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".

[EX Q]: Paragraph: A total of 29 faecal samples collected from dogs with diarrhoea following canine parvovirus (CPV) vaccination were tested by minor groove binder (MGB) probe assays for discrimination between CPV vaccine and field strains and by diagnostic tests for detection of other canine pathogens. Fifteen samples tested positive only for CPV field strains; however, both vaccine and field strains were detected in three samples. Eleven samples were found to contain only the vaccine strain, although eight of them tested positive for other pathogens of dogs. Only three samples were found to contain the vaccine strain without evidence of canine pathogens. The present study confirms that most cases of parvovirus-like disease occurring shortly after vaccination are related to infection with field strains of canine parvovirus type 2 (CPV-2) rather than to reversion to virulence of the modified live virus contained in the vaccine. 
 Title: Occurrence of severe gastroenteritis in pups after canine parvovirus vaccine administration: A clinical and laboratory diagnostic dilemma
[EX A]: True

[EX Q]: Paragraph: The synthesis of racemic substituted 7-amino-5,7,8,9-tetrahydrobenzocyclohepten-6-one hydrochlorides was optimized to enhance reproducibility and increase the overall yield. In order to investigate their specificity, series of enzyme inhibition assays were carried out against a diversity of proteases, covering representative members of aspartic, cysteine, metallo and serine endopeptidases and including eight members of the monometallic M1 family of aminopeptidases as well as two members of the bimetallic M17 and M28 aminopeptidase families. This aminobenzosuberone scaffold indeed demonstrated selective inhibition of M1 aminopeptidases to the exclusion of other tested protease families; it was particularly potent against mammalian APN and its bacterial/parasitic orthologues EcPepN and Pf AM1. 
 Title: molecules Aminobenzosuberone Scaffold as a Modular Chemical Tool for the Inhibition of Therapeutically Relevant M1 Aminopeptidases
[EX A]: True

[EX Q]: Paragraph: The ADP-ribosylation factor (ARF) family of low molecular weight guanine-nucleotide-binding (G) proteins controls membrane traffic and organelle structure, and each member is regulated through a cycle of GTP binding and GTP hydrolysis, which activate and inactivate the G protein, respectively 1,2 . ARFs have several important functions, including the recruitment of coat proteins that promote sorting of cargo into vesicles, the recruitment and activation of enzymes, such as the phosphatidylinositol (PtdIns) kinases, that alter membrane lipid composition, and interaction with cytoskeletal factors (TABLE 1) . There are six mammalian ARF proteins that can be divided into three classes based on sequence homology: Class I (ARF1, ARF2 and ARF3), Class II (ARF4 and ARF5) and Class III (ARF6) (FIG. 1) . The Class II ARFs arose late in animal cell evolution, possibly in metazoans, but Class I ARFs are highly conserved and are present in all eukaryotes examined to date. Hence, in Drosophila melanogaster and Caenorhabditis elegans, each class has a single ARF orthologue, but yeast lacks the Class II ARFs. Plants have Class I ARFs, and potentiall y also Class III ARFs (BOX 1). In addition, there are over 20 ARF-like (ARL) proteins, which seem to have broader roles than ARFs. Some ARL proteins, including ARL1, ARL2 and ARF-related protein 1 (ARFRP1), are ancient and have homologues in plants, yeast and metazoans, whereas others, such as ARL11, arose later in evolution and are present only in vertebrates 2 . SAR1, which is present in all eukaryotes examined to date, is also considered to be a member of the ARF family, owing to the presence of an aminotermina l amphipathic helix and the functional similarit y of this protein to ARF1 in recruiting a coat complex durin g vesicle budding. The study of ARF protein function was aided greatly by the early discovery of the regulators of ARF GTP binding and GTP hydrolysis. The ARF guanine nucleotid e exchange factors (GEFs) contain a conserved SEC7 domain that catalyses GDP release from, and GTP binding to, their substrate ARFs. The GTPase -activating proteins (GAPs) catalyse the hydrolysis of GTP-bound ARFs and are critically important because ARFs have negligible intrinsic GTP-hydrolysis activity. ARF GAPs contain a conserved zinc-finger GAP catalytic domain. The conserved, signature catalytic domains in the GEFs and GAPs are what facilitated the identification of these ARF regulators in all organisms from yeast to man. However, the ARF substrate specificity for these GEFs and GAPs remains unclear, and whether they also work on ARL proteins has yet to be determined. In the past, G protein activity was viewed as a linear signalling pathway, with the GDP-bound form being inactive and the GTP-bound form initiating effector functions until it returned to the inactive, GDP-bound state. The GEFs and GAPs were thought of as 'activators' and 'in activators' , respectively, that controlled this on-off switch (FIG. 1c) . However, work on ARF and ARL proteins over the past decade has revealed that their Abstract | Members of the ADP-ribosylation factor (ARF) family of guanine-nucleotidebindin g (G) proteins, including the ARF-like (ARL) proteins and SAR1, regulate membrane traffic and organelle structure by recruiting cargo-sorting coat proteins, modulating membrane lipid composition, and interacting with regulators of other G proteins. New roles of ARF and ARL proteins are emerging, including novel functions at the Golgi complex and in cilia formation. Their function is under tight spatial control, which is mediated by guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs) that catalyse GTP exchange and hydrolysis, respectively. Important advances are being gained in our understanding of the functional networks that are formed not only by the GEFs and GAPs themselves but also by the inactive forms of the ARF proteins. www.nature.com/reviews/molcellbio 
 Title: ARF family G proteins and their regulators: roles in membrane transport, development and disease
[EX A]:
True