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: Diseases caused by pathogenic microorganisms including bacteria and viruses can cause serious medical issues including death and result in huge economic losses. Despite the myriad of recent advances in the rapid and accurate detection of pathogens, large volume clinical samples with a low concentration of pathogens continue to present challenges for diagnosis and surveillance. We here report a simple and label-free approach via homobifunctional imidoesters (HIs) with a microfluidic platform (SLIM) to efficiently enrich and extract pathogens at low concentrations from clinical samples. The SLIM system consists of an assembled double microfluidic chip for streamlining large volume processing and HIs for capturing pathogens and isolating nucleic acids by both electrostatic and covalent interaction without a chaotropic detergent or bulky instruments. The SLIM system significantly increases the enrichment and extraction rate of pathogens (up to 80% at 10 CFU (colony forming unit) in a 1 mL volume within 50 min). We demonstrated its clinical utility in large sample volumes from 46 clinical specimens including environmental swabs, saliva, and blood plasma. The SLIM system showed higher sensitivity with these samples and could detect pathogens that were below the threshold of detection with other methods. Finally, by combining our SLIM approach with an isothermal optical sensor, pathogens could be detected at a very high sensitivity in blood plasma samples within 80 min via enrichment, extraction and detection steps. Our SLIM system thus provides a simple, reliable, cost-effective and ultrasensitive pathogen diagnosis platform for use with large volume clinical samples and would thus have significant utility for various infectious diseases. 
 Title: Simple and label-free pathogen enrichment via homobifunctional imidoesters using a microfluidic (SLIM) system for ultrasensitive pathogen detection in various clinical specimens

A: True
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Q: Paragraph: The severe acute respiratory syndrome (SARS) pandemic revealed that zoonotic transmission of animal coronaviruses (CoV) to humans poses a significant threat to public health and warrants surveillance and the development of countermeasures. The activity of host cell proteases, which cleave and activate the SARS-CoV spike (S) protein, is essential for viral infectivity and constitutes a target for intervention. However, the identities of the proteases involved have been unclear. Pioneer studies identified cathepsins and type II transmembrane serine proteases as cellular activators of SARS-CoV and demonstrated that several emerging viruses might exploit these enzymes to promote their spread. Here, we will review the proteolytic systems hijacked by SARS-CoV for S protein activation, we will discuss their contribution to viral spread in the host and we will outline antiviral strategies targeting these enzymes. This paper forms part of a series of invited articles in Antiviral Research on ''From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses.'' Ó 
 Title: Proteolytic activation of the SARS-coronavirus spike protein: Cutting enzymes at the cutting edge of antiviral research

A: False
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Q: 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

A:
False
****