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Atrogin-1, A Muscle-Specific F-Box Protein Highly Expressed during Muscle Atrophy

Proceedings of the National Academy of Sciences - PNAS, 2001-12, Vol.98 (25), p.14440-14445

2001

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What do we really know about the ubiquitin-proteasome pathway in muscle atrophy?

Current opinion in clinical nutrition and metabolic care, 2001-05, Vol.4 (3), p.183-190

2001

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Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy

Biochemical Society transactions, 2007-02, Vol.35 (Pt 1), p.12

Goldberg, A L

2007

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Proteolysis, proteasomes and antigen presentation

Nature (London), 1992-06, Vol.357 (6377), p.375-379

1992

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Muscle protein breakdown and the critical role of the ubiquitin-proteasome pathway in normal and disease states

The Journal of nutrition, 1999, Vol.129 (1S), p.227S-237S

1999

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Protein degradation and protection against misfolded or damaged proteins

Nature (London), 2003-12, Vol.426 (6968), p.895-899

Goldberg, Alfred L

2003

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Activation of the ATP-ubiquitin-proteasome pathway in skeletal muscle of cachectic rats bearing a hepatoma

American journal of physiology: endocrinology and metabolism, 1995-05, Vol.268 (5), p.E996-E1006

1995

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Ubiquitin conjugation by the N-end rule pathway and mRNAs for its components increase in muscles of diabetic rats

The Journal of clinical investigation, 1999-11, Vol.104 (10), p.1411-1420

1999

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Proteasomes play an essential role in thymocyte apoptosis

The EMBO journal, 1996-08, Vol.15 (15), p.3835-3844

1996

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PAN, the proteasome-activating nucleotidase from archaebacteria, is a protein-unfolding molecular chaperone

Nature cell biology, 2000-11, Vol.2 (11), p.833-839

2000

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Functions of the Proteasome: The Lysis at the End of the Tunnel

Science (American Association for the Advancement of Science), 1995-04, Vol.268 (5210), p.522-523

Goldberg, Alfred L.

1995

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Rates of Ubiquitin Conjugation Increase when Muscles Atrophy, Largely through Activation of the N-End Rule Pathway

Proceedings of the National Academy of Sciences - PNAS, 1998-10, Vol.95 (21), p.12602-12607

1998

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The N-end Rule Pathway Catalyzes a Major Fraction of the Protein Degradation in Skeletal Muscle

The Journal of biological chemistry, 1998-09, Vol.273 (39), p.25216-25222

1998

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Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting

American journal of physiology: endocrinology and metabolism, 1993-04, Vol.264 (4), p.E668-E676

1993

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Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles

The Journal of clinical investigation, 1997-07, Vol.100 (1), p.197-203

1997

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Increase in levels of polyubiquitin and proteasome mRNA in skeletal muscle during starvation and denervation atrophy

Biochemical journal, 1995-05, Vol.307 ( Pt 3) (3), p.631-637

1995

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Increase in ubiquitin-protein conjugates concomitant with the increase in proteolysis in rat skeletal muscle during starvation and atrophy denervation

Biochemical journal, 1995-05, Vol.307 ( Pt 3) (3), p.639-645

1995

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γ-Interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes

Nature (London), 1993-09, Vol.365 (6443), p.264-267

1993

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Metabolic acidosis stimulates muscle protein degradation by activating the adenosine triphosphate-dependent pathway involving ubiquitin and proteasomes

The Journal of clinical investigation, 1994-05, Vol.93 (5), p.2127-2133

1994

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Cellular Defenses against Unfolded Proteins: A Cell Biologist Thinks about Neurodegenerative Diseases

Neuron, 2001, Vol.29 (1), p.15-32

2001

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

American journal of physiology: endocrinology and metabolism, 2004-10, Vol.287 (4), p.E591-E601

2004

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Puromycin-sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradation

The EMBO journal, 2007-03, Vol.26 (5), p.1385-1396

2007

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The proteasome (multicatalytic protease) is a component of the 1500-kDa proteolytic complex which degrades ubiquitin-conjugated proteins

The Journal of biological chemistry, 1990-03, Vol.265 (9), p.4789-4792

1990

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Peptidase Activities of Proteasomes are Differentially Regulated by the Major Histocompatibility Complex-Encoded Genes for LMP2 and LMP7

Proceedings of the National Academy of Sciences - PNAS, 1994-09, Vol.91 (20), p.9213-9217

1994

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Role of different proteolytic pathways in degradation of muscle protein from streptozotocin-diabetic rats

American journal of physiology: endocrinology and metabolism, 1996-08, Vol.271 (2), p.E340-E347

1996

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Atrogin-1, A Muscle-Specific F-Box Protein Highly Expressed during Muscle Atrophy

What do we really know about the ubiquitin-proteasome pathway in muscle atrophy?

Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy

Proteolysis, proteasomes and antigen presentation

Muscle protein breakdown and the critical role of the ubiquitin-proteasome pathway in normal and disease states

Protein degradation and protection against misfolded or damaged proteins

Activation of the ATP-ubiquitin-proteasome pathway in skeletal muscle of cachectic rats bearing a hepatoma

Ubiquitin conjugation by the N-end rule pathway and mRNAs for its components increase in muscles of diabetic rats

Proteasomes play an essential role in thymocyte apoptosis

PAN, the proteasome-activating nucleotidase from archaebacteria, is a protein-unfolding molecular chaperone

Functions of the Proteasome: The Lysis at the End of the Tunnel

Rates of Ubiquitin Conjugation Increase when Muscles Atrophy, Largely through Activation of the N-End Rule Pathway

The N-end Rule Pathway Catalyzes a Major Fraction of the Protein Degradation in Skeletal Muscle

Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting

Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles

Increase in levels of polyubiquitin and proteasome mRNA in skeletal muscle during starvation and denervation atrophy

Increase in ubiquitin-protein conjugates concomitant with the increase in proteolysis in rat skeletal muscle during starvation and atrophy denervation

γ-Interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes

Metabolic acidosis stimulates muscle protein degradation by activating the adenosine triphosphate-dependent pathway involving ubiquitin and proteasomes

Cellular Defenses against Unfolded Proteins: A Cell Biologist Thinks about Neurodegenerative Diseases

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

Puromycin-sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradation

The proteasome (multicatalytic protease) is a component of the 1500-kDa proteolytic complex which degrades ubiquitin-conjugated proteins

Peptidase Activities of Proteasomes are Differentially Regulated by the Major Histocompatibility Complex-Encoded Genes for LMP2 and LMP7

Role of different proteolytic pathways in degradation of muscle protein from streptozotocin-diabetic rats

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