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".

Paragraph: The yeast Kre2p/Mntlp cxl,2-mannosyltransferase is a type II membrane protein with a short cytoplasmic amino terminus, a membrane-spanning region, and a large catalytic luminal domain containing one N-glycosylation site. Anti-Kre2p/Mntlp antibodies identify a 60-kD integral membrane protein that is progressively N-glycosylated in an MNNl-dependent manner. Kre2p/Mntlp is localized in a Golgi compartment that overlaps with that containing the medial-Golgi mannosyltransferase Mnnlp, and distinct from that including the late Golgi protein Kexlp. To determine which regions of Kre2p/Mntlp are required for Golgi localization, Kre2p/Mntlp mutant proteins were assem-bled by substitution of Kre2p domains with equivalent sequences from the vacuolar proteins DPAP B and Pho8p. Chimeric proteins were tested for correct topology, in vitro and in vivo activity, and were localized intracellularly by indirect immunofluorescence. The resuits demonstrate that the NH2-terminal cytoplasmic domain is necessary for correct Kre2p Golgi localization whereas, the membrane-spanning and stem domains are dispensable. However, in a test of targeting sufficiency, the presence of the entire Kre2p cytoplasmic tail, plus the transmembrane domain and a 36-amino acid residue luminal stem region was required to localize a Pho8p reporter protein to the yeast Golgi. T HE Golgi apparatus plays a fundamental role in glycan processing and sorting of newly synthesized proteins in the secretory pathway of eukaryotic cells. The Golgi apparatus of a typical mammalian cell is composed of a polarized stack of membranous saccules that are differentiated into functionally distinct subcompartments. After the addition of core N-linked sugar moieties in the endoplasmic reticulum, glycoproteins proceed through the cis-Golgi network, the cis-, medial-, and transcisternae, and the trans-Golgi network, where further modifications take place. These include the addition of O-linked sugars and the elaboration, in a protein-specific manner, of complex N-linked carbohydrate structures. The Golgi apparatus also constitutes a major organelle responsible for protein trafficking where particular proteins are directed to precise cellular locations. Two specific Golgi subcompartments have been found to be involved in protein sorting. The cis-Golgi network constitutes the site from which many resident ER proteins are retrieved, and the main function of the TGN is to direct glycoproteins exiting the Golgi complex to either the lysosome or the cell surface ( 
 Title: Localization and Targeting of the Saccharomyces cerevisiae Kre2p/Mnt lp oL 1,2-Mannosyltransferase to a medial.Gol Compartment
False

Paragraph: Cryptococcus gattii is a pathogenic environmental yeast that is considered to be emerging in different areas of the world including the Mediterranean Basin. Exposure to infection might be more likely in animals than in human beings, given their closer relationship with the natural habitat of the yeast, vegetation and soil. Thus, animals, and especially pets, can act as indicators of the presence of this yeast in a determined area. Domestic ferrets (Mustela putorius furo) have become common pets in the past 10-20 years. Their natural behavior of sniffing around and going inside narrow spaces makes them prone to contact with decaying organic matter and soil, the substrate for Cryptococcus species. This study describes two cases of cryptococcosis in ferrets in the Iberian Peninsula and Balearic Islands and documents a relationship of ferret cryptococcosis with environmental isolates in the same locations. Here, we emphasize the importance of how an adequate identification and environmental search of the yeast leads to a better understanding of the epidemiology of cryptococcosis and suggests ferrets may act as sentinels for this fungal disease. 
 Title: Ferrets as Sentinels of the Presence of Pathogenic Cryptococcus Species in the Mediterranean Environment
True

Paragraph: The human respiratory coronavirus OC43 was grown on a human rectal tumor cell line and was isotopically labeled with amino acids, glucosamine, and orthophosphate to analyze virion structural proteins. Four major protein species were resolved by electrophoresis and many of their properties were deduced from digestion studies using proteolytic enzymes. The four proteins are: (1) A 190 kDa protein, the presumed peplomeric protein, that was glycosylated and proteolytically cleavable by trypsin into subunits of 110 and 90 kDa. The subunits each represent a different amino acid sequence on the basis of peptide mapping; (2) a 130 kDa protein that was glycosylated and behaved as a disulfide-linked dimer of 65 kDa molecules. It is the apparent virion hemagglutinin on the basis of digestion studies with trypsin, bromelain and pronase; (3) a 55 kDa nucleocapsid protein that was phosphorylated; (4) a 26 kDa matrix protein that was glycosylated. The 190, 130, 55 and 26 kDa species can therefore be designated P, H, N and M, respectively. They exist in molar ratios of 4 : 1 : 33 : 33, and are calculated to be present at the rate of 88, 22, 726, and 726 molecules per virion, respectively. human respiratory coronovirus 0C43, structural proteins 0168-1702/86/$03.50 0 1986 Elsevier Science Publishers B.V. (Biomedical Division) 
 Title: Structural proteins of human respiratory coronavirus 0C43

True