The Experts below are selected from a list of 36 Experts worldwide ranked by ideXlab platform
Sergey Leikin - One of the best experts on this subject based on the ideXlab platform.
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chaperoning osteogenesis new Protein Folding Disease paradigms
Trends in Cell Biology, 2011Co-Authors: Elena Makareeva, Nydea A Aviles, Sergey LeikinAbstract:Recent discoveries of severe bone disorders in patients with deficiencies in several endoplasmic reticulum chaperones are reshaping the discussion of type I collagen Folding and related Diseases. Type I collagen is the most abundant Protein in all vertebrates and a crucial structural molecule for bone and other connective tissues. Its misFolding causes bone fragility, skeletal deformity and other tissue failures. Studies of newly discovered bone disorders indicate that collagen Folding, chaperones involved in the Folding process, cellular responses to misFolding and related bone pathologies might not follow conventional Protein Folding paradigms. In this review, we examine the features that distinguish collagen Folding from that of other Proteins and describe the findings that are beginning to reveal how cells manage collagen Folding and misFolding. We discuss implications of these studies for general Protein Folding paradigms, unfolded Protein response in cells and Protein Folding Diseases.
Elena Makareeva - One of the best experts on this subject based on the ideXlab platform.
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chaperoning osteogenesis new Protein Folding Disease paradigms
Trends in Cell Biology, 2011Co-Authors: Elena Makareeva, Nydea A Aviles, Sergey LeikinAbstract:Recent discoveries of severe bone disorders in patients with deficiencies in several endoplasmic reticulum chaperones are reshaping the discussion of type I collagen Folding and related Diseases. Type I collagen is the most abundant Protein in all vertebrates and a crucial structural molecule for bone and other connective tissues. Its misFolding causes bone fragility, skeletal deformity and other tissue failures. Studies of newly discovered bone disorders indicate that collagen Folding, chaperones involved in the Folding process, cellular responses to misFolding and related bone pathologies might not follow conventional Protein Folding paradigms. In this review, we examine the features that distinguish collagen Folding from that of other Proteins and describe the findings that are beginning to reveal how cells manage collagen Folding and misFolding. We discuss implications of these studies for general Protein Folding paradigms, unfolded Protein response in cells and Protein Folding Diseases.
Nydea A Aviles - One of the best experts on this subject based on the ideXlab platform.
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chaperoning osteogenesis new Protein Folding Disease paradigms
Trends in Cell Biology, 2011Co-Authors: Elena Makareeva, Nydea A Aviles, Sergey LeikinAbstract:Recent discoveries of severe bone disorders in patients with deficiencies in several endoplasmic reticulum chaperones are reshaping the discussion of type I collagen Folding and related Diseases. Type I collagen is the most abundant Protein in all vertebrates and a crucial structural molecule for bone and other connective tissues. Its misFolding causes bone fragility, skeletal deformity and other tissue failures. Studies of newly discovered bone disorders indicate that collagen Folding, chaperones involved in the Folding process, cellular responses to misFolding and related bone pathologies might not follow conventional Protein Folding paradigms. In this review, we examine the features that distinguish collagen Folding from that of other Proteins and describe the findings that are beginning to reveal how cells manage collagen Folding and misFolding. We discuss implications of these studies for general Protein Folding paradigms, unfolded Protein response in cells and Protein Folding Diseases.
Santiago Schnell - One of the best experts on this subject based on the ideXlab platform.
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Protein Interactions and Transition Times that Influence the Pathogenesis of Protein Folding Diseases
Biophysical Journal, 2014Co-Authors: Santiago SchnellAbstract:Protein Folding Diseases occur when a specific Protein fails to fold into its correct functional state as a consequence of mutation in the Protein amino acid sequence. In this talk, I present a model of the folded and misfolded Protein expression, processing and their interactions, which we have used to investigate how Protein Folding Disease phenotypes develop from mutated genotypes. Modeling Protein processing as a continuous flow reactor, we found that the pathogenesis of Protein Folding Diseases can be modulated by a combination of the transition time of folded and misfolded Proteins in the reactor, the ratio of folded and misfolded Protein inflow rates in the reactor and a chemical interaction parameter between folded and misfolded Proteins. Our analysis reveals therapeutic strategies targeting the modulation of Protein Folding Diseases, which have been recently explored in cellular and animal models of Mutant INS-gene Induced Diabetes of Youth and Congenital Hypothyroidism with deficient thyroglobulin.
Jozsef Szeberenyi - One of the best experts on this subject based on the ideXlab platform.
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problem solving test α1 antitrypsin deficiency an example for a Protein Folding Disease
Biochemistry and Molecular Biology Education, 2007Co-Authors: Jozsef SzeberenyiAbstract:Terms to be familiar with before you start to solve the test: Protein conformation, Protein Folding, proteases, Protein synthesis, Protein glycosylation, glycoProteins, N-linked and O-linked oligosaccharides, endoplasmic reticulum, Golgi complex, secretory pathway, microsomes, pulse/chase labeling, SDS-polyacrylamide gel electrophoresis, immunoprecipitation, chaperones, Protein translocation.
