我一直在寻找这个。我想按照以下方式对JSON文件进行排序：
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{
"title": "Modeling and simulation of bacterial outer membranes and interactions with membrane proteins.",
"link": "https://www.ncbi.nlm.nih.gov/pubmed/28157627?dopt=Abstract",
"description": "
<table border=\"0\" width=\"100%\"><tr><td align=\"left\"><a href=\"https://linkinghub.elsevier.com/retrieve/pii/S0959-440X(17)30003-9\"><img src=\"//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif\" border=\"0\"/></a> </td><td align=\"right\"><a href=\"https://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=Link&LinkName=pubmed_pubmed&from_uid=28157627\">Related Articles</a></td></tr></table>
<p><b>Modeling and simulation of bacterial outer membranes and interactions with membrane proteins.</b></p>
<p>Curr Opin Struct Biol. 2017 Jan 31;43:131-140</p>
<p>Authors: Patel DS, Qi Y, Im W</p>
<p>Abstract<br/>
The outer membrane (OM) of Gram-negative bacteria is composed of phospholipids in the periplasmic leaflet and lipopolysaccharides (LPS) in the external leaflet, along with β-barrel OM proteins (OMPs) and lipidated periplasmic lipoproteins. As a defensive barrier to toxic compounds, an LPS molecule has high antigenic diversity and unique combination of OM-anchored lipid A with core oligosaccharides and O-antigen polysaccharides, creating dynamic protein-LPS and LPS-LPS interactions. Here, we review recent efforts on modeling and simulation of native-like bacterial OMs to explore structures, dynamics, and interactions of different OM components and their roles in transportation of ions, substrates, and antibiotics across the OM and accessibility of monoclonal antibodies (mAbs) to surface epitopes. Simulation studies attempting to provide insight into the structural basis for LPS transport and OMP insertion in the bacterial OM are also highlighted.<br/>
</p><p>PMID: 28157627 [PubMed - as supplied by publisher]</p>
",
"author": " Patel DS, Qi Y, Im W",
"category": "Curr Opin Struct Biol",
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"#text": "PubMed:28157627"
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{
"title": "Refinement of OprH-LPS Interactions by Molecular Simulations.",
"link": "https://www.ncbi.nlm.nih.gov/pubmed/28122220?dopt=Abstract",
"description": "
<table border=\"0\" width=\"100%\"><tr><td align=\"left\"><a href=\"https://linkinghub.elsevier.com/retrieve/pii/S0006-3495(16)34281-3\"><img src=\"//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif\" border=\"0\"/></a> </td><td align=\"right\"><a href=\"https://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=Link&LinkName=pubmed_pubmed&from_uid=28122220\">Related Articles</a></td></tr></table>
<p><b>Refinement of OprH-LPS Interactions by Molecular Simulations.</b></p>
<p>Biophys J. 2017 Jan 24;112(2):346-355</p>
<p>Authors: Lee J, Patel DS, Kucharska I, Tamm LK, Im W</p>
<p>Abstract<br/>
The outer membrane (OM) of Gram-negative bacteria is composed of lipopolysaccharide (LPS) in the outer leaflet and phospholipids in the inner leaflet. The outer membrane protein H (OprH) of Pseudomonas aeruginosa provides an increased stability to the OMs by directly interacting with LPS. Here we report the influence of various P. aeruginosa and, for comparison, Escherichia coli LPS environments on the physical properties of the OMs and OprH using all-atom molecular dynamics simulations. The simulations reveal that although the P. aeruginosa OMs are thinner hydrophobic bilayers than the E. coli OMs, which is expected from the difference in the acyl chain length of their lipid A, this effect is almost imperceptible around OprH due to a dynamically adjusted hydrophobic match between OprH and the OM. The structure and dynamics of the extracellular loops of OprH show distinct behaviors in different LPS environments. Including the O-antigen greatly reduces the flexibility of the OprH loops and increases the interactions between these loops and LPS. Furthermore, our study shows that the interactions between OprH and LPS mainly depend on the secondary structure of OprH and the chemical structure of LPS, resulting in distinctive patterns in different LPS environments.<br/>
</p><p>PMID: 28122220 [PubMed - in process]</p>
",
"author": " Lee J, Patel DS, Kucharska I, Tamm LK, Im W",
"category": "Biophys J",
"guid": {
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"#text": "PubMed:28122220"
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{
"title": "CHARMM-GUI MDFF/xMDFF Utilizer for Molecular Dynamics Flexible Fitting Simulations in Various Environments.",
"link": "https://www.ncbi.nlm.nih.gov/pubmed/27936734?dopt=Abstract",
"description": "
<table border=\"0\" width=\"100%\"><tr><td align=\"left\"><a href=\"https://dx.doi.org/10.1021/acs.jpcb.6b10568\"><img src=\"//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg\" border=\"0\"/></a> </td><td align=\"right\"><a href=\"https://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=Link&LinkName=pubmed_pubmed&from_uid=27936734\">Related Articles</a></td></tr></table>
<p><b>CHARMM-GUI MDFF/xMDFF Utilizer for Molecular Dynamics Flexible Fitting Simulations in Various Environments.</b></p>
<p>J Phys Chem B. 2016 Dec 23;:</p>
<p>Authors: Qi Y, Lee J, Singharoy A, McGreevy R, Schulten K, Im W</p>
<p>Abstract<br/>
X-ray crystallography and cryo-electron microscopy are two popular methods for the structure determination of biological molecules. Atomic structures are derived through the fitting and refinement of an initial model into electron density maps constructed by both experiments. Two computational approaches, MDFF and xMDFF, have been developed to facilitate this process by integrating the experimental data with molecular dynamics simulation. However, the setup of an MDFF/xMDFF simulation requires knowledge of both experimental and computational methods, which is not straightforward for nonexpert users. In addition, sometimes it is desirable to include realistic environments, such as explicit solvent and lipid bilayers during the simulation, which poses another challenge even for expert users. To alleviate these difficulties, we have developed MDFF/xMDFF Utilizer in CHARMM-GUI that helps users to set up an MDFF/xMDFF simulation. The capability of MDFF/xMDFF Utilizer is greatly enhanced by integration with other CHARMM-GUI modules, including protein structure manipulation, a diverse set of lipid types, and all-atom CHARMM and coarse-grained PACE force fields. With this integration, various simulation environments are available for MDFF Utilizer (vacuum, implicit/explicit solvent, and bilayers) and xMDFF Utilizer (vacuum and solution). In this work, three examples are shown to demonstrate the usage of MDFF/xMDFF Utilizer.<br/>
</p><p>PMID: 27936734 [PubMed - as supplied by publisher]</p>
",
"author": " Qi Y, Lee J, Singharoy A, McGreevy R, Schulten K, Im W",
"category": "J Phys Chem B",
"guid": {
"-isPermaLink": "false",
"#text": "PubMed:27936734"
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}
我希望按照“PubMed”号码进行排序：
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"description": "NCBI: db=pubmed; Term=wonpil im",
"language": "en-us",
"docs": "http://blogs.law.harvard.edu/tech/rss",
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"title": "NCBI pubmed",
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"link": "https://www.ncbi.nlm.nih.gov/sites/entrez",
"description": "PubMed comprises more than millions of citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites."
},
"item": [
{
"title": "CHARMM-GUI MDFF/xMDFF Utilizer for Molecular Dynamics Flexible Fitting Simulations in Various Environments.",
"link": "https://www.ncbi.nlm.nih.gov/pubmed/27936734?dopt=Abstract",
"description": "
<table border=\"0\" width=\"100%\"><tr><td align=\"left\"><a href=\"https://dx.doi.org/10.1021/acs.jpcb.6b10568\"><img src=\"//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg\" border=\"0\"/></a> </td><td align=\"right\"><a href=\"https://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=Link&LinkName=pubmed_pubmed&from_uid=27936734\">Related Articles</a></td></tr></table>
<p><b>CHARMM-GUI MDFF/xMDFF Utilizer for Molecular Dynamics Flexible Fitting Simulations in Various Environments.</b></p>
<p>J Phys Chem B. 2016 Dec 23;:</p>
<p>Authors: Qi Y, Lee J, Singharoy A, McGreevy R, Schulten K, Im W</p>
<p>Abstract<br/>
X-ray crystallography and cryo-electron microscopy are two popular methods for the structure determination of biological molecules. Atomic structures are derived through the fitting and refinement of an initial model into electron density maps constructed by both experiments. Two computational approaches, MDFF and xMDFF, have been developed to facilitate this process by integrating the experimental data with molecular dynamics simulation. However, the setup of an MDFF/xMDFF simulation requires knowledge of both experimental and computational methods, which is not straightforward for nonexpert users. In addition, sometimes it is desirable to include realistic environments, such as explicit solvent and lipid bilayers during the simulation, which poses another challenge even for expert users. To alleviate these difficulties, we have developed MDFF/xMDFF Utilizer in CHARMM-GUI that helps users to set up an MDFF/xMDFF simulation. The capability of MDFF/xMDFF Utilizer is greatly enhanced by integration with other CHARMM-GUI modules, including protein structure manipulation, a diverse set of lipid types, and all-atom CHARMM and coarse-grained PACE force fields. With this integration, various simulation environments are available for MDFF Utilizer (vacuum, implicit/explicit solvent, and bilayers) and xMDFF Utilizer (vacuum and solution). In this work, three examples are shown to demonstrate the usage of MDFF/xMDFF Utilizer.<br/>
</p><p>PMID: 27936734 [PubMed - as supplied by publisher]</p>
",
"author": " Qi Y, Lee J, Singharoy A, McGreevy R, Schulten K, Im W",
"category": "J Phys Chem B",
"guid": {
"-isPermaLink": "false",
"#text": "PubMed:27936734"
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{
"title": "Modeling and simulation of bacterial outer membranes and interactions with membrane proteins.",
"link": "https://www.ncbi.nlm.nih.gov/pubmed/28157627?dopt=Abstract",
"description": "
<table border=\"0\" width=\"100%\"><tr><td align=\"left\"><a href=\"https://linkinghub.elsevier.com/retrieve/pii/S0959-440X(17)30003-9\"><img src=\"//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif\" border=\"0\"/></a> </td><td align=\"right\"><a href=\"https://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=Link&LinkName=pubmed_pubmed&from_uid=28157627\">Related Articles</a></td></tr></table>
<p><b>Modeling and simulation of bacterial outer membranes and interactions with membrane proteins.</b></p>
<p>Curr Opin Struct Biol. 2017 Jan 31;43:131-140</p>
<p>Authors: Patel DS, Qi Y, Im W</p>
<p>Abstract<br/>
The outer membrane (OM) of Gram-negative bacteria is composed of phospholipids in the periplasmic leaflet and lipopolysaccharides (LPS) in the external leaflet, along with β-barrel OM proteins (OMPs) and lipidated periplasmic lipoproteins. As a defensive barrier to toxic compounds, an LPS molecule has high antigenic diversity and unique combination of OM-anchored lipid A with core oligosaccharides and O-antigen polysaccharides, creating dynamic protein-LPS and LPS-LPS interactions. Here, we review recent efforts on modeling and simulation of native-like bacterial OMs to explore structures, dynamics, and interactions of different OM components and their roles in transportation of ions, substrates, and antibiotics across the OM and accessibility of monoclonal antibodies (mAbs) to surface epitopes. Simulation studies attempting to provide insight into the structural basis for LPS transport and OMP insertion in the bacterial OM are also highlighted.<br/>
</p><p>PMID: 28157627 [PubMed - as supplied by publisher]</p>
",
"author": " Patel DS, Qi Y, Im W",
"category": "Curr Opin Struct Biol",
"guid": {
"-isPermaLink": "false",
"#text": "PubMed:28157627"
}
},
{
"title": "Refinement of OprH-LPS Interactions by Molecular Simulations.",
"link": "https://www.ncbi.nlm.nih.gov/pubmed/28122220?dopt=Abstract",
"description": "
<table border=\"0\" width=\"100%\"><tr><td align=\"left\"><a href=\"https://linkinghub.elsevier.com/retrieve/pii/S0006-3495(16)34281-3\"><img src=\"//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif\" border=\"0\"/></a> </td><td align=\"right\"><a href=\"https://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=Link&LinkName=pubmed_pubmed&from_uid=28122220\">Related Articles</a></td></tr></table>
<p><b>Refinement of OprH-LPS Interactions by Molecular Simulations.</b></p>
<p>Biophys J. 2017 Jan 24;112(2):346-355</p>
<p>Authors: Lee J, Patel DS, Kucharska I, Tamm LK, Im W</p>
<p>Abstract<br/>
The outer membrane (OM) of Gram-negative bacteria is composed of lipopolysaccharide (LPS) in the outer leaflet and phospholipids in the inner leaflet. The outer membrane protein H (OprH) of Pseudomonas aeruginosa provides an increased stability to the OMs by directly interacting with LPS. Here we report the influence of various P. aeruginosa and, for comparison, Escherichia coli LPS environments on the physical properties of the OMs and OprH using all-atom molecular dynamics simulations. The simulations reveal that although the P. aeruginosa OMs are thinner hydrophobic bilayers than the E. coli OMs, which is expected from the difference in the acyl chain length of their lipid A, this effect is almost imperceptible around OprH due to a dynamically adjusted hydrophobic match between OprH and the OM. The structure and dynamics of the extracellular loops of OprH show distinct behaviors in different LPS environments. Including the O-antigen greatly reduces the flexibility of the OprH loops and increases the interactions between these loops and LPS. Furthermore, our study shows that the interactions between OprH and LPS mainly depend on the secondary structure of OprH and the chemical structure of LPS, resulting in distinctive patterns in different LPS environments.<br/>
</p><p>PMID: 28122220 [PubMed - in process]</p>
",
"author": " Lee J, Patel DS, Kucharska I, Tamm LK, Im W",
"category": "Biophys J",
"guid": {
"-isPermaLink": "false",
"#text": "PubMed:28122220"
}
},
]
}
}
}
根据给定的“#text”进行简单排序：“PubMed：28122220”。如果有人能提供帮助，我将不胜感激。