scholarly journals General insight into cancer: An overview of colorectal cancer (Review)

2021 ◽  
Vol 15 (6) ◽  
Author(s):  
Shiekhah Alzahrani ◽  
Huda Al Doghaither ◽  
Ayat Al‑Ghafari
2017 ◽  
Vol 18 (6) ◽  
pp. 734-750 ◽  
Author(s):  
Zar Chi Thent ◽  
Nurul Hannim Zaidun ◽  
Muhammad Fairuz Azmi ◽  
Mu`izuddin Senin ◽  
Haszianaliza Haslan ◽  
...  

Author(s):  
Nurul Amir Hashim ◽  
Sharaniza Ab‑Rahim ◽  
Leny Suddin ◽  
Mohd Ahmad Saman ◽  
Musalmah Mazlan

2018 ◽  
Vol 6 (1) ◽  
pp. 1-5
Author(s):  
Yovchev Y ◽  
Enchev E ◽  
Dimitrov E ◽  
Minkov G ◽  
Nikolov S

F1000Research ◽  
2019 ◽  
Vol 8 ◽  
pp. 997 ◽  
Author(s):  
Derek M. Lin ◽  
Henry C. Lin

Bacteriophages are the most prominent members of the gut microbiome, outnumbering their bacterial hosts by a factor of 10. Phages are bacteria-specific viruses that are gaining attention as highly influential regulators of the gut bacterial community. Dysregulation of the gut bacterial community contributes to dysbiosis, a microbiome disorder characterized by compositional and functional changes that contribute to disease. A role for phages in gut microbiome dysbiosis is emerging with evidence that the gut phage community is altered in dysbiosis-associated disorders such as colorectal cancer and inflammatory bowel disease. Several recent studies have linked successful fecal microbiota transplantation to uptake of the donor’s gut phage community, offering some insight into why some recipients respond to treatment whereas others do not. Here, we review the literature supporting a role for phages in mediating the gut bacterial community, giving special attention to Western diet dysbiosis as a case study to demonstrate a theoretical phage-based mechanism for the establishment and maintenance of dysbiosis.


2019 ◽  
Vol 116 (41) ◽  
pp. 20404-20410 ◽  
Author(s):  
Amy J. Fernandez ◽  
Earnest James Paul Daniel ◽  
Sai Pooja Mahajan ◽  
Jeffrey J. Gray ◽  
Thomas A. Gerken ◽  
...  

Polypeptide N-acetylgalactosaminyl transferases (GalNAc-Ts) initiate mucin type O-glycosylation by catalyzing the transfer of N-acetylgalactosamine (GalNAc) to Ser or Thr on a protein substrate. Inactive and partially active variants of the isoenzyme GalNAc-T12 are present in subsets of patients with colorectal cancer, and several of these variants alter nonconserved residues with unknown functions. While previous biochemical studies have demonstrated that GalNAc-T12 selects for peptide and glycopeptide substrates through unique interactions with its catalytic and lectin domains, the molecular basis for this distinct substrate selectivity remains elusive. Here we examine the molecular basis of the activity and substrate selectivity of GalNAc-T12. The X-ray crystal structure of GalNAc-T12 in complex with a di-glycosylated peptide substrate reveals how a nonconserved GalNAc binding pocket in the GalNAc-T12 catalytic domain dictates its unique substrate selectivity. In addition, the structure provides insight into how colorectal cancer mutations disrupt the activity of GalNAc-T12 and illustrates how the rules dictating GalNAc-T12 function are distinct from those for other GalNAc-Ts.


2020 ◽  
Vol 43 (6) ◽  
pp. 989-1001
Author(s):  
Pan Xie ◽  
Jun-Luan Mo ◽  
Jin-Hong Liu ◽  
Xi Li ◽  
Li-Ming Tan ◽  
...  

2019 ◽  
Vol 138 (7) ◽  
pp. 789-791
Author(s):  
Stephanie A. Bien ◽  
Yu-Ru Su ◽  
David V. Conti ◽  
Tabitha A. Harrison ◽  
Conghui Qu ◽  
...  

2011 ◽  
Vol 26 (10) ◽  
pp. 1241-1248 ◽  
Author(s):  
Mariana Petaccia Macedo ◽  
Louise De Brot Andrade ◽  
Renata Coudry ◽  
Rodrigo Crespo ◽  
Marina Gomes ◽  
...  

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