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PTF1 Is an Organ-Specific and Notch-Independent Basic Helix-Loop-Helix Complex Containing the Mammalian Suppressor of Hairless (RBP-J) or Its Paralogue, RBP-L
The presence of related peptide motifs in other transcription factors indicates a broader Notch-independent function for RBPJ/SU(H), which indicates that the association of P48 and RBPs is required for proper embryonic development.
Early pancreatic development requires the vertebrate Suppressor of Hairless (RBPJ) in the PTF1 bHLH complex.
It is shown that early in pancreatic development, active PTF1a requires interaction with RBPJ, the vertebrate Suppressor of Hairless, within a stable trimeric DNA-binding complex (PTF1).
A nonclassical bHLH Rbpj transcription factor complex is required for specification of GABAergic neurons independent of Notch signaling.
The requirement for a Ptf1a-Rbpj complex in controlling the balanced formation of inhibitory and excitatory neurons in the developing spinal cord is demonstrated, and a novel Notch-independent function for Rbpj in nervous system development is pointed to.
Characterization of a UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferase That Displays Glycopeptide N-Acetylgalactosaminyltransferase Activity*
The cloning, expression, and characterization of a novel member of the mammalian UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (ppGaNTase) family that transfers Gal NAc to a GalNAc-containing glycopeptide is reported, suggesting thatO-glycosylation of multisite substrates may proceed in a specific hierarchical manner and underscores the potential complexity of the processes that regulate O-glyCosylation.
Cloning and Characterization of a Ninth Member of the UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferase Family, ppGaNTase-T9*
Northern blot analysis revealed that the gene encoding this enzyme is expressed in a broadly distributed manner across many adult tissues, lending further support to the existence of a hierarchical network of differential enzymatic activity within the diversely regulated ppGaNTase family, which may play a role in the various processes governing development.
Cloning and Expression of a Novel, Tissue Specifically Expressed Member of the UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferase Family*
The cloning and expression of the fifth member of the mammalian UDP-GalNAc:polypeptideN-acetylgalactosaminyltransferase (ppGaNTase) family is reported, highlighting the diversity and complexity of the family of genes controllingO-linked glycosylation.
cDNA Cloning and Expression of a Novel UDP-N-acetyl-d-galactosamine:PolypeptideN-Acetylgalactosaminyltransferase*
The cDNA for a fourth member of the mammalian UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, termed ppGaNTase-T4, has been cloned from a murine spleen cDNA library and expressed
Characterization and expression analysis of Galnts in developing Strongylocentrotus purpuratus embryos
The characterization of this enzyme family in the purple sea urchin, S. purpuratus, has begun, and morpholino-mediated knockdown of SpGalnt13 transcripts, results in a deficiency of embryonic skeleton and neurons, suggesting that mucin-type O-glycans play essential roles during embryonic development in S. Purpuratus.
Chromosomal organization and expression analysis of two distinct genes encoding glutamine/glutamic acid-rich proteins.
It was determined by PCR analysis of both submandibular-gland cDNA and genomic DNA that the GRP-Cb gene shows interanimal variability in the number of 69 bp tandem repeats found within exon 3; GRP -Cb genes were shown to contain four, five or six repeats.