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Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression

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Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions

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IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1

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Insulin resistance accelerates muscle protein degradation: Activation of the ubiquitin-proteasome pathway by defects in muscle cell signaling

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Caspase 3 activity is required for skeletal muscle differentiation

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Docking of the Proteasomal ATPases' Carboxyl Termini in the 20S Proteasome's α Ring Opens the Gate for Substrate Entry

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The acidosis of chronic renal failure activates muscle proteolysis in rats by augmenting transcription of genes encoding proteins of the ATP-dependent ubiquitin-proteasome pathway.

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The Axial Channel of the Proteasome Core Particle Is Gated by the Rpt2 ATPase and Controls Both Substrate Entry and Product Release

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The KLHL12–Cullin-3 ubiquitin ligase negatively regulates the Wnt–β-catenin pathway by targeting Dishevelled for degradation

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Muscle wasting in insulinopenic rats results from activation of the ATP-dependent, ubiquitin-proteasome proteolytic pathway by a mechanism including gene transcription.

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Muscle-specific expression of IGF-1 blocks angiotensin II–induced skeletal muscle wasting

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Monitoring Activity and Inhibition of 26S Proteasomes with Fluorogenic Peptide Substrates

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Regulation of Muscle Protein Degradation

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ATP binding to PAN or the 26S ATPases causes association with the 20S proteasome, gate opening, and translocation of unfolded proteins.

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Sepsis is associated with increased mRNAs of the ubiquitin-proteasome proteolytic pathway in human skeletal muscle.

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Chronic Kidney Disease Causes Defects in Signaling through the Insulin Receptor Substrate/Phosphatidylinositol 3-Kinase/Akt Pathway

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Evaluation of signals activating ubiquitin-proteasome proteolysis in a model of muscle wasting

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Relative Structural and Functional Roles of Multiple Deubiquitylating Proteins Associated with Mammalian 26S Proteasome

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Increased mRNA levels for components of the lysosomal, Ca2+-activated, and ATP-ubiquitin-dependent proteolytic pathways in skeletal muscle from head trauma patients.

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Ubiquitinated Proteins Activate the Proteasome by Binding to Usp14/Ubp6, which Causes 20S Gate Opening

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Caspase Activation Inhibits Proteasome Function during Apoptosis

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Activity and Regulation of the Centrosome-associated Proteasome

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Differential Roles of the COOH Termini of AAA Subunits of PA700 (19 S Regulator) in Asymmetric Assembly and Activation of the 26 S Proteasome

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Exercise ameliorates chronic kidney disease–induced defects in muscle protein metabolism and progenitor cell function

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ENaC Degradation in A6 Cells by the Ubiquitin-Proteosome Proteolytic Pathway

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Evidence for Adipose-Muscle Cross Talk: Opposing Regulation of Muscle Proteolysis by Adiponectin and Fatty Acids

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Protein degradation and increased mRNAs encoding proteins of the ubiquitin-proteasome proteolytic pathway in BC3H1 myocytes require an interaction between glucocorticoids and acidification.

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Muscle wasting in disease: molecular mechanisms and promising therapies

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Glucocorticoid-Induced Skeletal Muscle Atrophy

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Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging

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Skeletal Muscle Wasting and Renewal: A Pivotal Role of Myokine IL-6

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Maintenance of muscle mass and load‐induced growth in Muscle <scp>RING</scp> Finger 1 null mice with age

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Regulation of Protein Degradation by Proteasomes in Cancer

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Protein Degradation by the 26S Proteasome System in the Normal and Stressed Myocardium

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Proteasomal and lysosomal protein degradation and heart disease

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Ubiquitin-like Protein FAT10-mediated Proteasome Degradation

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The Proteasome-associated Protein Ecm29 Inhibits Proteasomal ATPase Activity and in Vivo Protein Degradation by the Proteasome

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