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: Despite the wide use of Caenorhabditis elegans as a model organism, the first virus naturally infecting this organism was not discovered until six years ago. The Orsay virus and its related nematode viruses have a positive-sense RNA genome, encoding three proteins: CP, RdRP, and a novel protein that shares no homology with any other proteins. can be expressed either as a free or a CP- fusion protein by ribosomal frameshift, but the structure and function of both and CP- remain unknown. Using a combination of electron microscopy, X-ray crystallography, computational and biophysical analyses, here we show that the Orsay protein forms a~420-A long, pentameric fiber with an N-terminal -helical bundle, a -stranded filament in the middle, and a C-terminal head domain. The pentameric nature of the fiber has been independently confirmed by both mass spectrometry and analytical ultracentrifugation. Recombinant Orsay capsid containing CP- shows protruding long fibers with globular heads at the distal end. Mutant viruses with disrupted CP- fibers were generated by organism-based reverse genetics. These viruses were found to be either non-viable or with poor infectivity according to phenotypic and qRT-PCR analyses. Furthermore, addition of purified proteins to worm culture greatly reduced Orsay infectivity in a sequence-specific manner. Based on the structure resemblance between the Orsay CP- fiber and the fibers from reovirus and adenovirus, we propose that CP- functions as a cell attachment protein to mediate Orsay entry into worm intestine cells. Orsay, the only virus known to naturally infect the nematode Caenorhabditis elegans, expresses a capsid- fusion protein. We have demonstrated that the Orsay fusion protein is incorporated into Orsay capsid and forms a~420-A long fiber protruding from the PLOS Pathogens |
Title: Structure of a pentameric virion-associated fiber with a potential role in Orsay virus entry to host cells
[EX A]: False

[EX Q]: Paragraph: DNA vaccines present one of the most cost-effective platforms to develop global vaccines, which have been tested for nearly three decades in preclinical and clinical settings with some success in the clinic. However, one of the major challenges for the development of DNA vaccines is their poor immunogenicity in humans, which has led to refinements in DNA delivery, dosage in prime/boost regimens and the inclusion of adjuvants to enhance their immunogenicity. In this review, we focus on adjuvants that can enhance the immunogenicity of DNA encoded antigens and highlight the development of a novel cytolytic DNA platform encoding a truncated mouse perforin. The application of this innovative DNA technology has considerable potential in the development of effective vaccines.
Title: vaccines Cytolytic Perforin as an Adjuvant to Enhance the Immunogenicity of DNA Vaccines
[EX A]: True

[EX Q]: Paragraph: study, we present the results of comprehensive bioinformatics analyses of the abundance and roles of intrinsic disorder in 3,411 ribosomal proteins from 32 species. We show that many ribosomal proteins are intrinsically disordered or hybrid proteins that contain ordered and disordered domains. Predicted globular domains of many ribosomal proteins contain noticeable regions of intrinsic disorder. We also show that disorder in ribosomal proteins has different characteristics compared to other proteins that interact with RNa and DNa including overall abundance, evolutionary conservation, and involvement in protein-protein interactions. Furthermore, intrinsic disorder is not only abundant in the ribosomal proteins, but we demonstrate that it is absolutely necessary for their various functions. Abstract Intrinsic disorder (i.e., lack of a unique 3-D structure) is a common phenomenon, and many biologically active proteins are disordered as a whole, or contain long disordered regions. these intrinsically disordered proteins/regions constitute a significant part of all proteomes, and their functional repertoire is complementary to functions of ordered proteins. In fact, intrinsic disorder represents an important driving force for many specific functions. an illustrative example of such disordercentric functional class is RNa-binding proteins. In this Z. Peng and C. J. Oldfield contributed equally to this study. Electronic supplementary material the online version of this article (
Title: A creature with a hundred waggly tails: intrinsically disordered proteins in the ribosome
[EX A]:
False