none

碩士 === 國立中央大學 === 資訊工程學系 === 107 === Lysine malonylation is one of the newly recognized post-translational modification (PTMs), it is involved in many biological functions, such as cellular regulation, disease processes and carbon fixation. For better understanding the mechanisms of malonylation, id...

Full description

Bibliographic Details
Main Authors: Ya-Ping Chang, 張雅萍
Other Authors: Jorng-Tzong Horng
Format: Others
Language:en_US
Published: 2019
Online Access:http://ndltd.ncl.edu.tw/handle/pta4x4
id ndltd-TW-107NCU05392052
record_format oai_dc
spelling ndltd-TW-107NCU053920522019-10-22T05:28:10Z http://ndltd.ncl.edu.tw/handle/pta4x4 none 蛋白質賴氨酸丙二酰化修飾作用位點之預測系統 Ya-Ping Chang 張雅萍 碩士 國立中央大學 資訊工程學系 107 Lysine malonylation is one of the newly recognized post-translational modification (PTMs), it is involved in many biological functions, such as cellular regulation, disease processes and carbon fixation. For better understanding the mechanisms of malonylation, identifying malonylation sites is an essential process. Traditionally, their identifications mainly rely on the mass spectrometry and biological experiments, which is time-consuming, labor-intensive and expensive. Recently, some studies have proposed computational approaches to predict malonylation sites in mammalian proteins. However, there has no predictor for malonylation sites in plant proteins. In this study, we developed two deep learning-based frameworks for identifying malonylation sites in mammalian and plant proteins separately. Physicochemical properties, evolutionary information and sequenced-based features were extracted for training the perdition models. We utilized hybrid deep learning models to predict the malonylation sites. The independent testing results for mammalian and plant proteins achieved an area under the receiver operating characteristic curve (AUC) value of 0.943 and 0.772 respectively. Furthermore, the prediction models are freely available as an online server —named Kmalo at http://fdblab.csie.ncu.edu.tw/Kmalo/. Jorng-Tzong Horng Li-Ching Wu 洪炯宗 吳立青 2019 學位論文 ; thesis 46 en_US
collection NDLTD
language en_US
format Others
sources NDLTD
description 碩士 === 國立中央大學 === 資訊工程學系 === 107 === Lysine malonylation is one of the newly recognized post-translational modification (PTMs), it is involved in many biological functions, such as cellular regulation, disease processes and carbon fixation. For better understanding the mechanisms of malonylation, identifying malonylation sites is an essential process. Traditionally, their identifications mainly rely on the mass spectrometry and biological experiments, which is time-consuming, labor-intensive and expensive. Recently, some studies have proposed computational approaches to predict malonylation sites in mammalian proteins. However, there has no predictor for malonylation sites in plant proteins. In this study, we developed two deep learning-based frameworks for identifying malonylation sites in mammalian and plant proteins separately. Physicochemical properties, evolutionary information and sequenced-based features were extracted for training the perdition models. We utilized hybrid deep learning models to predict the malonylation sites. The independent testing results for mammalian and plant proteins achieved an area under the receiver operating characteristic curve (AUC) value of 0.943 and 0.772 respectively. Furthermore, the prediction models are freely available as an online server —named Kmalo at http://fdblab.csie.ncu.edu.tw/Kmalo/.
author2 Jorng-Tzong Horng
author_facet Jorng-Tzong Horng
Ya-Ping Chang
張雅萍
author Ya-Ping Chang
張雅萍
spellingShingle Ya-Ping Chang
張雅萍
none
author_sort Ya-Ping Chang
title none
title_short none
title_full none
title_fullStr none
title_full_unstemmed none
title_sort none
publishDate 2019
url http://ndltd.ncl.edu.tw/handle/pta4x4
work_keys_str_mv AT yapingchang none
AT zhāngyǎpíng none
AT yapingchang dànbáizhìlàiānsuānbǐngèrxiānhuàxiūshìzuòyòngwèidiǎnzhīyùcèxìtǒng
AT zhāngyǎpíng dànbáizhìlàiānsuānbǐngèrxiānhuàxiūshìzuòyòngwèidiǎnzhīyùcèxìtǒng
_version_ 1719273877528379392