Proteins are very important for many different functions in our bodies. However, they are prone to misfold, which could make them acquire new toxic functions. In order to prevent these incidents, a special type of proteins called chaperones assist in the proper folding of different proteins. We investigated a special type of chaperones that anchor at the site of protein synthesis, the ribosome, to assist with the proper folding of proteins in yeast. The purpose of this study is to understand if the human version of these chaperones could function in S. cerevisiae
Cotranslational chaperones, ubiquitous in all living organisms, protect nascent polypeptides from ag...
The yeast Hsp70/40 system SSB–RAC (stress 70 B–ribosome-associated complex) binds to ribosomes and c...
Exponentially growing yeast cells produce every minute 4160,000 ribosomal proteins. Owing to their d...
Prions are an infectious class of misfolded proteins, characterized by their ability to self-propaga...
Proteins are complex macromolecules that carry out a variety of different functions like structural ...
Proteins are important molecules that are needed for structure, function, and other vital processes ...
The folding of newly synthesized proteins into their native structures is a fundamental but failure ...
Proteins are essential for life. A protein’s function in cells heavily depends on its shape. When a ...
<p>a) The Hsp70/Hsp40-chaperone system that consists of RAC (Ssz and Zuo), shown in purple and light...
The existence of specialized molecular chaperones that interact directly with ribosomes is well esta...
A central dogma in biology is the conversion of genetic information into active proteins. The biosyn...
Ribosome-tethered chaperones that interact with nascent polypeptide chains have been identified in b...
Ribosome-associated chaperones act in early folding events during protein synthesis. Structural info...
Zuotin and Ssz from yeast are members of the conserved Hsp40 and Hsp70 family of molecular chaperone...
De novo protein folding is delicate and error-prone and requires the guidance of molecular chaperone...
Cotranslational chaperones, ubiquitous in all living organisms, protect nascent polypeptides from ag...
The yeast Hsp70/40 system SSB–RAC (stress 70 B–ribosome-associated complex) binds to ribosomes and c...
Exponentially growing yeast cells produce every minute 4160,000 ribosomal proteins. Owing to their d...
Prions are an infectious class of misfolded proteins, characterized by their ability to self-propaga...
Proteins are complex macromolecules that carry out a variety of different functions like structural ...
Proteins are important molecules that are needed for structure, function, and other vital processes ...
The folding of newly synthesized proteins into their native structures is a fundamental but failure ...
Proteins are essential for life. A protein’s function in cells heavily depends on its shape. When a ...
<p>a) The Hsp70/Hsp40-chaperone system that consists of RAC (Ssz and Zuo), shown in purple and light...
The existence of specialized molecular chaperones that interact directly with ribosomes is well esta...
A central dogma in biology is the conversion of genetic information into active proteins. The biosyn...
Ribosome-tethered chaperones that interact with nascent polypeptide chains have been identified in b...
Ribosome-associated chaperones act in early folding events during protein synthesis. Structural info...
Zuotin and Ssz from yeast are members of the conserved Hsp40 and Hsp70 family of molecular chaperone...
De novo protein folding is delicate and error-prone and requires the guidance of molecular chaperone...
Cotranslational chaperones, ubiquitous in all living organisms, protect nascent polypeptides from ag...
The yeast Hsp70/40 system SSB–RAC (stress 70 B–ribosome-associated complex) binds to ribosomes and c...
Exponentially growing yeast cells produce every minute 4160,000 ribosomal proteins. Owing to their d...