Search Results - "proteins"

Protein turnover

Subjects: “…Proteins Metabolism Congresses.…”
An electronic book accessible through the World Wide Web; click to view

Protein degradation

Table of Contents: “…Contents: Protein levels in cells are regulated by their rates of synthesis and degradation -- Regulatory proteins are rapidly degraded by the ubiquitin-proteasome pathway -- Examples include many oncogenes, transcription factors and cyclins which control progress through the cell cycle -- NF-kappa B activation in disease depends on degradation of the inhibitor, I-kappa B -- Misfolded or mutant proteins are rapidly degraded -- Neurodegenerative and protein folding diseases -- Two major proteolytic pathways exist in mammalian cells -- Many acid hydrolases exist in lysosomes -- Endocytosed proteins and those in autophagic vacuoles are degraded in lysosomes -- The ubiquitin-proteasome pathway -- 3D structure of ubiquitin -- Formation of the isopeptide bonds during ubiquitin conjugation to proteins -- The ubiquitin-proteasome pathway -- Proteasome function is linked to ATP hydrolysis -- Proteasomes unfold proteins and translocate them into 20S particles -- Three types of peptidase sites -- Proposed mechanism of proteasome inhibitors -- Therapeutic applications of proteasome inhibitors -- Two systems for protein breakdown function in the two pathways for antigen presentation -- Changes in proteasome subunits induced by interferon -- Steps involved in generating antigenic peptides.…”
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Protein degradation

Table of Contents: “…Contents: Protein levels in cells are regulated by their rates of synthesis and degradation -- Regulatory proteins are rapidly degraded by the ubiquitin-proteasome pathway -- Examples include many oncogenes, transcription factors and cyclins which control progress through the cell cycle -- NF-kappa B activation in disease depends on degradation of the inhibitor, I-kappa B -- Misfolded or mutant proteins are rapidly degraded -- Neurodegenerative and protein folding diseases -- Two major proteolytic pathways exist in mammalian cells -- Many acid hydrolases exist in lysosomes -- Endocytosed proteins and those in autophagic vacuoles are degraded in lysosomes -- The ubiquitin-proteasome pathway -- 3D structure of ubiquitin -- Formation of the isopeptide bonds during ubiquitin conjugation to proteins -- The ubiquitin-proteasome pathway -- Proteasome function is linked to ATP hydrolysis -- Proteasomes unfold proteins and translocate them into 20S particles -- Three types of peptidase sites -- Proposed mechanism of proteasome inhibitors -- Therapeutic applications of proteasome inhibitors -- Two systems for protein breakdown function in the two pathways for antigen presentation -- Changes in proteasome subunits induced by interferon -- Steps involved in generating antigenic peptides.…”
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Protein turnover by Waterlow, J. C. (John Conrad)

Subjects: “…Proteins Metabolism.…”
An electronic book accessible through the World Wide Web; click to view

Protein degradation

Table of Contents: “…Contents: Protein levels in cells are regulated by their rates of synthesis and degradation -- Regulatory proteins are rapidly degraded by the ubiquitin-proteasome pathway -- Examples include many oncogenes, transcription factors and cyclins which control progress through the cell cycle -- NF-kappa B activation in disease depends on degradation of the inhibitor, I-kappa B -- Misfolded or mutant proteins are rapidly degraded -- Neurodegenerative and protein folding diseases -- Two major proteolytic pathways exist in mammalian cells -- Many acid hydrolases exist in lysosomes -- Endocytosed proteins and those in autophagic vacuoles are degraded in lysosomes -- The ubiquitin-proteasome pathway -- 3D structure of ubiquitin -- Formation of the isopeptide bonds during ubiquitin conjugation to proteins -- The ubiquitin-proteasome pathway -- Proteasome function is linked to ATP hydrolysis -- Proteasomes unfold proteins and translocate them into 20S particles -- Three types of peptidase sites -- Proposed mechanism of proteasome inhibitors -- Therapeutic applications of proteasome inhibitors -- Two systems for protein breakdown function in the two pathways for antigen presentation -- Changes in proteasome subunits induced by interferon -- Steps involved in generating antigenic peptides.…”
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Biogenesis of cellular iron-sulfur proteins part 1, structure, function, and assembly in mitochondria /

Table of Contents: “…Contents: Structure and functions of iron-sulfur (Fe/S) clusters and proteins -- Analysis of Fe/S proteins and their biogenesis -- Mechanisms of Fe/S protein assembly in mitochondria -- Mitochondrial "Fe/S diseases."…”
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Aging and protein homeostasis

Table of Contents: “…Contents: Aging and protein homeostasis -- What is the role of proteotoxicity in aging? …”
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Series (Autophagy and lysosomal storage diseases)
Series (Aging)

Protein homeostasis in mitochondria chaperones and proteases of the mitochondrial matrix /

Table of Contents: “…Contents: Protein homeostasis in mitochondria: the role of chaperones and proteases -- Principles of mitochondrial protein homeostasis -- Protein quality control in the matrix compartment -- Substrate selectivity of the mitochondrial protease Pim1 -- Proteomic analysis of mitochondrial protein turnover -- Proteome alterations under oxidative stress -- Identification of aggregation-prone polypeptides -- Protective effects of chaperones -- Cooperation of Hsp78 and Pim1 in removal of aggregated polypeptides.…”
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The unfolded protein response

Table of Contents: “…Contents: Molecular mechanism unfolded protein response -- Physiological importance of the unfolded protein response -- Intracellular signaling from the endoplasmic reticulum (ER) to the nucleus -- Reasons for activation -- Maintenance of homeostasis of the ER.…”
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Protein folding in vivo

Table of Contents: “…Contents: Protein folding in vivo -- Protein folding as facilitated by the acid inducible chaperone HdeA -- Optimization of folding in vivo illustrates a tradeoff between stability and function -- The Spy chaperone.…”
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Protein homeostasis in mitochondria AAA+ chaperones & proteases /

Table of Contents: “…Contents: Protein homeostasis in mitochondria -- Mitochondria play an important role in ageing and disease -- Quality control of mitochondria is controlled at three different levels -- Protein quality control (PQC) in mitochondria is maintained by mitochondrial chaperones and AAA+ proteases -- Following proteotoxic stress a specific mitochondrial unfolded protein response (mtUPR) is activated -- The AAA+ protease CLPXP is proposed to play a key role in mtUPR signaling -- A novel mtCLPX interacting protein that modulates the activity of mtCLPXP both in vitro and in vivo has been identified.…”
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Aging and protein homeostasis

Table of Contents: “…Contents: Aging and protein homeostasis -- What is the role of proteotoxicity in aging? …”
Get full text
Series (Autophagy and lysosomal storage diseases)
Series (Aging)

Protein homeostasis in mitochondria chaperones and proteases of the mitochondrial matrix /

Table of Contents: “…Contents: Protein homeostasis in mitochondria: the role of chaperones and proteases -- Principles of mitochondrial protein homeostasis -- Protein quality control in the matrix compartment -- Substrate selectivity of the mitochondrial protease Pim1 -- Proteomic analysis of mitochondrial protein turnover -- Proteome alterations under oxidative stress -- Identification of aggregation-prone polypeptides -- Protective effects of chaperones -- Cooperation of Hsp78 and Pim1 in removal of aggregated polypeptides.…”
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The unfolded protein response

Table of Contents: “…Contents: Molecular mechanism unfolded protein response -- Physiological importance of the unfolded protein response -- Intracellular signaling from the endoplasmic reticulum (ER) to the nucleus -- Reasons for activation -- Maintenance of homeostasis of the ER.…”
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Series

Protein folding in vivo

Table of Contents: “…Contents: Protein folding in vivo -- Protein folding as facilitated by the acid inducible chaperone HdeA -- Optimization of folding in vivo illustrates a tradeoff between stability and function -- The Spy chaperone.…”
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Series

Protein homeostasis in mitochondria AAA+ chaperones & proteases /

Table of Contents: “…Contents: Protein homeostasis in mitochondria -- Mitochondria play an important role in ageing and disease -- Quality control of mitochondria is controlled at three different levels -- Protein quality control (PQC) in mitochondria is maintained by mitochondrial chaperones and AAA+ proteases -- Following proteotoxic stress a specific mitochondrial unfolded protein response (mtUPR) is activated -- The AAA+ protease CLPXP is proposed to play a key role in mtUPR signaling -- A novel mtCLPX interacting protein that modulates the activity of mtCLPXP both in vitro and in vivo has been identified.…”
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Series

Protein homeostasis in mitochondria chaperones and proteases of the mitochondrial matrix /

Table of Contents: “…Contents: Protein homeostasis in mitochondria: the role of chaperones and proteases -- Principles of mitochondrial protein homeostasis -- Protein quality control in the matrix compartment -- Substrate selectivity of the mitochondrial protease Pim1 -- Proteomic analysis of mitochondrial protein turnover -- Proteome alterations under oxidative stress -- Identification of aggregation-prone polypeptides -- Protective effects of chaperones -- Cooperation of Hsp78 and Pim1 in removal of aggregated polypeptides.…”
Get full text
Series

The unfolded protein response

Table of Contents: “…Contents: Molecular mechanism unfolded protein response -- Physiological importance of the unfolded protein response -- Intracellular signaling from the endoplasmic reticulum (ER) to the nucleus -- Reasons for activation -- Maintenance of homeostasis of the ER.…”
Get full text
Series

Protein folding in vivo

Table of Contents: “…Contents: Protein folding in vivo -- Protein folding as facilitated by the acid inducible chaperone HdeA -- Optimization of folding in vivo illustrates a tradeoff between stability and function -- The Spy chaperone.…”
Get full text
Series

Protein homeostasis in mitochondria AAA+ chaperones & proteases /

Table of Contents: “…Contents: Protein homeostasis in mitochondria -- Mitochondria play an important role in ageing and disease -- Quality control of mitochondria is controlled at three different levels -- Protein quality control (PQC) in mitochondria is maintained by mitochondrial chaperones and AAA+ proteases -- Following proteotoxic stress a specific mitochondrial unfolded protein response (mtUPR) is activated -- The AAA+ protease CLPXP is proposed to play a key role in mtUPR signaling -- A novel mtCLPX interacting protein that modulates the activity of mtCLPXP both in vitro and in vivo has been identified.…”
Get full text
Series