Search results for "chaperonopathies by mistake"

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Molecular Chaperones and Thyroid Cancer

2021

Thyroid cancers are the most common of the endocrine system malignancies and progress must be made in the areas of differential diagnosis and treatment to improve patient management. Advances in the understanding of carcinogenic mechanisms have occurred in various fronts, including studies of the chaperone system (CS). Components of the CS are found to be quantitatively increased or decreased, and some correlations have been established between the quantitative changes and tumor type, prognosis, and response to treatment. These correlations provide the basis for identifying distinctive patterns useful in differential diagnosis and for planning experiments aiming at elucidating the role of t…

QH301-705.5thyroid tumorsHsp90Reviewmedicine.disease_causeCatalysisChaperoninHsp70Inorganic ChemistryHsp27chaperone systemdifferential diagnosismedicineAnimalsHumansHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsThyroid NeoplasmsBiology (General)Physical and Theoretical ChemistryHsp27QD1-999Molecular BiologyThyroid cancerSpectroscopychaperonotherapybiologychaperonopathies by mistakeOrganic ChemistryThyroidmolecular chaperonesChaperonin 60General Medicinemedicine.diseaseHsp60Hsp90Computer Science ApplicationsChemistrymedicine.anatomical_structureChaperone (protein)biology.proteinCancer researchHSP60CarcinogenesisInternational Journal of Molecular Sciences
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Chaperonopathies of senescence and the scrambling of interactions between the chaperoning and the immune systems.

2010

Aging entails progressive deterioration of molecules and supramolecular structures, including Hsp chaperones and their complexes, paralleled by functional decline. Recent research has changed our views on Hsp chaperones. They work inside and outside cells in many locations, alone or forming teams, interacting with cells, receptors, and molecules that are not chaperones, in roles that are not typically attributed to chaperones, such as protein folding. Hsp chaperones form a physiological system with a variety of functions and interactions with other systems, for example, the immune system. We propose that chaperone malfunctioning due to structural damage or gene dysregulation during aging ha…

AgingProtein Foldingchaperonopathies by mistakeSettore BIO/16 - Anatomia Umanachaperoning systemImmune Systemchaperoning system interactionchaperonopathieCarrier Proteinschaperonotherapy Hsp60Molecular ChaperonesAnnals of the New York Academy of Sciences
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