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".

Input: Consider Input: Paragraph: Pulmonary arterial hypertension (PAH) is a chronic lung disease with poor diagnosis and limited therapeutic options. The currently available therapies are ineffective in improving the quality of life and reducing mortality rates. There exists a clear unmet medical need to treat this disease, which necessitates the discovery of novel therapeutic targets/agents for safe and successful therapy. An altered renin-angiotensin system (RAS) has been implicated as a causative factor in the pathogenesis of PAH. Angiotensin II (Ang II), a key effector peptide of the RAS, can exert deleterious effects on the pulmonary vasculature resulting in vasoconstriction, proliferation, and inflammation, all of which contribute to PAH development. Recently, a new member of the RAS, angiotensin converting enzyme 2 (ACE2), was discovered. This enzyme functions as a negative regulator of the angiotensin system by metabolizing Ang II to a putative protective peptide, angiotensin-(1-7). ACE2 is abundantly expressed in the lung tissue and emerging evidence suggests a beneficial role for this enzyme against lung diseases. In this review, we focus on ACE2 in relation to pulmonary hypertension and provide proof of principle for its therapeutic role in PAH.
Title: ACE2, a promising therapeutic target for pulmonary hypertension

Output: False

Input: Consider Input: Paragraph: Aquaporins are small channel proteins which facilitate the diffusion of water and small neutral molecules across biological membranes. Compared with animals, plant genomes encode numerous aquaporins, which display a large variety of subcellular localization patterns. More specifically, plant aquaporins of the plasma membrane intrinsic protein (PIP) subfamily were first described as plasma membrane (PM)-resident proteins, but recent research has demonstrated that the trafficking and subcellular localization of these proteins are complex and highly regulated. In the past few years, PIPs emerged as new model proteins to study subcellular sorting and membrane dynamics in plant cells. At least two distinct sorting motifs (one cytosolic, the other buried in the membrane) are required to direct PIPs to the PM. Hetero-oligomerization and interaction with SNAREs (soluble N-ethylmaleimide-sensitive factor protein attachment protein receptors) also influence the subcellular trafficking of PIPs. In addition to these constitutive processes, both the progression of PIPs through the secretory pathway and their dynamics at the PM are responsive to changing environmental conditions. The first aquaporins discovered in plants were classified on the basis of their subcellular localization. NIPs (nodulin26-like
Title: Trafficking of Plant Plasma Membrane Aquaporins: Multiple Regulation Levels and Complex Sorting Signals

Output: False

Input: Consider Input: Paragraph: Glycyrrhetic acid polyglycosides were synthesized in one-pot via cationic ring-opening condensation polymerization of cyclic sulfite (4) initiated by glycyrrhetic acid as an aglycon. Sulfite 4 worked as a practical monomer for the preparation of (1 ? 2)-linked polysaccharide skeletons. The chemical stability of 4 was evaluated by the comparison of thermodynamic parameters with those of conventional epoxide (2). The grafting reaction of 4 from glycyrrhetic acid (5) was performed in the presence of TfOH and MS 3A in CH 2 Cl 2 at room temperature. The polymerization degree was moderately controllable by the change of feed ratio of initiator.
Title: One-pot synthesis of glycyrrhetic acid polyglycosides based on grafting-from method using cyclic sulfite
Output: False