In this task, you're given a paragraph from the research paper and your task is to generate a suitable title for the research paper based on the given paper. Under 100 words is a good title length.
--------
Question: Muscle wasting is one of the main features of cancer cachexia, a multifactorial syndrome frequently occurring in oncologic patients. The onset of cachexia is associated with reduced tolerance and response to antineoplastic treatments, eventually leading to clinical conditions that are not compatible with survival. Among the mechanisms underlying cachexia, protein and energy dysmetabolism play a major role. In this regard, several potential treatments have been proposed, mainly on the basis of promising results obtained in preclinical models. However, at present, no treatment yet reached validation to be used in the clinical practice, although several drugs are currently tested in clinical trials for their ability to improve muscle metabolism in cancer patients. Along this line, the results obtained in both experimental and clinical studies clearly show that cachexia can be effectively approached by a multidirectional strategy targeting nutrition, inflammation, catabolism, and inactivity at the same time. In the present study, approaches aimed to modulate muscle metabolism in cachexia will be reviewed.

Answer: Modulating Metabolism to Improve Cancer-Induced Muscle Wasting


Question: Bovine viral diarrhea virus (BVDV) is a pestivirus member of the Flaviviridae family, closely related to, and used as a surrogate model for the hepatitis C virus. Its envelope contains the E1 and E2 glycoproteins, disulfide linked into homo-and heterodimers. In this study, we investigate the role of disulfide bond formation in the folding, assembly, and stability of BVDV glycoproteins. We provide molecular evidence that intact disulfide bonds are critical for the acquirement of a stable conformation of E2 monomers. Forcing the E2 glycoproteins to adopt a reduced conformation either co-or post-translationally before assembly into dimers, determines their misfolding and degradation by proteasome. In contrast, dimerization of E2 glycoproteins results in a conformation resistant to reducing agents and degradation. Furthermore, inhibition of the ER-a-mannosidase activity leads to impairment of misfolded E2 degradation, demonstrating the involvement of this enzyme in targeting viral proteins towards proteasomal degradation. Ó

Answer: Role of disulfide bond formation in the folding and assembly of the envelope glycoproteins of a pestivirus


Question: Variation in temperature and R 0 amongst Canadian sites 2 Table S1 . Basic characteristics of sites used in this study 4 Figure S1 . The locations of sites used in the study 5 Figure S2 . Model-estimated R 0 and DD > 0°C using observed daily temperature 5 Figure S3 . Climate classification tree for the sites 6 Figure S4. Daily normal of ANUSPLIN daily maximum temperatures for each cluster 6 Model sensitivity analysis 7 Table S2. The parameters used in sensitivity analysis 9 Fig S5. Local sensitivity analysis 10 Fig S6. Results of global sensitivity analysis 11 Validation of climate model output 11 Table S3 . Basic information about RCM simulations 13 Figure S7 . Mean DD > 0°C for each cluster using observed and model temperature 14 Figure S8. Mean R 0 for each cluster using observed and climate model temperature 14 Mapping R 0 15 Figure S9. Plots of model-estimated R 0 values plotted against DD > 0°C 16 References 17

Answer:
Supplemental Material Estimated Effects of Projected Climate Change on the B asic Reproductive Number of the Lyme Disease Vector Ixodes scapularis