Zobrazeno 1 - 10
of 153
pro vyhledávání: '"Sheng-You Huang"'
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-16 (2023)
Abstract Membrane proteins are encoded by approximately a quarter of human genes. Inter-chain residue-residue contact information is important for structure prediction of membrane protein complexes and valuable for understanding their molecular mecha
Externí odkaz:
https://doaj.org/article/6b7b18a75fbe49d8bc80fb490e808ce0
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-16 (2023)
Abstract Cryo-EM has emerged as the most important technique for structure determination of macromolecular complexes. However, raw cryo-EM maps often exhibit loss of contrast at high resolution and heterogeneity over the entire map. As such, various
Externí odkaz:
https://doaj.org/article/45a57828e52a4c1886b07be0a6322d6e
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-16 (2022)
One challenge in cryo-EM is to build atomic models into intermediate resolution maps. Here, the authors present a deep learning-guided iterative assembling method by integrating AlphaFold, FFTbased fitting, and domain-based refinement.
Externí odkaz:
https://doaj.org/article/eedb71d516ff4604a333ce0257fc5313
Publikováno v:
Journal of Cheminformatics, Vol 14, Iss 1, Pp 1-12 (2022)
Abstract Cyclic peptides formed by disulfide bonds have been one large group of common drug candidates in drug development. Structural information of a peptide is essential to understand its interaction with its target. However, due to the high flexi
Externí odkaz:
https://doaj.org/article/01ed3463d6eb40d9897f76c4231b9ac3
Autor:
Yumeng Yan, Sheng-You Huang
Publikováno v:
BMC Bioinformatics, Vol 20, Iss S25, Pp 1-10 (2019)
Abstract Background Protein-protein docking is a valuable computational approach for investigating protein-protein interactions. Shape complementarity is the most basic component of a scoring function and plays an important role in protein-protein do
Externí odkaz:
https://doaj.org/article/2f3055473e9a4e78ba75438a98d6de9a
Autor:
Yumeng Yan, Sheng-You Huang
Publikováno v:
Big Data Mining and Analytics, Vol 2, Iss 2, Pp 92-99 (2019)
Symmetric proteins play important roles in many biological processes, such as signal transduction and molecular transportation. Therefore, determining the symmetric oligomeric structure of subunits is crucial to investigate the molecular mechanism of
Externí odkaz:
https://doaj.org/article/ba758297450e4d759620b4e8d7fe450f
Publikováno v:
Journal of Cheminformatics, Vol 9, Iss 1, Pp 1-13 (2017)
Abstract Conformation generation of protein-bound peptides is critical for the determination of protein–peptide complex structures. Despite significant progress in conformer generation of small molecules, few methods have been developed for modelin
Externí odkaz:
https://doaj.org/article/fe9aaa06717c42488efd371bedd0f62d
Publikováno v:
Viruses, Vol 12, Iss 4, p 428 (2020)
The outbreak of a novel coronavirus, which was later formally named the severe acute respiratory coronavirus 2 (SARS-CoV-2), has caused a worldwide public health crisis. Previous studies showed that SARS-CoV-2 is highly homologous to SARS-CoV and inf
Externí odkaz:
https://doaj.org/article/efaef2e268da4dbe99acd4e72298691e
Publikováno v:
International Journal of Molecular Sciences, Vol 20, Iss 13, p 3325 (2019)
The recruitment and transference of proteins through protein−protein interactions is a general process involved in various biological functions in cells. Despite the importance of this general process, the dynamic mechanism of how proteins are recr
Externí odkaz:
https://doaj.org/article/69ce282a6e3646669911238864408c06
Autor:
Xiaoqin Zou, Sheng-You Huang
Publikováno v:
International Journal of Molecular Sciences, Vol 11, Iss 8, Pp 3016-3034 (2010)
Molecular docking is a widely-used computational tool for the study of molecular recognition, which aims to predict the binding mode and binding affinity of a complex formed by two or more constituent molecules with known structures. An important typ
Externí odkaz:
https://doaj.org/article/4899c8d846e6492f8d0fa2ffb7d4de0f