instruction:
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".
question:
Paragraph: Translational stalling of ribosome bound to endoplasmic reticulum (ER) membrane requires an accurate clearance of the associated polypeptides, which is not completely understood in mammals. We characterized in mammalian cells the model of ribosomal stalling at the STOP-codon based on proteins tagged at the C-terminus with the picornavirus 2A peptide followed by a termination codon instead of the Proline (2A*). We exploited the 2A* stalling model to characterize the pathway of degradation of ER-targeted polypeptides. We report that the ER chaperone BiP/GRP78 is a new main factor involved. Moreover, degradation of the ER-stalled polypeptides required the activities of the AAA-ATPase VCP/p97, its associated deubiquitinylase YOD1, the ribosome-associated ubiquitin ligase Listerin and the proteasome. In human proteome, we found two human C-terminal amino acid sequences that cause similar stalling at the STOP-codon. Our data suggest that translational stalling at the ER membrane activates protein degradation at the interface of ribosomal-and ERassociated quality control systems. 
 Title: BiP/GRP78 Mediates ERAD Targeting of Proteins Produced by Membrane-Bound Ribosomes Stalled at the STOP-Codon
answer:
False


question:
Paragraph: The 3C-like (3CL) protease of the severe acute respiratory syndrome (SARS) coronavirus is a key enzyme for the virus maturation. We found for the first time that the mature SARS 3CL protease is subject to degradation at 188Arg/189Gln. Replacing Arg with Ile at position 188 rendered the protease resistant to proteolysis. The R188I mutant digested a conserved undecapeptide substrate with a K m of 33.8 lM and k cat of 4753 s À1 . Compared with the value reported for the mature protease containing a C-terminal His-tag, the relative activity of the mutant was nearly 10 6 . Novel peptide-aldehyde derivatives containing a sidechain-protected C-terminal Gln efficiently inhibited the catalytic activity of the R188I mutant. The results indicated for the first time that the tetrapeptide sequence is enough for inhibitory activities of peptidealdehyde derivatives. 
 Title: Evaluation of peptide-aldehyde inhibitors using R188I mutant of SARS 3CL protease as a proteolysis-resistant mutant
answer:
True


question:
Paragraph: Severe Acute Respiratory Syndrome (SARS) has become a new worldwide epidemic whose origin was until recently unknown. It is the unpredictable nature of this epidemic that makes people want answers to some important questions about what they can do to protect themselves. This study presents an inquiry into people's knowledge and self-reported changes in behavior in response to the epidemic. Respondents were drawn from seven major occupational groups in the large central city of Wuhan. Although most respondents knew of SARS, there was still 8.4% who did not know about it. Knowledge was lowest among farmers who had come to the city for temporary work. Most respondents took action to avoid being infected by SARS, including, most commonly, efforts to improve indoor ventilation, to disinfect the indoor environment and to increase handwashing frequency. Self-reported increases in hand-washing frequency were significant; however, among the seven occupational groups, reports of increased hand-washing were consistently greater among commercial service workers, students and farmers. While it seems that possible fears induced by the epidemic led to these changes, there are still about one-third of respondents who do not wash their hands as frequently as desired. There is also the challenge of devising strategies for maintaining the desired frequency of hand-washing among those who did change. 
 Title: Severe Acute Respiratory Syndrome epidemic and change of people's health behavior in China
answer:

False