In this task, you're given a paragraph from the research paper and your task is to generate a suitable title for the research paper based on the given paper. Under 100 words is a good title length.

Example Input: We have previously shown that immunotherapy directed against the protein Nogo-A leads to recovery on a skilled forelimb reaching task in rats after sensorimotor cortex stroke, which correlated with axonal and dendritic plasticity. Here we investigated anti-Nogo-A immunotherapy as an intervention to improve performance on a spatial memory task in aged rats after stroke, and whether cognitive recovery was correlated with structural plasticity. Aged rats underwent a unilateral distal permanent middle cerebral artery occlusion and one week later were treated with an anti-Nogo-A or control antibody. Nine weeks post-stroke, treated rats and normal aged rats were tested on the Morris water maze task. Following testing rats were sacrificed and brains processed for the Golgi-Cox method. Hippocampal CA3 and CA1 pyramidal and dentate gyrus granule cells were examined for dendritic length and number of branch segments, and CA3 and CA1 pyramidal cells were examined for spine density and morphology. Anti-Nogo-A immunotherapy given one week following stroke in aged rats improved performance on the reference memory portion of the Morris water maze task. However, this improved performance was not correlated with structural changes in the hippocampal neurons examined. Our finding of improved performance on the Morris water maze in aged rats after stroke and treatment with anti-Nogo-A immunotherapy demonstrates the promising therapeutic potential for anti-Nogo-A immunotherapy to treat cognitive deficits after stroke. The identification of sites of axonal and dendritic plasticity in the aged brain after stroke and treatment with anti-Nogo-A immunotherapy is still under investigation.
Example Output: Corresponding Author) Research Service 151 Building 1 Hines VA Hospital 5000 S. Fifth Avenue Hines, IL, USA Behav Brain Res

Example Input: This experiment was conducted to evaluate whether pretreatment with fenofibrate could mitigate acute lung injury (ALI) in a mice model of intestinal ischemia/reperfusion (I/R). Male C57BL/6 mice were randomly assigned into three groups (n = 6): sham, intestinal I/R + vehicle, and intestinal I/R + fenofibrate. Intestinal I/R was achieved by clamping the superior mesenteric artery. Fenofibrate (100 mg/kg) or equal volume of vehicle was injected intraperitoneally 60 minutes before the ischemia. At the end of experiment, measurement of pathohistological score, inflammatory mediators and other markers were performed. In addition, a 24-hour survival experiment was conducted in intestinal I/R mice treated with fenofibrate or vehicle. The chief results were as anticipated. Pathohistological evaluation indicated that fenofibrate ameliorated the local intestine damage and distant lung injury. Pretreatment with fenofibrate significantly decreased inflammatory factors in both the intestine and the lung. Consistently, renal creatine levels and hepatic ALT levels were significantly decreased in the fenofibrate group. Moreover, serum systemic inflammatory response indicators were significantly alleviated in the fenofibrate group. In addition, fenofibrate administration significantly improved the survival rate. Collectively, our data indicated that pretreatment with fenofibrate prior to ischemia attenuated intestinal I/R injury and ALI. Acute lung injury (ALI) is a critically severe, life-threatening condition in ICU, characterized by high mortality of approximately 40% 1 . ALI, along with its more severe form, acute respiratory distress syndrome, often results from a massive insult to the lung, whether be the direct alveolar infiltration or the indirect effects of systemic inflammatory response syndrome or multiple organ dysfunction syndromes 2 . An effective treatment of this life-threatening disorder calls for a better understanding of the molecular pathophysiology of ALI. The intestine is recognized to be one of the largest immune barrier systems and to be the source of bacteria and endotoxins in the body 3 . Previous reports indicate that the intestinal organ plays a crucial role in the development of ALI 4 . Mesenteric artery ischemia, a commonly seen critical state during small bowel transplantation or trauma, may lead to intestinal ischemia/reperfusion (I/R) injury. During the process of intestinal I/R injury, local bacteria overgrow and translocate, gastrointestinal mobility decreases, and mucosal permeability increases, all of which subsequently lead to the local intestine damage or distant lung injuries through the activation of systemic inflammatory response syndrome or multiple organ dysfunction syndromes 5,6 . Intestinal I/R is, therefore, a useful model for the investigation of pathophysiological mechanism of indirect ALI. Fenofibrate is known as an agonist of the peroxisome proliferator-activated receptor -α (PPARα ), the nuclear receptor superfamily member 7 . As a nuclear receptor activator, fenofibrate up-regulates or down-regulates genes that are involved in many pathophysiological processes, such as oxidative stress, inflammation, and leukocyte endothelium interactions 8, 9 . Recent studies have demonstrated an anti-oxidant, anti-inflammatory, and anti-ischemic role of fenofibrate to attenuate I/R injury in kidney 10,11 , liver 12 , brain 13,14 and heart 15 . But to date there are no literatures reporting the protective effects of fenofibrate in I/R injury in the organ of intestine. Moreover, the functional significance of fenofibrate in the intestinal I/R-induced ALI remains unclear. Therefore, this experiment is aimed to investigate whether fenofibrate administration would ameliorate the lung injury and inflammation in the model of intestinal I/R injury. Animals. The male C57BL/6 mice (8-10-wk-old; 20 ± 2 g) were purchased from Charles River (Beijing, China). Mice were kept in a temperature (21 ± 2 °C) and humidity (60 ± 5%) controlled room on a 12-hour light/dark cycle. They were fed a standard mice chow and water ad liblitum. All experiments were performed in accordance with the Declaration of Helsinki and were approved by the Institutional Animal Ethical Committee of the Peking Union Medical College Hospital.
Example Output: Protective effects of fenofibrate against acute lung injury induced by intestinal ischemia/reperfusion in mice OPEN

Example Input: Zika virus (ZIKV) is a global public health issue due to its association with severe developmental disorders in infants and neurological disorders in adults. ZIKV uses glycosylation of its envelope (E) protein to interact with host cell receptors to facilitate entry; these interactions could also be important for designing therapeutics and vaccines. Due to a lack of proper information about Asn-linked (N-glycans) on ZIKV E, we analyzed ZIKV E of various strains derived from different cells. We found ZIKV E proteins being extensively modified with oligomannose, hybrid and complex N-glycans of a highly heterogeneous nature. Host cell surface glycans correlated strongly with the glycomic features of ZIKV E. Mechanistically, we observed that ZIKV N-glycans might play a role in viral pathogenesis, as mannose-specific C-type lectins DC-SIGN and L-SIGN mediate host cell entry of ZIKV. Our findings represent the first detailed mapping of N-glycans on ZIKV E of various strains and their functional significance. well as a significant increase in severe fetal abnormalities, including spontaneous abortion, stillbirth, hydrocephaly, microcephaly, hydranencephaly/hydrops fetalis, and placental insufficiency [10] [11] [12] [13] [14] . ZIKV is a small, enveloped positive-strand RNA virus [15] . The genomic RNA of this mosquito-borne flavivirus contains a single open reading frame (ORF) that encodes a polyprotein [16, 17] . This polyprotein undergoes co-and post-translational processing to produce three structural proteins, which are capsid (C), pre-membrane (prM), and envelope (E), in addition to seven non-structural proteins (NS1, NS2A, NS2B, NS3, NS4A, NS4B, and NS5) [17, 18] . Of the three structural proteins, E is the major surface glycoprotein, containing three domains (I, II, III) and two transmembrane helices [17] [18] [19] . The majority of flavivirus E proteins upon post-translational modification are modified by N-glycans at amino acid 153/154 within a highly conserved glycosylation motif of N-X-T/S at positions 154-156 (where X is any amino acid except proline) [16] . This is a primary target of neutralizing antibodies and is required for virus entry [20] . Previously, it was demonstrated that the N-linked glycosylation sites on the E protein of flaviviruses are highly conserved, playing a vital role in both infectivity and assembly [16, [21] [22] [23] . Loss of N-glycosylation motif on domain I of E protein (N154) results in impaired expression and secretion of E ectodomain from mammalian cells [24, 25] . Furthermore, studies in mice have shown that ZIKVs lacking the N-glycans of the ZIKV E were severely compromised for their ability to cause mortality and neuroinvasion, suggesting a vital role for these glycans of the E protein in ZIKV pathogenesis [22, 26] . In this study, we utilized mass spectrometry (MS) and a lectin microarray to analyze the structures and composition of glycans on ZIKV E protein from different strains and on the surface of the virus-producing cells, as well as to explore mosquito-human mode of ZIKV transmission and its association to neurological disorders. Importantly, our functional studies show that these N-glycans of the ZIKV envelope glycoprotein are important in viral infection of cells. Our findings might have implications in understanding the roles for these glycan patterns on ZIKV E in virus-host interaction and pathogenic potential. Results In order to understand ZIKV E protein-associated N-glycans, we initially looked for the characteristic features of the envelope protein(s). After generating alignments of the available ZIKV strains of Asian and African origin on the sequences retrieved from GenBank, the sequences were checked by phylogenetic tree (neighbour-joining tree without distance corrections), followed by NetNglyc analysis. This analysis was performed to better understand the variations in sequences and number of N-Glycosylation sites (Asn-Xaa-Ser/Thr, where X is any amino acid except proline) between Asian strains (PRVABC59 and FLR isolates), African strains (MR766 and IbH isolates), and a Brazilian isolate from 2016 (SJRP) (Figure 1 ). Taken together, these analyses indicate that the number and conservation of glycosylation sites vary across different strains. Asian strains (PRVABC59 and FLR isolates) and the Brazilian isolate (BR_SJRP1840) contain five potential N-linked glycosylation sites, whereas the African strain MR766 isolate contains four and IbH isolate contains three potential N-linked glycosylation sites. However, phylogenetic tree analysis clearly indicates that the Brazilian isolate (BR_SJRP1840) clusters distinctly from Asian and African strains, denoting differences in the envelope proteins sequences. (B) A phylogenetic tree (neighbour-joining tree without distance corrections) constructed based on the multiple sequence alignments of glycoprotein E from different ZIKV strains. Consensus sequences for N-linked glycosylation are highlighted in the square box. (C) The NetNglyc server was used to examine the sequence context of N-glycosylation sites (Asn-Xaa-Ser/Thr) in E proteins, and we depict the N-glycosylation sites at the individual ZIKV E protein sequence sites. +++ N-glycosylation sites very likely to be glycosylated.
Example Output:
Glycosylation of Zika Virus is Important in Host-Virus Interaction and Pathogenic Potential