ReviewMolecular biology reports1999
Adaptation of the ubiquitin-proteasome proteolytic pathway in cancer cachexia.
Review in Molecular biology reports, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
12 citing papers in PubMed.
- The canonical ER stress IRE1α/XBP1 pathway mediates skeletal muscle wasting during pancreatic cancer cachexia.EMBO molecular medicine · 2025Article
- Muscle alterations in the development and progression of cancer-induced muscle atrophy: a review.Journal of applied physiology (Bethesda, Md. : 1985) · 2020Review
- mTOR and Tumor Cachexia.International journal of molecular sciences · 2018Review
- Molecular pathways leading to loss of skeletal muscle mass in cancer cachexia--can findings from animal models be translated to humans?BMC cancer · 2016Review
- Effects of celecoxib and ibuprofen on metabolic disorders induced by Walker-256 tumor in rats.Molecular and cellular biochemistry · 2015Article
- Prophylactic effects of swimming exercise on autophagy-induced muscle atrophy in diabetic rats.Laboratory animal research · 2012Article
- Molecular events and signalling pathways involved in skeletal muscle disuse-induced atrophy and the impact of countermeasures.Journal of cellular and molecular medicine · 2009Review
- Induction of proteasome expression in skeletal muscle is attenuated by inhibitors of NF-kappaB activation.British journal of cancer · 2004Article
- Torbafylline (HWA 448) inhibits enhanced skeletal muscle ubiquitin-proteasome-dependent proteolysis in cancer and septic rats.The Biochemical journal · 2002Article
- Elongated conformers of charge states +11 to +15 of bovine ubiquitin studied using ESI-FAIMS-MS.Journal of the American Society for Mass Spectrometry · 2001Article
- Amino acid regulation of gene expression.The Biochemical journal · 2000Review
- Manipulation of the ubiquitin-proteasome pathway in cachexia: pentoxifylline suppresses the activation of 20S and 26S proteasomes in muscles from tumor-bearing rats.Molecular biology reports · 1999Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ubiquitin-proteasome proteolytic pathway is of major importance in the breakdown of skeletal muscle proteins. The first step in this pathway is the covalent attachment of polyubiquitin chains to the targeted protein. Polyubiquitinylated proteins are then recognized and degraded by the 26S proteasome complex. In this review, we critically analyze recent findings in the regulation of ubiquitinylation of protein substrates and of their subsequent proteasome-dependent degradation in animal models of cancer cachexia. In particular, we discuss the influence of various mediators (anorexia, hormones, prostaglandins, cytokines, and proteolysis-inducing factor) in signaling the activation of ubiquitin-proteasome proteolysis in skeletal muscle. These findings have lead to new concepts that are starting to be used for preventing cachexia in cancer and other wasting diseases.
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10363651What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.