In this task, you're given a paragraph and title from the research paper. Your task is to classify whether the given title is suitable or not for the research paper based on the given paragraph. Return "True" if title is proper according to paragraph else "False".

[Q]: Paragraph: Objectives: Cow and calf performance in a semi-confined cow-calf production system was compared with total confinement using summer-born calves. Material and Methods: The experiment was conducted over 3 yr in eastern Nebraska (ENREC) and 2 yr in western Nebraska (PREC) in a randomized complete block design. Lactating, crossbred beef cows (n = 127 at ENREC; n = 56 at PREC) with summer-born calves were used from November to April. Treatments were (1) drylot feeding or (2) cornstalk grazing with supplementation. Dry-lot pairs were limit fed a crop residue and distillersbased diet to meet energy requirements of a lactating cow. A dried distillers grain-based pellet was supplemented to pairs on cornstalks at a rate of 2.4 kg of DM/pair daily. Dry-lot cow-calf pairs were limit fed 12.1 kg of DM/d throughout the trial. Results and Discussion: At ENREC, cows wintered on cornstalks lost BW and had a 0.46-unit decrease in BCS (P < 0.01), whereas cows in the dry-lot gained BW and had a 0.24-unit increase in BCS. At PREC, BCS increased by 0.03 units for cows wintered in the dry-lot and decreased by 0.26 units for cows wintered on cornstalks (P < 0.04). At both locations, calves fed in a dry-lot had greater ADG and BW per day of age compared with calves offered cornstalk grazing with supplementation (P 0.03). Implications and Applications: A partial budget suggests that lower winter production inputs compensate for reduced performance of calves when cow-calf pairs are wintered on cornstalks, making residue grazing a viable option in partial confinement systems.
Title: Performance of cows and summer-born calves and economics in semi-confined and confined beef systems
[A]: False

[Q]: Paragraph: We aimed to test the hypothesis that gene silencing of tumor necrosis factor alpha converting enzyme (TACE) may attenuate lesion inflammation and positive vascular remodeling and enhance plaque stability in a rabbit model of atherosclerosis. Lentivirus-mediated TACE shRNA was injected into the abdominal aortic plaques of rabbits which effectively down-regulated TACE expression and activities from week 8 to week 16. TACE gene silencing reduced remodeling index and plaque burden, and diminished the content of macrophages and lipids while increased that of smooth muscle cells and collagen in the aortic plaques. In addition, TACE gene silencing attenuated the local expression of P65, iNOS, ICAM-1, VEGF and Flt-1 and activities of MMP9 and MMP2 while increased the local expression of TGF-1 together with reduced number of neovessels in the aorta. TACE shRNA treatment resulted in down-regulated expression of TACE in macrophages and blunted ERK-P38 phosphorylation and tube formation of co-cultured mouse vascular smooth muscle cells or human umbilical vein endothelial cells. In conclusion, gene silencing of TACE enhanced plaque stability and improved vascular positive remodeling. The mechanisms may involve attenuated local inflammation, neovascularization and MMP activation, as well as enhanced collagen production probably via down-regulated ERK-NF-B and upregulated TGF-1 signaling pathways. Tumor necrosis factor alpha converting enzyme (TACE), also known as ADAM17 (A disintegrin and A metalloproteinase 17), was initially discovered as a protease that cleaves the 26-kDa precursor of TNF- and sheds transmembrane TNF- to generate a soluble form of TNF- that can bind to TNF- receptors to induce inflammatory response 1 . Recently it has been recognized that TACE is a type I transmembrane protein and a member of a superfamily of Zn dependent metalloproteases. The major physiological role of TACE is to regulate the proteolytic release of a number of growth factors, cytokines, adhesion molecules and cleavage enzymes from cellular membrane 2,3 . The major pro-inflammatory cytokine processed by TACE is TNF- which is produced by macrophages, monocytes and T-cells, and acts as a major player in the pathogenesis of inflammation. It has been increasingly recognized that TACE-mediated shedding is involved in a variety of diseases such as ischemia, heart failure, arthritis, atherosclerosis, diabetes, cancer, neurological and immune diseases 3-5 . Ashley EA et al. provided functional evidence for TACE as a candidate gene of atherosclerosis susceptibility and found that polymorphisms of the TACE genes had relation to cardiovascular mortality in humans 6 . Canault M et al. found that TACE expression was associated with lesion formation in atherosclerosis-prone sites of apolipoprotein E-knockout (ApoE -/-) mice 7 . Oksala N demonstrated that TACE was upregulated in advanced human atherosclerotic lesions in samples from carotid, aortic, and femoral arteries compared to samples from internal thoracic artery free of atherosclerotic plaques 8 . In addition, Stoehr R et al. showed that loss of TIMP3, an endogenous inhibitor of TACE, exacerbated atherosclerosis 1
Title: Gene silencing of TACE enhances plaque stability and improves vascular remodeling in a rabbit model of atherosclerosis
[A]: False

[Q]: Paragraph: Bovine renal brush-border membrane vesicle aminopeptidase N at various stages of purity was treated with two bifunctional cross-linking agents. A pattern of emergence of higher molecular weight forms was observed. By using a cleavable cross-linker, aminopeptidase N was shown to cross-link both to itself and to its breakdown products as well as to dipeptidyl peptidase IV. Using this technique it was possible to identify three of the breakdown products as 45 kDa, 66 kDa and 95 kDa peptides. N-terminal amino acid sequence analysis was used to define the precise cleavage points for the bovine renal aminopeptidase N breakdown products. The short amino acid sequences obtained show strong sequence similarity with the human intestinal and rat kidney aminopeptidase N.
Title: The oligomeric structure of renal aminopeptidase N from bovine brush-border membrane vesicles
[A]:
False