Add to ORKGSome proteins synthesized by growing eukaryotic cells are transferred along unidirectional pathways of molecular chaperones until the risk of aggregation has decreased and they can be released safely. Mature proteins denatured by stress may instead be handled by chaperones acting in branched, reversible networks
Molecular chaperones are diverse families of multidomain proteins that have evolved to assist nascen...
External stresses or mutations may cause labile proteins to lose their distinct native conformations...
The efficiency, divergence, and specificity of virtually all intracellular metabolic and signalling ...
AbstractSome proteins synthesized by growing eukaryotic cells are transferred along unidirectional p...
Efficient folding of many newly synthesized proteins depends on assistance from molecular chaperones...
The biological functions of proteins are governed by their three-dimensional fold. Protein folding, ...
Efficient folding of many newly synthesized proteins depends on assistance from molecular chaperones...
After the discovery of the need for extensive assistance in protein folding in the case of many nasc...
Chaperones are centrally involved in the control of protein structure, function, localization and tr...
Stress-denatured or de novo synthesized and translocated unfolded polypeptides can spontaneously rea...
A variety of cellular internal and external stress conditions can be classified as proteotoxic stres...
Co-chaperones are important mediators of the outcome of chaperone assisted protein homeostasis, whic...
Proteins are composed of linear chains of amino acids. Upon synthesis in the cell, most proteins mus...
AbstractMolecular chaperones and energy-dependent proteases have long been viewed as opposing forces...
Stress, molecular crowding and mutations may jeopardize the native folding of proteins. Misfolded an...
Molecular chaperones are diverse families of multidomain proteins that have evolved to assist nascen...
External stresses or mutations may cause labile proteins to lose their distinct native conformations...
The efficiency, divergence, and specificity of virtually all intracellular metabolic and signalling ...
AbstractSome proteins synthesized by growing eukaryotic cells are transferred along unidirectional p...
Efficient folding of many newly synthesized proteins depends on assistance from molecular chaperones...
The biological functions of proteins are governed by their three-dimensional fold. Protein folding, ...
Efficient folding of many newly synthesized proteins depends on assistance from molecular chaperones...
After the discovery of the need for extensive assistance in protein folding in the case of many nasc...
Chaperones are centrally involved in the control of protein structure, function, localization and tr...
Stress-denatured or de novo synthesized and translocated unfolded polypeptides can spontaneously rea...
A variety of cellular internal and external stress conditions can be classified as proteotoxic stres...
Co-chaperones are important mediators of the outcome of chaperone assisted protein homeostasis, whic...
Proteins are composed of linear chains of amino acids. Upon synthesis in the cell, most proteins mus...
AbstractMolecular chaperones and energy-dependent proteases have long been viewed as opposing forces...
Stress, molecular crowding and mutations may jeopardize the native folding of proteins. Misfolded an...
Molecular chaperones are diverse families of multidomain proteins that have evolved to assist nascen...
External stresses or mutations may cause labile proteins to lose their distinct native conformations...
The efficiency, divergence, and specificity of virtually all intracellular metabolic and signalling ...