Your browser doesn't support javascript.
loading
Bioinformatics analysis of Myelin Transcription Factor 1.
Ding, Hongjun; Li, Yanju; Zhang, Yanlong; Meng, Huipeng; Wang, Keqiang; Sun, Qian; Li, Xichuan; Dong, Huajiang; Chen, Long; He, Feng.
Afiliación
  • Ding H; School of Precision Instruments and Opto-Electronics Engineering, Tianjin University, Tianjin, China.
  • Li Y; Tianjin Public Security Profession College, Tianjin, China.
  • Zhang Y; School of Precision Instruments and Opto-Electronics Engineering, Tianjin University, Tianjin, China.
  • Meng H; Medical Laboratory Department, National Clinical Research Center for Cancer, Key Laboratory of Cancer Prevention and Therapy, Tianjin's Clinical Research Center for Cancer, Tianjin Medical University Cancer Institute, Tianjin, China.
  • Wang K; School of Precision Instruments and Opto-Electronics Engineering, Tianjin University, Tianjin, China.
  • Sun Q; School of Precision Instruments and Opto-Electronics Engineering, Tianjin University, Tianjin, China.
  • Li X; School of Precision Instruments and Opto-Electronics Engineering, Tianjin University, Tianjin, China.
  • Dong H; School of Precision Instruments and Opto-Electronics Engineering, Tianjin University, Tianjin, China.
  • Chen L; School of Precision Instruments and Opto-Electronics Engineering, Tianjin University, Tianjin, China.
  • He F; College of Life Sciences, Tianjin Normal University, Tianjin, China.
Technol Health Care ; 29(S1): 441-453, 2021.
Article en En | MEDLINE | ID: mdl-33682781
ABSTRACT
BACKGROUND AND

OBJECTIVE:

We aimed to further study the role of Myelin Transcription Factor 1(MyT1) in tumor and other diseases and epigenetic regulation, and better understand the regulatory mechanism of MyT1.

METHODS:

Using bioinformatics analysis, the structure and function of MyT1sequence were predicted and analyzed using bioinformatics analysis, and providing a theoretical basis for further experimental verification and understanding the regulatory mechanism of MyT1. The first, second and third-level structures of MyT1 were predicted and analyzed by bioinformatics analysis tools.

RESULTS:

MyT1 is found to be an unstable hydrophilic protein, rather than a secretory protein, with no signal peptide or trans-membrane domain; total amino acids located on the surface of the cell membrane. It contains seven zinc finger domains structurally. At sub-cellular level, MyT1 is localized in the nucleus. The phosphorylation site mainly exists in serine, and its secondary structure is mainly composed of random coils and alpha helices; the three-dimensional structure is analyzed by modeling.

CONCLUSIONS:

In this study, the structure and function of MyT1 protein were predicted, thereby providing a basis for subsequent expression analysis and functional research; it laid the foundation for further investigation of the molecular mechanism involved in the development of diseases.
Asunto(s)
Palabras clave

Texto completo: 1 Base de datos: MEDLINE Asunto principal: Factores de Transcripción / Proteínas de Unión al ADN Tipo de estudio: Prognostic_studies Idioma: En Revista: Technol Health Care Asunto de la revista: ENGENHARIA BIOMEDICA / SERVICOS DE SAUDE Año: 2021 Tipo del documento: Article

Texto completo: 1 Base de datos: MEDLINE Asunto principal: Factores de Transcripción / Proteínas de Unión al ADN Tipo de estudio: Prognostic_studies Idioma: En Revista: Technol Health Care Asunto de la revista: ENGENHARIA BIOMEDICA / SERVICOS DE SAUDE Año: 2021 Tipo del documento: Article