IndraLab
Statements
sparser
"It possesses several RNA-binding structural domains, namely four C-terminal heterologous ribonucleoprotein K homology (KH) (KH1-KH4) domains and two N-terminal RNA recognition motifs [ xref ], and are involved in the regulation of a wide range of RNA processing mechanisms, such as localization, stability, and translation [ xref ]."
sparser
"IGF2BP2 contains dual N‐terminal RNA recognition motifs (RRM1/RRM2, residues 3–157) mediating mRNA binding through conserved RNP1/RNP2 sequences, and four C‐terminal K homology domains (KH1‐KH4, residues 193–575) that stereospecifically recognize m6A‐modified RNAs via conserved GXXG motif interactions. xref To spatially resolve CPSF6‐binding epitopes, we engineered Myc‐tagged truncations: RRM, KH1‐4, KH1‐2, and KH3‐4 (Figure xref )."
sparser
"It contains three K-homology domains (KH1-KH3) responsible for nucleic acid binding, one K protein interactive domain (KI) responsible for protein binding, and a nuclear-cytoplasmic shuttling domain (KNS) that confers the ability to translocate bidirectionally through the nuclear pore complex."
| PMC
sparser
"It is well known that post‐transcriptional modifications of messenger RNAs (mRNAs), among which m 6 A is the most abundant internal RNA modification, regulate genes expression by influencing mRNA splicing, stability, translocation and translation. [ xref ] m 6 A modification is deposited by “writers” the methyltransferase complex containing the methyltransferase‐like 3 and 14 proteins (METTL3 and METTL14) and their regulator Wilms tumor 1‐associated protein, and removed by “erasers” demethylases: fat mass and obesity‐associated protein (FTO) and α‐ketoglutarate dependent dioxygenase AlkB homolog 5 (ALKBH5). [ xref , xref , xref , xref ] Moreover, m 6 A modification exerts its biological functions by “readers”: YTH (YT521‐B homology) domain proteins including YTHDC1–2 and the YTH‐family proteins YTHDF1–3 as well as insulin‐like growth factor 2 mRNA binding proteins IGF2BP1–3. [ xref ] Among these m 6 A readers, IGF2BP2 binds RNA via its six characteristic RNA‐binding domains, containing two RNA recognition motifs (RRM1 and RRM2) and four K Homology (KH) domains (KH1–KH4). [ xref ] Dysregulation of IGF2BP2 is implicated in certain diseases such as diabetes and cancer, nevertheless, little is known about IGF2BP2's functions in immunity."
sparser
"Previous studies have reported
increased bitterness in hydrolyzed
plant-based proteins such as soy, pea, canola, chickpeas, and peanut
hydrolysate compared to unhydrolyzed proteins. xref , xref , xref , xref , xref However, recent studies have not investigated the
taste of potato protein hydrolysates; only studies concerning the
functional properties of these hydrolysates have been published. xref Therefore, the taste profiles of one commercial
potato protein isolate (KPI) and four hydrolysates (KH1–KH4)
were investigated ( xref )."