Results 11 to 20 of about 203,778 (305)

Immunomodulatory Effect of Toll-Like Receptor-3 Ligand Poly I:C on Cortical Spreading Depression [PDF]

, 2009
The release of inflammatory mediators following cortical spreading depression (CSD) is suggested to play a role in pathophysiology of CSD-related neurological disorders.
Aghabarari, A., Ghaemi, A., Gorji, A., Khaleghi Ghadiri, M., Khodaie, B., Lotfinia, A.A., Lotfinia, M., Meuth, S., Sajadian, A.   +8 more
core   +3 more sources

Electrospinning and Post-Spun Chain Conformations of Synthetic, Hydrophobic Poly(α-amino acid)s. [PDF]

, 2020
Electrospinning and post-spun conformations of hydrophobic poly(α-amino acid)s are described in this study. The poly(α-amino acid)s, poly(Gly), poly(L-Ala), poly(L-Val), and poly(L-Leu) were synthesized via corresponding N-carboxy-a-amino acid anhydrides.
Devarayan, Kesavan, Nakagami, Souta, Ohkawa, Kousaku, Suzuki, Shuichi, Yuki, Ichiro   +4 more
core   +1 more source

Translation of dipeptide repeat proteins in C9ORF72 ALS/FTD through unique and redundant AUG initiation codons

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, Soojin Lee, Gopinath Krishnan, Yuanzheng Gu, Deborah Y Kwon, Fen-Biao Gao, Raymond P Roos, Paschalis Kratsios   +7 more
doaj   +1 more source

Human testis expresses a specific poly(A)-binding protein [PDF]

Nucleic Acids Research, 2001
In testis mRNA stability and translation initiation are extensively under the control of poly(A)-binding proteins (PABP). Here we have cloned a new human testis-specific PABP (PABP3) of 631 amino acids (70.1 kDa) with 92.5% identical residues to the ubiquitous PABP1.
Féral, Chloé, Guellaën, Georges, Pawlak, André   +2 more
openaire   +3 more sources

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, Egor Svidritskiy, Denis Susorov, Soojin Lee, Alexander Park, Sarah Zvornicanin, Gabriel Demo, Fen-Biao Gao, Andrei A. Korostelev   +8 more
doaj   +1 more source

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
openaire   +2 more sources

Proximity proteomics of C9orf72 dipeptide repeat proteins identifies molecular chaperones as modifiers of poly-GA aggregation

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, Dmytro Morderer, Melissa C. Wren, Sara A. Vettleson-Trutza, Yanzhe Wang, Benjamin E. Rabichow, Michelle R. Salemi, Brett S. Phinney, Björn Oskarsson, Dennis W. Dickson, Wilfried Rossoll   +10 more
doaj   +1 more source

The RNA Binding Domains of the Nuclear poly(A)-binding Protein [PDF]

Journal of Biological Chemistry, 2003
The nuclear poly(A)-binding protein (PABPN1) is involved in the synthesis of the mRNA poly(A) tails in most eukaryotes. We report that the protein contains two RNA binding domains, a ribonucleoprotein-type RNA binding domain (RNP domain) located approximately in the middle of the protein sequence and an arginine-rich C-terminal domain.
Uwe, Kühn, Anne, Nemeth, Sylke, Meyer, Elmar, Wahle   +3 more
openaire   +2 more sources

Study of the functional product’s protein compounds digestion features

Теория и практика переработки мяса, 2020
The aim of the study was to investigate the transformation of meat product’s proteins from pig hearts and aortas during enzymatic hydrolysis in an in vitro model of the gastrointestinal tract.
E. R. Vasilevskaya, A. G. Akhremko, E. K. Polishchuk, L. V. Fedulova   +3 more
doaj   +1 more source

Poly(A) Nuclease Interacts with the C-terminal Domain of Polyadenylate-binding Protein Domain from Poly(A)-binding Protein [PDF]

Journal of Biological Chemistry, 2007
The poly(A)-binding protein (PABP) is an essential protein found in all eukaryotes and is involved in an extensive range of cellular functions, including translation, mRNA metabolism, and mRNA export. Its C-terminal region contains a peptide-interacting PABC domain that recruits proteins containing a highly specific PAM-2 sequence motif to the ...
Nadeem, Siddiqui, David A, Mangus, Tsung-Cheng, Chang, Jeanne-Marie, Palermino, Ann-Bin, Shyu, Kalle, Gehring   +5 more
openaire   +2 more sources