The oncogenic potential of NANOG: An important cancer induction mediator

MEX3A belongs to the MEX3 (Muscle EXcess) protein family consisting of four members (MEX3A-D) in humans. Characteristic for MEX3 proteins is their domain structure with 2 HNRNPK homology (KH) domains mediating RNA binding and a C-terminal really interesting new gene (RING) domain that harbors E3 ligase function. In agreement with their domain composition, MEX3 proteins were reported to modulate both RNA fate and protein ubiquitination. MEX3 paralogs exhibit an oncofetal expression pattern, they are severely downregulated postnatally, and re-expression is observed in various malignancies. Enforced expression of MEX3 proteins in various cancers correlates with poor prognosis, emphasizing their oncogenic potential. The latter is supported by MEX3A’s impact on proliferation, self-renewal as well as migration of tumor cells in vitro and tumor growth in xenograft studies.

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Oncogenic potential of ATAD2 in stomach cancer and insights into the protein-protein interactions at its AAA + ATPase domain and bromodomain

Journal of Biomolecular Structure and Dynamics ◽

10.1080/07391102.2021.1871959 ◽

2021 ◽

pp. 1-17

Author(s):

Aditi Nayak ◽

Sugandh Kumar ◽

Shivaram Prasad Singh ◽

Asima Bhattacharyya ◽

Anshuman Dixit ◽

...

Keyword(s):

Stomach Cancer ◽

Protein Interactions ◽

Atpase Domain ◽

Protein Protein Interactions ◽

Oncogenic Potential ◽

Aaa Atpase

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Modeling and Molecular Dynamics of the 3D Structure of the HPV16 E7 Protein and Its Variants

International Journal of Molecular Sciences ◽

10.3390/ijms22031400 ◽

2021 ◽

Vol 22 (3) ◽

pp. 1400

Author(s):

Ciresthel Bello-Rios ◽

Sarita Montaño ◽

Olga Lilia Garibay-Cerdenares ◽

Lilian Esmeralda Araujo-Arcos ◽

Marco Antonio Leyva-Vázquez ◽

...

Keyword(s):

Molecular Dynamics ◽

3D Structure ◽

Epidemiological Studies ◽

Dynamics Simulation ◽

Structural Refinement ◽

Oncogenic Potential ◽

Structural Differences ◽

Reference Protein ◽

E6 And E7 ◽

First Time

The oncogenic potential of high-risk human papillomavirus (HPV) is predicated on the production of the E6 and E7 oncoproteins, which are responsible for disrupting the control of the cell cycle. Epidemiological studies have proposed that the presence of the N29S and H51N variants of the HPV16 E7 protein is significantly associated with cervical cancer. It has been suggested that changes in the amino acid sequence of E7 variants may affect the oncoprotein 3D structure; however, this remains uncertain. An analysis of the structural differences of the HPV16 E7 protein and its variants (N29S and H51N) was performed through homology modeling and structural refinement by molecular dynamics simulation. We propose, for the first time, a 3D structure of the E7 reference protein and two of Its variants (N29S and H51N), and conclude that the mutations induced by the variants in N29S and H51N have a significant influence on the 3D structure of the E7 protein of HPV16, which could be related to the oncogenic capacity of this protein.

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