Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Venkateshwarlu, Bandi"'
Autor:
Venkateshwarlu Bandi, Martin Rennie, Intisar Koch, Polly Gill, Oscar D. Pacheco, Aaron D. Berg, Hong Cui, D. Isum Ward, Francisco Bustos
Publikováno v:
HGG Advances, Vol 6, Iss 1, Pp 100378- (2025)
Summary: Tonne-Kalscheuer syndrome (TOKAS; MIM: 300978) is an X-linked recessive disorder with devastating consequences for patients, such as intellectual disability, developmental delay, and multiple congenital abnormalities. TOKAS is associated wit
Externí odkaz:
https://doaj.org/article/0ed6e124f5e44c17b1df5777321a9a16
Autor:
Pulicherla, Yugandhar, Meher, Sudhanshu, Nagayya, Shiddamallayya, Bora, Devanjal, Cheemanapalli, Srinivasulu, Bhardwaj, Yashpal, Tripathi, Ashish, Venkateshwarlu, Bandi, Rath, Chinmay, Mangal, Anupam, Narayanam, Srikanth
Publikováno v:
Journal of Drug Research in Ayurvedic Sciences (JDRAS); Apr-Jun2023, Vol. 8 Issue 2, p159-172, 14p
Autor:
Murugan Selvam, Venkateshwarlu Bandi, Saravanaraman Ponne, Cheemala Ashok, Sudhakar Baluchamy
Publikováno v:
Experimental cell research. 415(1)
The Polycomb Repressive Complex (PRC) proteins, EZH2 and EZH1 regulate many biological processes by generating the repressive H3K27me3 modifications in the chromatin. However, the factors that regulate the EZH1/EZH2 functions are poorly studied. We i
Publikováno v:
Medical oncology (Northwood, London, England). 34(8)
MiR-181a-2 plays a major role in cell proliferation both positively and negatively depending on tissue type by targeting several regulators 3'UTR regions. We have predicted several targets for miR-181a-2 through computational approaches and character
Autor:
Kannan Muthu, Venkateshwarlu Bandi, Gokulapriya Govindarajalu, Sudhakar Baluchamy, Prachi Singh, Anand Thirunavukarasou
Publikováno v:
Molecular and Cellular Biochemistry. 401:219-228
Regulated polyubiquitination is a key step for controlling protein degradation and maintaining proper balance between the proliferation of normal and uncontrolled cells. Addition of ubiquitin to the proteins by E3 ubiquitin ligases targets them for d