Overproduction of non-translatable mRNA silences. The transcription ofTy1 retrotransposons inS. cerevisiae via functional inactivation of the nuclear cap-binding complex and subsequent hyperstimulation of the TORC1 pathway

Yeast ◽  
2008 ◽  
Vol 25 (5) ◽  
pp. 327-347 ◽  
Author(s):  
Xiaofeng Wu ◽  
Yi Wei Jiang
Keyword(s):  
Cap Binding Complex ◽  
Functional Inactivation ◽  
Translatable Mrna

scholarly journals Roles of pRB in the Regulation of Nucleosome and Chromatin Structures

2016 ◽  
Vol 2016 ◽  
pp. 1-11 ◽  
Author(s):  
Chiharu Uchida
Keyword(s):  
Target Genes ◽  
Chromosome Instability ◽  
Cancer Therapies ◽  
Induce Cell Cycle Arrest ◽  
Cellular Events ◽  
Cycle Arrest ◽  
Histone Modifiers ◽  
Physical Interactions ◽  
Functional Inactivation

Retinoblastoma protein (pRB) interacts with E2F and other protein factors to play a pivotal role in regulating the expression of target genes that induce cell cycle arrest, apoptosis, and differentiation. pRB controls the local promoter activity and has the ability to change the structure of nucleosomes and/or chromosomes via histone modification, epigenetic changes, chromatin remodeling, and chromosome organization. Functional inactivation of pRB perturbs these cellular events and causes dysregulated cell growth and chromosome instability, which are hallmarks of cancer cells. The role of pRB in regulation of nucleosome/chromatin structures has been shown to link to tumor suppression. This review focuses on the ability of pRB to control nucleosome/chromatin structures via physical interactions with histone modifiers and chromatin factors and describes cancer therapies based on targeting these protein factors.

scholarly journals Levels of translatable mRNA coding for rat liver glucokinase.

1983 ◽  
Vol 258 (15) ◽  
pp. 9143-9146 ◽  
Author(s):  
J T Spence
Keyword(s):  
Rat Liver ◽  
Translatable Mrna

scholarly journals Biofunctional Peptide FNIII14: Therapeutic Potential

Encyclopedia ◽  
2021 ◽  
Vol 1 (2) ◽  
pp. 350-359
Author(s):  
Motomichi Fujita ◽  
Manabu Sasada ◽  
Takuya Iyoda ◽  
Satoshi Osada ◽  
Hiroaki Kodama ◽  
...  
Keyword(s):  
Molecular Structure ◽  
Extracellular Matrix ◽  
Conformational Changes ◽  
Metabolic Diseases ◽  
Therapeutic Potential ◽  
Malignant Tumors ◽  
Β1 Integrin ◽  
Inactive Form ◽  
Functional Inactivation ◽  
Organ Fibrosis

Biofunctional peptide FNIII14, which is derived from the 14th fibronectin (FN) type III-like (FN-III) repeat of FN molecule, is capable of inhibiting cell adhesion to the extracellular matrix (ECM). This functional site is usually buried within the molecular structure of FN, but can be exposed by conformational changes and proteolytic cleavage. Peptide FNIII14 can induce a conformational change in β1-integrin from the active to the inactive form, causing functional inactivation. Based on this anti-adhesive activity, peptide FNIII14 exhibits therapeutic potential for several diseases such as metabolic diseases, organ fibrosis, and malignant tumors. Peptide FNIII14 blocks integrin-mediated signaling by a mechanism entirely distinct from that of conventional antagonisitic peptides, including Arg-Gly-Asp peptides that competitively inhibit the ECM binding of integrin.

NOVEL WAY OF CAPPING mRNA TRIMER AND STUDIES OF ITS INTERACTION WITH HUMAN NUCLEAR CAP-BINDING COMPLEX

2005 ◽  
Vol 24 (5-7) ◽  
pp. 1131-1134 ◽  
Author(s):  
Remigiusz Worch ◽  
Janusz Stepinski ◽  
Anna Niedzwiecka ◽  
Marzena Jankowska-Anyszka ◽  
Catherine Mazza ◽  
...  
Keyword(s):  
Cap Binding Complex

scholarly journals The nuclear cap-binding complex interacts with the U4/U6{middle dot}U5 tri-snRNP and promotes spliceosome assembly in mammalian cells

RNA ◽  
2013 ◽  
Vol 19 (8) ◽  
pp. 1054-1063 ◽  
Author(s):  
M. Pabis ◽  
N. Neufeld ◽  
M. C. Steiner ◽  
T. Bojic ◽  
Y. Shav-Tal ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Spliceosome Assembly ◽  
Cap Binding Complex
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