex), a type II chaperonin, facilitates protein folding, and we previously showed that TRiC crosslinks to ribosome-bound actin and luciferase nascent chains. Here, it was found that actin and luciferase nascent chains were adjacent to more than one TRiC subunit at different stages of translation. Six and seven out of the eight TRiC subunits were photocrosslinked to the luciferase and actin nascent chains, respectively. Actin nascent chains with widely-spaced, site-specific probe locations were adjacent to the same three TRiC subunits (a, b and e) at different stages of translation. The exposure of other TRiC subunits to nascent chains varied with the length and identity of the nascent chain. In addition, the presence or absence of ATP influences the photocrosslinking yields. This suggests that ATP alters the conformation of the subunits and/or their affinity for the nascent chain. Photocrosslinking also revealed that TRiC is in close proximity to the exit site of the ribosomal tunnel, presumably to create a protected folding environment for the nascent chain. Immunoprecipitations under native conditions revealed that prefoldin photocrosslinks to the actin nascent chain and that these prefoldin-containing photoadducts are coimmunoprecipitated with antibodies specific for the TRiC a subunit. This result suggests that prefoldin and TRiC bind simultaneously to the same actin nascent chain. Photocrosslinking studies with probes at position 68 in the actin nascent chain revealed that prefoldin binds to the nascent chain subsequently to TRiC binding. An unknown protein with an apparent molecular mass of 105 kDa was shown to photocrosslink to the luciferase nascent chain in a length-dependent manner at specific probe locations close to the N-terminus of the nascent chain. Thus, the nascent chain sees a variety of proteins in its immediate environment as it emerges from the ribosomal tunnel and undergoes its chaperonin-assisted folding.
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Gomes, Francisco Edvan Rodrigues. "Clonagem, expressão e estudo de 3 co-chaperonas de Leishmania braziliensis." Universidade de São Paulo, 2011. http://www.teses.usp.br/teses/disponiveis/75/75132/tde-16092011-160310/.

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A leishmaniose é uma enfermidade infecciosa causada por várias espécies de parasitas do gênero Leishmania e representa um dos principais problemas de saúde pública nos países subdesenvolvidos. No hospedeiro, a sobrevivência do protozoário causador dessa doença depende de uma classe especial de proteínas, as chaperonas moleculares ou proteínas de choque térmico como também são conhecidas. A função dessas proteínas é auxiliar no processo de enovelamento protéico, no transporte de proteínas entre as membranas e em muitas outras importantes funções celulares. Neste processo, as chaperonas moleculares são auxiliadas pelas suas co-chaperonas que desempenham função de destaque. Dentre as principais famílias de chaperonas moleculares temos as Hsp70 e as Hsp90 com suas respectivas co-chaperonas, as Hsp40 e a Aha1. O presente trabalho pretendeu inicialmente expressar e purificar as co-chaperonas moleculares Hsp40I e Hsp40II de L. braziliensis para realizar estudos de caracterização estrutural por meio das técnicas de dicroísmo circular e fluorescência. Contudo, a insolubilidade dessas proteínas, que pode ter sido causada pela presença de mutações nas sequências de DNA, motivou a caracterização de outra co-chaperona, a Aha1 de L. braziliensis (LbAha1). A LbAha1 foi expressa no sobrenadante celular e purificada por três etapas cromatográficas (troca aniônica, afinidade por íons cálcio e gel filtração). A análise da sequência de aminoácidos dessa proteína mostra que ela possui 9 resíduos de triptofano distribuídos nos dois domínios característicos da LbAha1. Estudos de desnaturação química por uréia, monitorados pelas técnicas de dicroísmo circular e fluorescência, mostram que os dois domínios da LbAha1 apresentam estabilidades diferentes. Os estudos estruturais realizados permitiram identificar as transições com o respectivo domínio.
Leishmaniasis is an infectious disease caused by several species of Leishmania species and represents major public health problems in developing countries. In the harborer, the survival of the parasite that cause this disease depends on a special class of proteins, molecular chaperones or heat shock proteins as they are also known. The function of these proteins is to assist in protein folding, transport of proteins and many other important cellular functions. In this process the molecular chaperones are helped by their co-chaperones that play a prominent role. Among the main families of molecular chaperones, there are Hsp70 and Hsp90 with their respective co-chaperones, Hsp40 and the Aha1. The present work, initially pretended to express and purify the molecular co-chaperones Hsp40I and Hsp40II of the L. braziliensis for structural characterization by spectroscopic techniques like fluorescence and circular dichroism. However, the insolubility of these proteins, possibly caused by the presence of mutations in their DNA sequences, led to the characterization of another co-chaperone, the Aha1 of the L. braziliensis. These proteins were expressed in the cell supernatant and purified by three chromatographic steps (anion exchange, affinity for calcium ions and gel filtration). The analysis of the DNA sequence of this protein shows that it has nine Trp residues distributed between the two domains and by urea denaturation studies monitored by fluorescence techniques and circular dichroism show that they have different stabilities.
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Murakami, Letícia Maria Zanphorlin 1984. "Hsp90 humana : interação com a co-chaperona Tom70 e efeito do celastrol na estrutura e função." [s.n.], 2014. http://repositorio.unicamp.br/jspui/handle/REPOSIP/249751.

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Orientador: Carlos Henrique Inácio Ramos
Tese (doutorado) - Universidade Estadual de Campinas, Instituto de Química
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Resumo: Chaperonas moleculares e proteínas de choque térmico (Heat shock protein, Hsp) atuam contra a agregação e o enovelamento incorreto de proteínas, que são os agentes causais de doenças neurodegenerativas, como por exemplo, Alzheimer e Parkinson. A Hsp90 é uma das mais importantes chaperonas moleculares, considerada essencial para a viabilidade celular em eucariotos, pois está associada com a maturação de proteínas atuantes na sinalização e ciclo celular. Além disso, foi demonstrado que a Hsp90 está envolvida na estabilização do fenótipo tumoral de diversos tipos de câncer, destacando a sua importância biomédica. A interação com co-chaperonas, proteínas auxiliares das chaperonas, permite que a Hsp90 atue como uma proteína "hub", ou seja, um ponto central de regulação de diversas proteínas. Muitas dessas co-chaperonas possuem um ou mais domínios do tipo TPR (do inglês, tetratricopeptide repeat) que interagem com o C-terminal da Hsp90. No presente projeto de doutorado, investigamos as características estruturais e termodinâmicas da interação entre o domínio C-terminal da Hsp90 (C-Hsp90) e a co-chaperona TPR Tom70 humana, utilizando técnicas de reação-cruzada acoplada à espectrometria de massas (LC-MS/MS), calorimetria de titulação isotérmica (ITC), espalhamento de raios-X à baixos ângulos (SAXS) e modelagem molecular. Os resultados de LC-MS/MS e ITC evidenciaram novas regiões na interação do complexo C-Hsp90/Tom70 que envolve a hélice A7 presente na Tom70 e experimentos de SAXS revelaram a estrutura em baixa resolução das proteínas C-Hsp90, Tom70 e do complexo C-Hsp90/Tom70. Além disso, investigamos o efeito do celastrol, um composto com potencial atividade anti-câncer, na conformação e na função da Hsp90. Na presença do composto, a Hsp90 sofre um processo de oligomerização e a natureza dos oligômeros foi determinada por ferramentas bioquímicas e biofísicas, tais como espalhamento dinâmico de luz (DLS), cromatografia de exclusão molecular analítica acoplada a espalhamento de luz em multiângulos (SEC-MALS) e eletroforese em gel nativo. Interessantemente, a oligomerização induzida pelo celastrol não afetou a atividade de proteção da Hsp90 contra a agregação protéica e a capacidade de ligação as co-chaperonas com enovelamento tipo TPR. Este é o primeiro trabalho a apontar um possível mecanismo para a ação do celastrol sobre a Hsp90. Coletivamente, nossos resultados e descobertas contribuem para uma melhor compreensão dos mecanismos moleculares relacionados à interação entre chaperonas e co-chaperonas, bem como, chaperonas e potenciais ligantes.
Abstract: Molecular chaperones and heat shock proteins (Hsp) act against protein aggregation and misfolding, which are the causal agents of neurodegenerative diseases such as Alzheimer and Parkinson. Hsp90 is one of the most important molecular chaperones, considered essential for cell viability in eukaryotes, since it is associated with the maturation of proteins involved in cell cycle and signaling. In addition, it was demonstrated that Hsp90 is implicated in the stabilization of the tumor phenotype of various types of cancer, highlighting its biomedical importance. The interaction with co-chaperones, auxiliary proteins of chaperones, allows that Hsp90 acts as a hub, being a central point for regulation of several other proteins. Many of these co-chaperones have one or more TPR domains that interact with the C-terminus of Hsp90. In this PhD project, we investigated structural and thermodynamic characteristics of the interaction between the C-terminus domain of Hsp90 (C-Hsp90) and the TPR co-chaperone human Tom70, using techniques of cross-linking coupled with mass spectrometry (LC-MS/MS), isothermal titration calorimetry (ITC), small angle X-ray scattering (SAXS) and molecular modeling. The results of LC-MS/MS and ITC revealed new regions involved in the interaction of the C-Hsp90 with Tom70, which encompasses the A7 helix from Tom70, and SAXS experiments unveiled the low resolution structure of the proteins C-Hsp90, Tom70 and the C-Hsp90/Tom70 complex. In addition, we investigated the effect of celastrol, a compound with a potential anti-cancer activity, on the conformation and function of Hsp90. In the presence of celastrol, Hsp90 undergoes oligomerization and the nature of the oligomers was determined by biochemical and biophysical tools such as dynamic light scattering (DLS), size-exclusion chromatography coupled to multi-angle light scattering (SEC-MALS) and native gel electrophoresis. Interestingly, the celastrol-induced oligomerization did not affect the protective activities of Hsp90 against protein aggregation or the capacity to bind TPR co-chaperones. This is the first study to point out a possible mechanism for the action of celastrol on Hsp90. Collectively, our findings contribute to a better understanding of the molecular mechanisms associated to the interaction between chaperones and co-chaperones, as well as chaperones and potential ligands
Doutorado
Quimica Organica
Doutora em Ciências
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Klunker, Daniel. "Chaperon-vermittelte Proteinfaltung in Archaea strukturelle und funktionelle Charakterisierung von MtGimC, einem hochkonservierten neuartigen Chaperon, MmGroEL, GroES, einem Gruppe-I-Chaperonin in Archaea /." [S.l. : s.n.], 2003. http://deposit.ddb.de/cgi-bin/dokserv?idn=969891806.

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Molina, Roberto Augusto Silva. "Caracterização da distribuição subcelular e tecidual da proteína KIAA0090 e estudos de seu envolvimento em câncer e resposta a estresses." Universidade de São Paulo, 2010. http://www.teses.usp.br/teses/disponiveis/17/17136/tde-19072010-140649/.

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O gene humano KIAA0090 mapeia uma região cromossômica (1p36.13) com freqüentes aberrações em cânceres humanos e é superexpresso em muitos tipos de tumores. É um gene altamente complexo cujas seqüências de cDNA oriundas de bases de dados públicas apóiam a existência de mais de 20 transcritos alternativos. Sua RefSeq prediz a codificação de uma proteína altamente conservada com 993aa, cujo ortólogo em S. cerevisae (ECM1) foi proposto recentemente atuar no enovelamento de proteínas transmembrana no retículo endoplasmático (RE). O objetivo deste trabalho foi adquirir conhecimento sobre a localização e função da proteína KIAA0090, em células e tecidos normais e tumorais, bem como em células expostas a estresse. Geramos anticorpos policlonais (anti-K2) contra a metade C-terminal da proteína e comparamos seu padrão ao tratamento obtido com o anticorpo (anti-K1), previamente gerado contra a metade N-terminal. A proteína endógena foi localizada primariamente no Golgi e na mitocôndria, dependendo se o anticorpo utilizado foi contra a região N- ou C-terminal, respectivamente. Observamos também, embora menos notável, uma marcação sobreposta com a rede do RE e na margem celular, e variáveis graus de marcação dentro do núcleo e associada a pequenas partículas citoplasmáticas. A análise imunohistoquímica forneceu evidências que a KIAA0090 é ubiquamente epressa. O anti-K2 marcou estruturas semelhantes a Golgi em todo tipo celular, predominando assim naquelas com Golgi mais visíveis, como células secretórias. Observamos para a maioria dos tecidos uma marcação leve a moderada para o anti-K1, mas uma forte marcação foi encontrada em grupos restritos de células, como as células reticulares do timo, epitélio ductal das glândulas da língua e na lâmina basal do epitélio escamoso na zona de transição esôfago-gástrica. Em cortes histológicos de melanoma primário, observamos uma forte marcação para o anti-K1, principalmente em vasos e em células invasoras na margem do tumor, enquanto o anti-K2 mostrou um padrão sugestivo de infiltrado inflamatório e/ou células mesenquimais. Em tecidos de câncer de mama, vimos uma forte marcação nas células de carcinoma ductal em comparação ao epitélio ductal normal para o anti-K2, ao passo que o anti-K1, marcou fortemente vasos e células basais no epitélio de revestimento glandular, tanto no tecido normal como no tumoral. Utilizando uma matriz com amostras teciduais de câncer de mama obtidas de 96 pacientes, observamos uma marcação forte a moderada para o anti-K1 em 84% dos casos, enquanto 16% dos casos não apresentaram marcação. Notamos que os casos positivos para o anti-K1 estavam 100, 85 e 71% entre os casos de grade 1, 2 e 3, respectivamente, sugerindo uma tendência de perda da KIAA0090 associada à progressão do câncer de mama. Foi interessante notar que a brefeldina A e MG132 alteraram os níveis de RNAm da KIAA0090 e levaram à redistribuição da proteína endógena. Outros tratamentos de estresse, incluindo tunicamicina, complexo de rutênio doador de óxido nítrico e etoposídeo, também alteraram o padrão de distribuição da proteína. Este estudo fornece evidências preliminares que corroboram os resultados obtidos de estudos de expressão gênica em larga escala, fortalecendo os indícios de que a KIAA0090 desenvolve um papel na homeostase celular e está envolvida no câncer.
Human KIAA0090 gene maps to a chromosomal region (1p36.13) with frequent aberrations in cancer and is overexpressed in many tumor types. It is a highly complex gene with cDNA sequences in databases supporting the occurrence of more than 20 alternative transcripts. The RefSeq transcript is predicted to encode a highly conserved 993 aa transmembrane protein whose S. cerevisiae ortolog (EMC1) was recently proposed to function on transmembrane protein folding in the endoplasmic reticulum (ER). The aim of this work was to gain insight into the localization and function of KIAA0090 protein, in normal and tumor cells and tissues, as well as in cells exposed to stress treatments. We raised a polyclonal antibody (anti-K2) to the C-terminal half of the protein and compared its pattern of staining with an antibody (anti-K1) previously generated in our laboratory to the N-terminal half. The endogenous protein was primarily localized either to mitochondria or Golgi, depending whether the antibody used was to the N- or C-terminal, respectively. Also, less conspicuous staining overlapped with the ER network and cell margin, and variable degrees of labeling was observed within the nucleus and associated to small cytoplasmic particles. Immunohistochemistry survey provided evidence that the KIAA0090 protein is ubiquitously expressed. Anti-K2 labeled in a Golgi-like pattern in every cell type, predominating in those with more conspicuous Golgi, such as secretory cells. Faint to moderate anti-K1 staining was found in most tissues, but very strong staining was seen in restricted groups of cells, such as thymus reticular cells, ductal epithelium of salivary lingual glands and the basal layer of the squamous epithelium in the esophagus-gastric transition zone. In histological sections of primary melanomas, we observed a strong staining for the anti-K1, mostly in vessels and at the invasive tumor margin, while the anti-K2 showed a staining pattern suggestive of infiltrating inflammatory and mesenchymal cells. In breast tissues, stronger staining was seen in ductal carcinoma cells in comparison to normal ductal epithelium for anti-K2 antibody, whereas anti-K1 strongly marked vessels and basal cells in epithelia lining glandular ducts both in normal and tumor tissues. Using a tissue array of breast cancer samples obtained from 96 patients, we observed strong to moderate staining for anti-K1 in 84% of the samples and lack of staining in 16%, interestingly anti-K1 positive cases were 100, 85 and 71% among cases of grades 1, 2 and 3, respectively, suggesting a tendency of KIAA0090 loss associated with breast cancer progression. A positive correlation was found with estrogen receptor expression and the opposite for HER2. Interestingly, Brefeldin A and MG132 altered KIAA0090 mRNA levels and caused endogenous KIAA0090 protein to redistribute. Other stress treatments, including tunicamycin, a ruthenium complex nitric oxide donor and etoposide, also altered KIAA0090 distribution. This study supports the notion that KIAA0090 play a role in cellular homeostasis and is involved in cancer.
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Moosavi, Behrooz. "The Role of Molecular Chaperone Hsp104 and its Co-chaperones in the Yeast [PSI+] Propagation." Thesis, University of Kent, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.499804.

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Genest, Olivier. "Les chaperons dédiés à la biogénèse des molybdoenzymes : étude du couple chaperon TorD - molybdoenzyme TorA chez Escherichia coli." Aix-Marseille 2, 2008. http://theses.univ-amu.fr.lama.univ-amu.fr/2008AIX22087.pdf.

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Les molybdoenzymes sont des métalloprotéines dont le site actif est constitué d’un cofacteur à molybdène. Ces molybdoenzymes sont retrouvées chez tous les êtres vivants, des bactéries à l’homme. Leur biogenèse est un processus complexe qui nécessite la présence de protéines chaperons spécifiques. Au cours de ma thèse, j’ai étudié le rôle de la protéine chaperon TorD dans la biogenèse de la molybdoenzyme TorA chez Escherichia coli. TorA est l’enzyme terminale périplasmique de la chaîne respiratoire triméthylamine oxyde (TMAO) réductase. J’ai montré que le chaperon spécifique TorD, localisé dans le cytoplasme, est essentiel à la protection de la forme non mature de TorA (apoTorA) lors d’un stress thermique ou d’une carence en cofacteur à molybdène. En effet, l’absence de TorD dans ces conditions entraîne la dégradation complète de l’apoprotéine. J’ai également montré que la séquence signal Tat de TorA, qui permet l’export de la protéine vers le périplasme est hypersensible à la dégradation par les protéases. Cette séquence signal pourrait être une voie d’entrée pour les protéases qui ensuite dégraderaient l’ensemble de l’apoenzyme. TorD en interagissant avec la séquence signal de TorA empêche cette première dégradation et permet donc la protection de l’apoenzyme. TorD se lie également à la partie globulaire d’poTorA. Par cette interaction, TorD permet une maturation optimale de l’apoenzyme. Les acides aminés de TorD impliqués dans cette interaction ont été déterminés après mutagenèse aléatoire. Ils sont localisés dans la cinquième hélice de TorD. J’ai également montré que TorD présente un rôle de plate-forme sur laquelle se lie le précurseur du cofacteur à molybdène et l’enzyme MobA permettant la synthèse de la forme mature du cofacteur. Après catalyse, cette forme mature du cofacteur qui se lie à TorD peut être délivrée à l’apoenzyme TorA. Ainsi, TorD connecte tous les éléments nécessaires à la maturation de TorA : d’une part il interagit avec le cofacteur à molybdène et d’autre part avec l’apoenzyme. Nous proposons donc que TorD interagisse à proximité du site actif de TorA pour y délivrer directement le cofacteur à molybdène
T-ALL is a lymphoid neoplasia that accounts for 10-15% of pediatric ALL and 25% of adult ALL. Alarmingly, and despite indisputable success achieved in treatments its incidence is increasing and its prognostic remains pejorative. Survival rate outcome depend notably on a better understanding in pathogenic mechanisms. In this context, the thesis work has been the following: 1) Based on the observation that rare chromosomal SJ keep on recombining in cis using V(D)J recombination, we hypothesized that episomal SJ (ESJ) still remain reactives and can undergo genomic reintegration. We show that mechanistically, ESJ efficiently rearrange in trans and that the cRSS, the sequences targeted in oncogenic chromosomal translocations, are good ESJ integration sites. Moreover, we demonstrate the presence of ESJ reintegration events in vivo and estimate their frequency to ~1/104-6. In conclusion, ESJ reintegration is a potential mechanism of oncogenic deregulation. 2) Conventional and illegitimate V(D)J recombination events (e. G. Translocations) are ordered during lymphocyte development. Based on our knowledge on chromosomal translocation mechanisms, we determine the kinetics of a subset of oncogenic activations acquired during the transformation process in a T-ALL patient’s leukemic cells. Moreover, we identified up to 10 independent oncogenic events in this patient, illustrating the multi-hit characteristic of T-ALL. Finally, the oncogenic event’s functional impact suggests that cMyc play an important role in the particularly aggressive features of the T-ALL developed by this patient
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Books on the topic "Chaperony"

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Moriarty, Laura. The chaperone. Detroit: Large Print Press/Gale Cengage Learning, 2013.

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Moriarty, Laura. The chaperone. New York: Riverhead Books, 2012.

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Moriarty, Laura. The chaperone. Waterville, Maine: Thorndike Press, 2012.

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Chaperoned. Las Vegas, NV: AmazonCrossing, 2012.

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Braakman, Ineke, ed. Chaperones. Berlin, Heidelberg: Springer Berlin Heidelberg, 2006. http://dx.doi.org/10.1007/b100697.

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Calderwood, Stuart K., and Thomas L. Prince, eds. Chaperones. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7477-1.

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Lambert, Lisa. The drowsy chaperone. Canada?: s.n., 2008.

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His lordship's chaperone. New York: Avalon Books, 2009.

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Copyright Paperback Collection (Library of Congress), ed. The Chaperon Bride. Toronto: Harlequin, 2004.

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Copyright Paperback Collection (Library of Congress), ed. The unsuitable chaperon. New York: New American Library, 1988.

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Book chapters on the topic "Chaperony"

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Fiedler, H. "Chaperone." In Springer Reference Medizin, 558. Berlin, Heidelberg: Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_708.

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Fiedler, H. "Chaperone." In Lexikon der Medizinischen Laboratoriumsdiagnostik, 1–2. Berlin, Heidelberg: Springer Berlin Heidelberg, 2018. http://dx.doi.org/10.1007/978-3-662-49054-9_708-1.

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Ecroyd, Heath. "Redefining the Chaperone Mechanism of sHsps: Not Just Holdase Chaperones." In Heat Shock Proteins, 179–95. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-16077-1_7.

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Bousset, Luc, Nicolas Fay, and Ronald Melki. "Template-induced protein misfolding underlying prion diseases." In Chaperones, 221–50. Berlin, Heidelberg: Springer Berlin Heidelberg, 2005. http://dx.doi.org/10.1007/4735_107.

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de Jonge, Wim, Henk F. Tabak, and Ineke Braakman. "Chaperone proteins and peroxisomal protein import." In Chaperones, 149–83. Berlin, Heidelberg: Springer Berlin Heidelberg, 2005. http://dx.doi.org/10.1007/b136669.

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Workman, Paul. "Reflections and Outlook on Targeting HSP90, HSP70 and HSF1 in Cancer: A Personal Perspective." In Advances in Experimental Medicine and Biology, 163–79. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-40204-4_11.

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Abstract This personal perspective focuses on small-molecule inhibitors of proteostasis networks in cancer—specifically the discovery and development of chemical probes and drugs acting on the molecular chaperones HSP90 and HSP70, and on the HSF1 stress pathway. Emphasis is on progress made and lessons learned and a future outlook is provided. Highly potent, selective HSP90 inhibitors have proved invaluable in exploring the role of this molecular chaperone family in biology and disease pathology. Clinical activity was observed, especially in non small cell lung cancer and HER2 positive breast cancer. Optimal use of HSP90 inhibitors in oncology will likely require development of creative combination strategies. HSP70 family members have proved technically harder to drug. However, recent progress has been made towards useful chemical tool compounds and these may signpost future clinical drug candidates. The HSF1 stress pathway is strongly validated as a target for cancer therapy. HSF1 itself is a ligandless transcription factor that is extremely challenging to drug directly. HSF1 pathway inhibitors have been identified mostly by phenotypic screening, including a series of bisamides from which a clinical candidate has been identified for treatment of ovarian cancer, multiple myeloma and potentially other cancers.
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Baker, Julien S., Fergal Grace, Lon Kilgore, David J. Smith, Stephen R. Norris, Andrew W. Gardner, Robert Ringseis, et al. "Protein Chaperone." In Encyclopedia of Exercise Medicine in Health and Disease, 732. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-540-29807-6_2918.

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Claeys, Kristl G., and Joachim Weis. "Chaperone Proteins." In Muscle Disease, 246–51. Oxford, UK: John Wiley & Sons, Ltd, 2013. http://dx.doi.org/10.1002/9781118635469.ch26.

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Boshoff, Aileen. "Chaperonin—Co-chaperonin Interactions." In Subcellular Biochemistry, 153–78. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-11731-7_8.

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Fasman, Gerald D. "Chaperones." In Circular Dichroism and the Conformational Analysis of Biomolecules, 531–54. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4757-2508-7_15.

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Conference papers on the topic "Chaperony"

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Strickland, T. Stephen, Sam Tobin-Hochstadt, Robert Bruce Findler, and Matthew Flatt. "Chaperones and impersonators." In the ACM international conference. New York, New York, USA: ACM Press, 2012. http://dx.doi.org/10.1145/2384616.2384685.

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Kampinga, Harm H. "A17 Chaperone biology and huntington aggregation." In EHDN 2018 Plenary Meeting, Vienna, Austria, Programme and Abstracts. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/jnnp-2018-ehdn.16.

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THIRUMALAI, DEVARAJAN. "CHAPERONIN-MEDIATED PROTEIN FOLDING." In Folding and Self-Assembly of Biological Macromolecules Conference. WORLD SCIENTIFIC, 2004. http://dx.doi.org/10.1142/9789812703057_0012.

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LANDRY, S. J., N. K. STEEDE, A. M. GARAUDY, K. MASKOS, and P. V. VIITANEN. "CHAPERONIN FUNCTION DEPENDS ON STRUCTURE AND DISORDER IN CO-CHAPERONIN MOBILE LOOPS." In Proceedings of the Pacific Symposium. WORLD SCIENTIFIC, 1998. http://dx.doi.org/10.1142/9789814447300_0052.

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Kabakov, A., E. Zotova, and A. Sobenin. "P5.16 Combination of inhibitors of chaperone activity and chaperone expression for prevention of hiv-1 reactivation from latency." In STI and HIV World Congress Abstracts, July 9–12 2017, Rio de Janeiro, Brazil. BMJ Publishing Group Ltd, 2017. http://dx.doi.org/10.1136/sextrans-2017-053264.632.

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Hosaka, Yusuke, Jun Araya, Kazuya Tsubouchi, Shunsuke Minagawa, Hiromichi Hara, Akihiro Ichikawa, Nayuta Saito, et al. "Role of chaperone-mediated autophagy in COPD pathogenesis." In ERS International Congress 2018 abstracts. European Respiratory Society, 2018. http://dx.doi.org/10.1183/13993003.congress-2018.pa2182.

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Kloog, Yoel, Roni Haklai, and Galit Elad-Sfadia. "Abstract B40: Blocking Ras chaperons for cancer therapy." In Abstracts: AACR Special Conference on RAS Oncogenes: From Biology to Therapy; February 24-27, 2014; Lake Buena Vista, FL. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1557-3125.rasonc14-b40.

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Saran, Shashwat, Mahadeva Ganesh, and Ezdihar Yousif. "P2 Chaperons for child protection medical examinations: a missing link?" In Faculty of Paediatrics of the Royal College of Physicians of Ireland, 9th Europaediatrics Congress, 13–15 June, Dublin, Ireland 2019. BMJ Publishing Group Ltd and Royal College of Paediatrics and Child Health, 2019. http://dx.doi.org/10.1136/archdischild-2019-epa.358.

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Hosaka, Yusuke, Jun Araya, Yu Fujita, Kazuya Tsubouchi, Shunsuke Minagawa, Hiromichi Hara, Takayuki Nakano, et al. "Chaperone-mediated autophagy modulates epithelial cell apoptosis in COPD pathogenesis." In ERS International Congress 2019 abstracts. European Respiratory Society, 2019. http://dx.doi.org/10.1183/13993003.congress-2019.pa2411.

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Yang, Lifang, and Zhuo Li. "Data Mining for the Interactive Requirement of Elderly Chaperone Robot." In 3rd International Conference on Mechatronics, Robotics and Automation. Paris, France: Atlantis Press, 2015. http://dx.doi.org/10.2991/icmra-15.2015.211.

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Reports on the topic "Chaperony"

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Vierling, Elizabeth. Hsp100/ClpB Chaperone Function and Mechanism. Office of Scientific and Technical Information (OSTI), January 2015. http://dx.doi.org/10.2172/1168677.

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Muga, Arturo. Asociaciones funcionales de chaperonas. Sociedad Española de Bioquímica y Biología Molecular (SEBBM), January 2012. http://dx.doi.org/10.18567/sebbmdiv_anc.2012.01.1.

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Paschal, Bryce M. Chaperone Function in Androgen-Independent Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, May 2010. http://dx.doi.org/10.21236/ada542323.

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Paschal, Bryce. Chaperone Function in Androgen-Independent Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, May 2011. http://dx.doi.org/10.21236/ada600480.

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Paschal, Bryce M. Chaperone Function in Androgen-Independent Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, May 2012. http://dx.doi.org/10.21236/ada601369.

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Trent, J. D., H. K. Kagawa, Takuro Yaoi, E. Olle, and N. J. Zaluzec. Chaperonin filaments: The archael cytoskeleton. Office of Scientific and Technical Information (OSTI), August 1997. http://dx.doi.org/10.2172/510354.

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Galili, Gad, and Alan Bennett. Role of Molecular Chaperone in Wheat Storage Protein Assembly. United States Department of Agriculture, April 1995. http://dx.doi.org/10.32747/1995.7604926.bard.

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Following sequestration into the ER, wheat gliadins assemble into complexes that initiate the formation of protein bodies. In the present work we have characterized the DNA sequence and regulation of expression of a plant BiP and also studied its interaction with wheat storage proteins as well as its role in the maturation of these storage proteins. In the Israeli lab, immunoprecipitation studies were made using anti BiP and anti storage proteins sera, both in wheat and in transgenic tobacco plants expressing a wheat gliadin storage proteins. In both cases, we could show that BiP interacts with the gliadin storage proteins. In addition, we could show that BiP also played an important role in the initial assembly of the gliadins. In the American lab, the complexity, structure and properties of tomato BiP was characterized at the molecular and biochemical levels. In addition, tomato BiP was also overexpressed in bacteria and the overexpressed protein was found to be active. The cooperative findings of the Israeli and American labs clearly improves our understanding of the structure and expression of a plant BiP as well as its role in the maturation of storage proteins in plants seeds. In addition, it will serve as a foundation for future studies of the mechanisms of BiP function in in vitro studies using purified storage proteins and purified recombinant active BiP.
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Trent, J. D., H. K. Kagawa, and N. J. Zaluzec. Chaperonin polymers in archaea: The cytoskeleton of prokaryotes? Office of Scientific and Technical Information (OSTI), July 1997. http://dx.doi.org/10.2172/505321.

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9

Robb, Frank T. Mechanisms of Stability of Robust Chaperones from Hyperthermophiles. Fort Belvoir, VA: Defense Technical Information Center, February 2009. http://dx.doi.org/10.21236/ada586573.

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10

Phillips, Courtney K. The Role of the Co-Chaperone, CHIP, in Androgen-Independent Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, February 2012. http://dx.doi.org/10.21236/ada585699.

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