Results 11 to 20 of about 122,513 (306)
Evidence that Poly(A) Binding Protein C1 Binds Nuclear Pre-mRNA Poly(A) Tails [PDF]
Molecular and Cellular Biology, 2006 In mammalian cells, poly(A) binding protein C1 (PABP C1) has well-known roles in mRNA translation and decay in the cytoplasm. However, PABPC1 also shuttles in and out of the nucleus, and its nuclear function is unknown. Here, we show that PABPC1, like the major nuclear poly(A) binding protein PABPN1, associates with nuclear pre-mRNAs that are ...
Nao, Hosoda +2 more
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Dynamic interaction of poly(A)-binding protein with the ribosome [PDF]
Scientific Reports, 2018 Abstract Eukaryotic mRNA has a cap structure and a poly(A) tail at the 5′ and 3′ ends, respectively. The cap structure is recognized by eIF (eukaryotic translation initiation factor) 4 F, while the poly(A) tail is bound by poly(A)-binding protein (PABP).
Kodai Machida +6 more
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HIV protease cleaves poly(A)-binding protein [PDF]
Biochemical Journal, 2006 The PABP [poly(A)-binding protein] is able to interact with the 3′ poly(A) tail of eukaryotic mRNA, promoting its translation. Cleavage of PABP by viral proteases encoded by several picornaviruses and caliciviruses plays a role in the abrogation of cellular protein synthesis.
Álvarez, Enrique +3 more
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eLife, 2023 A hexanucleotide repeat expansion in C9ORF72 is the most common genetic cause of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). A hallmark of ALS/FTD pathology is the presence of dipeptide repeat (DPR) proteins, produced from both
Yoshifumi Sonobe +7 more
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Recognition of Polyadenylate RNA by the Poly(A)-Binding Protein [PDF]
Cell, 1999 The cocrystal structure of human poly(A)-binding protein (PABP) has been determined at 2.6 A resolution. PABP recognizes the 3' mRNA poly(A) tail and plays critical roles in eukaryotic translation initiation and mRNA stabilization/degradation. The minimal PABP used in this study consists of the N-terminal two RRM-type RNA-binding domains connected by a
Deo, Rahul C +3 more
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Ribosome inhibition by C9ORF72-ALS/FTD-associated poly-PR and poly-GR proteins revealed by cryo-EM
Nature Communications, 2022 The expansion of GGGGCC repeats in the C9ORF72 gene results in the production of disease causing abnormal proteins with polymeric glycine-arginine (poly-GR) and polymeric glycine-proline (poly-PR).
Anna B. Loveland +8 more
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Identification of proteins associating with poly(A)‐binding‐protein mRNA [PDF]
European Journal of Biochemistry, 1992 Synthesis of poly(A)‐binding protein is regulated at the translational level. We have investigated the binding of proteins to this mRNA on the premise that the protein(s) of the mRNP complex may be involved in regulating the expression of the mRNA. We found the first 243 nucleotides of the 5′ untranslated region to contain sequences essential for RNP ...
L C, Berger, J, Bag, B H, Sells
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Ribosomal Association of Poly(A)-binding Protein in Poly(A)-deficient Saccharomyces cerevisiae [PDF]
Journal of Biological Chemistry, 1996 Poly(A)-binding protein, the most abundant eukaryotic mRNP protein, is known primarily for its association with polyadenylate tails of mRNA. In the yeast, Saccharomyces cerevisiae, this protein (Pabp) was found to be essential for viability and has been implicated in models featuring roles in mRNA stability and as an enhancer of translation initiation.
A, Proweller, J S, Butler
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Acta Neuropathologica Communications, 2022 The most common inherited cause of two genetically and clinico-pathologically overlapping neurodegenerative diseases, amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), is the presence of expanded GGGGCC intronic hexanucleotide ...
Feilin Liu +10 more
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mRNA stabilization by poly(A) binding protein is independent of poly(A) and requires translation [PDF]
Genes & Development, 1998 Translation and mRNA stability are enhanced by the presence of a poly(A) tail. In vivo, the tail interacts with a conserved polypeptide, poly(A) binding protein (Pab1p). To examine Pab1p function in vivo, we have tethered Pab1p to the 3′ UTR of reporter mRNAs by fusing it to MS2 coat protein and placing MS2 binding sites in the 3′ UTR of the reporter ...
J M, Coller, N K, Gray, M P, Wickens
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