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Given the success of Volume I of this Research Topic, and how rapid the subject area is evolving, we are pleased to announce the launch of the expanded volume: ‘Influence of Mutations, Stresses and Post-Translational Modifications on the Structure and Function of Heat Shock Proteins and their Relationship with Various Diseases'

Heat shock proteins (Hsps) are molecular chaperones induced under stress conditions such as
oxidative, heat, acidic etc., and prevent the aggregation/mis-folding of various client proteins that
are prone to partial denaturation and aid in the folding of the nascent proteins. Heat shock proteins
are classified into large and small heat shock proteins based on their monomeric molecular weight.
Large heat shock proteins (LHsps) help in the protein folding mostly via ATP dependent manner.
However, small heat shock proteins (sHsps) generally function in an ATP independent manner and
are regarded as the first line of defense against stress. They exhibit holdase function. Both large and
small heat shock proteins are found in almost all organisms and are characterized by their signature
conserved domain. Mutations, stresses, and post-translational modifications (PTMs) of Hsps are
implicated in various diseases that often modulate the structure, substrate binding capability,
subunit exchange dynamics, and chaperone function of Hsps. Therefore, understanding the
structure-function relationship of Hsps with different diseases will provide new avenues for building
better therapeutics and drugs by targeting the Hsps. Investigating the role of structural and
functional modulations of Hsps (due to mutations, stresses, and PTMs) in diseases is
multidisciplinary in nature. It involves the intervention from the areas of molecular biology,
microbiology, biophysics, biophysical chemistry, cell biology, biochemistry, and protein engineering.

Therefore, our aim is to collate a series of original articles, and reviews, and other article types that address the structural-functional role of sHsps in diseases. We aim to collect studies that outline the role of mutations, different stresses, and PTMs on the structure and function of Hsps and their relationship to the disease. This will expand our knowledge of the relationship between structure-function modulations of Hsps with diseases and will be a steppingstone towards the generation of new therapeutics.

We are seeking contributions in form of original articles, reviews, mini-reviews, and short communications on the following topics:

• PTMs and their effects on the structure-function of sHsps and their correlation with a particular disease

• Understanding the structure-function relationship of different Hsps in presence of stresses (especially oxidative stress)

• Effect of mutations that are responsible for a particular disease on the structure, function, and
substrate binding capability of Hsps

• Protein engineering of sHsps by mutagenesis to build better therapeutics.

The above list is neither exhaustive nor exclusive. Articles may be either data-based novel observations or must grant new insights into the correlation between the structure-function dynamics of sHsps with disease.

Keywords: holdase, chaperone function, Heat shock proteins, stressed client proteins, post- translational modifications, redox stress, apoptosis, human and plant diseases


Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.

Given the success of Volume I of this Research Topic, and how rapid the subject area is evolving, we are pleased to announce the launch of the expanded volume: ‘Influence of Mutations, Stresses and Post-Translational Modifications on the Structure and Function of Heat Shock Proteins and their Relationship with Various Diseases'

Heat shock proteins (Hsps) are molecular chaperones induced under stress conditions such as
oxidative, heat, acidic etc., and prevent the aggregation/mis-folding of various client proteins that
are prone to partial denaturation and aid in the folding of the nascent proteins. Heat shock proteins
are classified into large and small heat shock proteins based on their monomeric molecular weight.
Large heat shock proteins (LHsps) help in the protein folding mostly via ATP dependent manner.
However, small heat shock proteins (sHsps) generally function in an ATP independent manner and
are regarded as the first line of defense against stress. They exhibit holdase function. Both large and
small heat shock proteins are found in almost all organisms and are characterized by their signature
conserved domain. Mutations, stresses, and post-translational modifications (PTMs) of Hsps are
implicated in various diseases that often modulate the structure, substrate binding capability,
subunit exchange dynamics, and chaperone function of Hsps. Therefore, understanding the
structure-function relationship of Hsps with different diseases will provide new avenues for building
better therapeutics and drugs by targeting the Hsps. Investigating the role of structural and
functional modulations of Hsps (due to mutations, stresses, and PTMs) in diseases is
multidisciplinary in nature. It involves the intervention from the areas of molecular biology,
microbiology, biophysics, biophysical chemistry, cell biology, biochemistry, and protein engineering.

Therefore, our aim is to collate a series of original articles, and reviews, and other article types that address the structural-functional role of sHsps in diseases. We aim to collect studies that outline the role of mutations, different stresses, and PTMs on the structure and function of Hsps and their relationship to the disease. This will expand our knowledge of the relationship between structure-function modulations of Hsps with diseases and will be a steppingstone towards the generation of new therapeutics.

We are seeking contributions in form of original articles, reviews, mini-reviews, and short communications on the following topics:

• PTMs and their effects on the structure-function of sHsps and their correlation with a particular disease

• Understanding the structure-function relationship of different Hsps in presence of stresses (especially oxidative stress)

• Effect of mutations that are responsible for a particular disease on the structure, function, and
substrate binding capability of Hsps

• Protein engineering of sHsps by mutagenesis to build better therapeutics.

The above list is neither exhaustive nor exclusive. Articles may be either data-based novel observations or must grant new insights into the correlation between the structure-function dynamics of sHsps with disease.

Keywords: holdase, chaperone function, Heat shock proteins, stressed client proteins, post- translational modifications, redox stress, apoptosis, human and plant diseases


Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.

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