Results 71 to 80 of about 3,296,549 (170)
Engineering and evolution of molecular chaperones and protein disaggregases with enhanced activity
Frontiers in Molecular Biosciences, 2016 Cells have evolved a sophisticated proteostasis network to ensure that proteins acquire and retain their native structure and function. Critical components of this network include molecular chaperones and protein disaggregases, which function to prevent ...
Korrie eMack, James eShorter
doaj +1 more source
Type III secretion chaperones [Elektronisk resurs] : a molecular toolkit for all occasions
, 2010 Common to many bacteria is the ability to establish a symbiotic relationship or to evade innate immune responses of an animal, plant, fish or insect host. Most often this capacity is mediated by a type III secretion system (T3SS).
Francis, Matthew S,
core
Molecular chaperones and neuronal proteostasis. [PDF]
, 2015 Protein homeostasis (proteostasis) is essential for maintaining the functionality of the proteome. The disruption of proteostasis, due to genetic mutations or an age-related decline, leads to aberrantly folded proteins that typically lose their function.
Smith, HL, Li, W, Cheetham, ME
core
Cell Reports, 2019 Summary: The extracellular molecular chaperone heat shock protein 90 (eHSP90) stabilizes protease client the matrix metalloproteinase 2 (MMP2), leading to tumor cell invasion.
Alexander J. Baker-Williams +15 more
doaj +1 more source
Disaggregases, molecular chaperones that resolubilize protein aggregates
Anais da Academia Brasileira de Ciências, 2015 The process of folding is a seminal event in the life of a protein, as it is essential for proper protein function and therefore cell physiology. Inappropriate folding, or misfolding, can not only lead to loss of function, but also to the formation of ...
David Z. Mokry +2 more
doaj +1 more source
The Chaperonopathies - Diseases with Defective Molecular Chaperones
European Journal of Histochemistry, 2013 In the mid 1950's the Nobel Prize Laureate Christian B. Anfinsen from his research on the folding of ribonuclease A, began to concentrate on the problem of the relationship between structure and function in enzymes.
Giovanni Li Volti
doaj +1 more source
Molecular chaperons: chaperones and chaperonins [PDF]
, 2007 Proteins must be folded into their correct three-dimensional conformation in order to attain biological function. Conversely, protein aggregation and misfolding are primary contributors to many devastating "conformational" diseases.
Bregier, Cezary +2 more
core
Interaction of human heat shock protein 70 with tumor-associated peptides [PDF]
, 2009 Molecular chaperones of the heat shock protein 70 (Hsp70) family play a crucial role in the presentation of exogenous antigenic peptides by antigen-presenting cells (APCs).
Manzenrieder, Florian +20 more
core +1 more source
Structural and functional characterization of Pseudomonas aeruginosa CupB chaperones [PDF]
, 2010 Pseudomonas aeruginosa, an important human pathogen, is estimated to be responsible for,10% of nosocomial infections worldwide. The pathogenesis of P. aeruginosa starts from its colonization in the damaged tissue or medical devices (e. g.
Filloux, A. +23 more
core +1 more source
Molecular Chaperones and Neurodegeneration
, 2017 Molecular chaperones or heat-shock proteins (HSPs) play essential roles in safeguarding structural stability and preventing misfolding and aggregation of proteins, and maintaining the proteome functionality in the cell.
Cintia Roodveldt +2 more
core +1 more source