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RISS 인기검색어
- 검색키워드
- 저자 : Velankar, Sameer (검색결과 3 건)
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Lensink, Marc F.,Velankar, Sameer,Kryshtafovych, Andriy,Huang, Shen‐,You,Schneidman‐,Duhovny, Dina,Sali, Andrej,Segura, Joan,Fernandez‐,Fuentes, Narcis,Viswanath, Shruthi,Elber, Ron John Wiley and Sons Inc. 2016 Proteins Vol.84 No.-
<P><B>ABSTRACT</B></P><P>We present the results for CAPRI Round 30, the first joint CASP‐CAPRI experiment, which brought together experts from the protein structure prediction and protein–protein docking communities. The Round comprised 25 targets from amongst those submitted for the CASP11 prediction experiment of 2014. The targets included mostly homodimers, a few homotetramers, and two heterodimers, and comprised protein chains that could readily be modeled using templates from the Protein Data Bank. On average 24 CAPRI groups and 7 CASP groups submitted docking predictions for each target, and 12 CAPRI groups per target participated in the CAPRI scoring experiment. In total more than 9500 models were assessed against the 3D structures of the corresponding target complexes. Results show that the prediction of homodimer assemblies by homology modeling techniques and docking calculations is quite successful for targets featuring large enough subunit interfaces to represent stable associations. Targets with ambiguous or inaccurate oligomeric state assignments, often featuring crystal contact‐sized interfaces, represented a confounding factor. For those, a much poorer prediction performance was achieved, while nonetheless often providing helpful clues on the correct oligomeric state of the protein. The prediction performance was very poor for genuine tetrameric targets, where the inaccuracy of the homology‐built subunit models and the smaller pair‐wise interfaces severely limited the ability to derive the correct assembly mode. Our analysis also shows that docking procedures tend to perform better than standard homology modeling techniques and that highly accurate models of the protein components are not always required to identify their association modes with acceptable accuracy. Proteins 2016; 84(Suppl 1):323–348. © 2016 The Authors Proteins: Structure, Function, and Bioinformatics Published by Wiley Periodicals, Inc.</P>
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Computed Tomography and Anatomical Findings Encountered During Revision Endoscopic Sinus Surgery
Akanksha Ajay Saberwal,Haritosh Velankar,Yogesh Dabholkar,Adip K Shetty,Sharad Bhalekar,Devayani Shinde 대한비과학회 2020 Journal of rhinology Vol.27 No.2
Background and Objectives: Functional endoscopic sinus surgery (FESS) is a well-established strategy for the treatment of rhinosinusitis. However, some patients do not respond to primary surgery and may require revision surgery. Anatomic alterations due to prior sinus surgery, scarring and adhesions as well as associated chronic mucosal inflammation can make revision procedures challenging. In order to shed more light on the difficulties faced by surgeons performing revision FESS, a study was performed to identify areas of recurrent disease on computed tomography in patients undergoing revision surgery, as well as to evaluate intraoperative findings during revision FESS.Materials and Method: A hospital-based, interventional, non-randomized study was undertaken in 40 patients who underwent revision FESS. Multiple clinical parameters were recorded including number and type of previous surgeries, latest CT scans of the nose and paranasal sinuses, as well as intraoperative findings.Results: Our findings demonstrated the diffuse nature of mucosal disease on CT in our patient population. Fibrosis and adhesion formation were the most common intraoperative findings on revision sinus surgery along with residual air cells, polypoid mucosal regrowth, and middle meatal antrostomy stenosis.Conclusion: A careful evaluation of the patient is needed while contemplating revision surgery. A recent high-resolution CT scan is of paramount importance. The most common areas of disease recurrence are the ostiomeatal complex and residual ethmoids, and these areas should be given careful attention.
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Blind prediction of homo‐ and hetero‐protein complexes: The CASP13‐CAPRI experiment
Lensink, Marc F.,Brysbaert, Guillaume,Nadzirin, Nurul,Velankar, Sameer,Chaleil, Raphaë,l A. G.,Gerguri, Tereza,Bates, Paul A.,Laine, Elodie,Carbone, Alessandra,Grudinin, Sergei,Kong, Ren,Liu, Ran& John WileySons, Inc. 2019 Proteins Vol.87 No.12
<P><B>Abstract</B></P><P>We present the results for CAPRI Round 46, the third joint CASP‐CAPRI protein assembly prediction challenge. The Round comprised a total of 20 targets including 14 homo‐oligomers and 6 heterocomplexes. Eight of the homo‐oligomer targets and one heterodimer comprised proteins that could be readily modeled using templates from the Protein Data Bank, often available for the full assembly. The remaining 11 targets comprised 5 homodimers, 3 heterodimers, and two higher‐order assemblies. These were more difficult to model, as their prediction mainly involved “ab‐initio” docking of subunit models derived from distantly related templates. A total of ~30 CAPRI groups, including 9 automatic servers, submitted on average ~2000 models per target. About 17 groups participated in the CAPRI scoring rounds, offered for most targets, submitting ~170 models per target. The prediction performance, measured by the fraction of models of acceptable quality or higher submitted across all predictors groups, was very good to excellent for the nine easy targets. Poorer performance was achieved by predictors for the 11 difficult targets, with medium and high quality models submitted for only 3 of these targets. A similar performance “gap” was displayed by scorer groups, highlighting yet again the unmet challenge of modeling the conformational changes of the protein components that occur upon binding or that must be accounted for in template‐based modeling. Our analysis also indicates that residues in binding interfaces were less well predicted in this set of targets than in previous Rounds, providing useful insights for directions of future improvements.</P>
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