Browsing by Author "Goldberg, Alfred"
Now showing items 1-14 of 14
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Development of proteasome inhibitors as research tools and cancer drugs
Goldberg, Alfred L. (The Rockefeller University Press, 2012)The proteasome is the primary site for protein degradation in mammalian cells, and proteasome inhibitors have been invaluable tools in clarifying its cellular functions. The anticancer agent bortezomib inhibits the major ... -
During Muscle Atrophy, Thick, but not Thin, Filament Components are Degraded by MuRF1-Dependent Ubiquitylation
Cohen, Shenhav Orit; Brault, Jeffrey J.; Gygi, Steven P.; Glass, David Jonathan; Valenzuela, David M.; Gartner, Carlos; Latres, Esther; Goldberg, Alfred L. (Rockefeller University Press, 2009)Loss of myofibrillar proteins is a hallmark of atrophying muscle. Expression of muscle RING-finger 1 (MuRF1), a ubiquitin ligase, is markedly induced during atrophy, and MuRF1 deletion attenuates muscle wasting. We generated ... -
Effects of chymostatin and other proteinase inhibitors on protein breakdown and proteolytic activities in muscle
Libby, Peter; Goldberg, Alfred Lewis (Portland Press, 1980)To learn more about the enzymes involved in protein catabolism in skeletal and cardiac muscle and to identify selective inhibitors of this process, we studied the effects of proteinase inhibitors on protein turnover in ... -
The Influence of Skeletal Muscle on Systemic Aging and Lifespan
Demontis, Fabio; Piccirillo, Rosanna; Goldberg, Alfred; Perrimon, Norbert (Wiley, 2013-12)Epidemiological studies in humans suggest that skeletal muscle aging is a risk factor for the development of several age-related diseases such as metabolic syndrome, cancer, Alzheimer’s disease, and Parkinson’s disease. ... -
The Internal Sequence of the Peptide-Substrate Determines Its N-Terminus Trimming by ERAP1
Evnouchidou, Irini; Momburg, Frank; Papakyriakou, Athanasios; Chroni, Angeliki; Leondiadis, Leondios; Chang, Shih-Chung; Goldberg, Alfred L.; Stratikos, Efstratios (Public Library of Science, 2008)Background: Endoplasmic reticulum aminopeptidase 1 (ERAP1) trims N-terminally extended antigenic peptide precursors down to mature antigenic peptides for presentation by major histocompatibility complex (MHC) class I ... -
JunB Transcription Factor Maintains Skeletal Muscle Mass and Promotes Hypertrophy
Raffaello, Anna; Milan, Giulia; Masiero, Eva; Carnio, Silvia; Lee, Dong-Hoon; Lanfranchi, Gerolamo; Goldberg, Alfred L.; Sandri, Marco (The Rockefeller University Press, 2010)The size of skeletal muscle cells is precisely regulated by intracellular signaling networks that determine the balance between overall rates of protein synthesis and degradation. Myofiber growth and protein synthesis are ... -
Mechanisms of Muscle Growth and Atrophy in Mammals and Drosophila
Piccirillo, Rosanna; Demontis, Fabio; Perrimon, Norbert; Goldberg, Alfred (Wiley, 2014-02)The loss of skeletal muscle mass (atrophy) that accompanies disuse and systemic diseases is highly debilitating. Although the pathogenesis of this condition has been primarily studied in mammals, Drosophila is emerging as ... -
Mechanisms of Skeletal Muscle Aging: Insights From Drosophila and Mammalian Models
Demontis, Fabio; Piccirillo, Rosanna; Goldberg, Alfred; Perrimon, Norbert (The Company of Biologists, 2013-11-01)A characteristic feature of aged humans and other mammals is the debilitating, progressive loss of skeletal muscle function and mass that is known as sarcopenia. Age-related muscle dysfunction occurs to an even greater ... -
\(Mycobacterium\) \(tuberculosis\) ClpP1 and ClpP2 Function Together in Protein Degradation and are Required for Viability \(in\) \(vitro\) and During Infection
Unnikrishnan, Meera; Krishnamoorthy, Vidhya; Raju, Ravikiran M.; Rubin, Daniel H. F.; Kandror, Olga; Akopian, Tatos; Goldberg, Alfred L.; Rubin, Eric Joseph (Public Library of Science, 2012)In most bacteria, Clp protease is a conserved, non-essential serine protease that regulates the response to various stresses. Mycobacteria, including \(Mycobacterium\) \(tuberculosis\) (Mtb) and \(Mycobacterium\) \(smegmatis\), ... -
Puromycin-sensitive Aminopeptidase Protects Against Aggregation-prone Proteins via Autophagy
Menzies, Fiona M.; Hourez, Raphael; Imarisio, Sara; Raspe, Marcel; Sadiq, Oana; Chandraratna, Dhia; O'Kane, Cahir; Rock, Kenneth L.; Reits, Eric; Rubinsztein, David C.; Goldberg, Alfred L. (Oxford University Press, 2010)A major function of proteasomes and macroautophagy is to eliminate misfolded potentially toxic proteins. Mammalian proteasomes, however, cannot cleave polyglutamine (polyQ) sequences and seem to release polyQ-rich peptides. ... -
Regulation of autophagy and the ubiquitin–proteasome system by the FoxO transcriptional network during muscle atrophy
Milan, Giulia; Romanello, Vanina; Pescatore, Francesca; Armani, Andrea; Paik, Ji-Hye; Frasson, Laura; Seydel, Anke; Zhao, Jinghui; Abraham, Reimar; Goldberg, Alfred L.; Blaauw, Bert; DePinho, Ronald A.; Sandri, Marco (Nature Pub. Group, 2015)Stresses like low nutrients, systemic inflammation, cancer or infections provoke a catabolic state characterized by enhanced muscle proteolysis and amino acid release to sustain liver gluconeogenesis and tissue protein ... -
Thiostrepton interacts covalently with Rpt subunits of the 19S proteasome and proteasome substrates
Sandu, Cristinel; Chandramouli, Nagaranjan; Glickman, Joseph Fraser; Molina, Henrik; Kuo, Chueh-Ling; Kukushkin, Nikolay; Goldberg, Alfred L; Steller, Hermann (John Wiley & Sons, Ltd, 2015)Here, we report a novel mechanism of proteasome inhibition mediated by Thiostrepton (Thsp), which interacts covalently with Rpt subunits of the 19S proteasome and proteasome substrates. We identified Thsp in a cell-based ... -
Trim32 reduces PI3K–Akt–FoxO signaling in muscle atrophy by promoting plakoglobin–PI3K dissociation
Cohen, Shenhav; Lee, Donghoon; Zhai, Bo; Gygi, Steven P.; Goldberg, Alfred L. (The Rockefeller University Press, 2014)Activation of the PI3K–Akt–FoxO pathway induces cell growth, whereas its inhibition reduces cell survival and, in muscle, causes atrophy. Here, we report a novel mechanism that suppresses PI3K–Akt–FoxO signaling. Although ... -
Ubiquitylation by Trim32 causes coupled loss of desmin, Z-bands, and thin filaments in muscle atrophy
Cohen, Shenhav Orit; Zhai, Bo; Gygi, Steven P.; Goldberg, Alfred L. (The Rockefeller University Press, 2012)During muscle atrophy, myofibrillar proteins are degraded in an ordered process in which MuRF1 catalyzes ubiquitylation of thick filament components (Cohen et al. 2009. J. Cell Biol. http://dx.doi.org/10.1083/jcb.200901052). ...