1,721,129 research outputs found
Signaling by EGFR
No full textThe epidermal growth factor receptor (EGFR) is one member of the ErbB family of transmembrane glycoprotein tyrosine
receptor kinases (RTK). Binding of EGFR to its ligands leads to autophosphorylation of tyrosine residues on the receptor and
subsequent activation of signal transduction pathways that are involved in regulating cellular proliferation, differentiation, and
survival. Ligand binding with EGFR results in receptor homo- or heterodimerization at the cell surface
Introduction
No full textThe introduction offers a frame of reference for the individual studies that follow. It starts with modern definitions and taxonomies of memory and introduces some approaches to memory studies. It then focuses on some key aspects of memory in ancient Greece: (1) its connection with time and history; (2) its perceived divine nature and trans-temporal power; (3) the impact of the introduction of writing on Greek conceptions of memory and memorial practices; (4) memory and archives; (5) memory's persistence as a powerful divinity, for instance in the 'Dionysiac-Orphic' tablets; (6) the dynamic tension between memory and forgetting; (7) the relations between memory, cognition, and knowledge; (8) the connections between memory, reciprocity, justice, and retribution; (9) gender and memory; (10) the role of objects and places as sites of memory. The chapter then proposes a reading of the contributions to the volume, pointing out intersections, coincidences and divergences among the various approaches adopted by the Contributors
PTPRJ (protein tyrosine phosphatase, receptor type, J)
Full text linkMultiple transcript variants encoding different isoforms have been found for this gene.
Three transcripts are described in Ensembl (ID: ENSG00000149177).
The first (ENST00000418331) represents the longer isoform and encodes a protein that
consists of an extracellular fibronectin type 3 domain and a cytosolic catalytic domain.
The second isoform (ENST00000440289) has multiple differences in the presence and
absence of exons at its 3' end, compared to the first isoform. These differences produce
a unique 3' UTR and the encoded protein is shorter and consists of the extracellular
fibronectin type 3 domain without the cytosolic catalytic region. The third transcript
(ENST00000278456) has the same length as the first, but it encodes a truncated protein,
that consists of fibronectin type 3 domains. Only the first two isoforms are members of
the human CCDS set and have been described in NCBI (IDs: NM_001098503.1,
NM_001098503.1).
The cDNA encoding PTPRJ/DEP-1 was isolated from a HeLa cell library (Ostman et
al., 1994). The expression level and the activity of DEP-1 increase with cell density.
This increase occurs gradually with increasing cell contact and is initiated before
saturation cell density is reached. These observations suggest that DEP-1 may contribute
to the mechanism of contact inhibition of cell growth
Mapping protein-protein interactions with phage-displayed combinatorial peptide libraries
No full textThis unit describes the process and analysis of affinity selecting bacteriophage M13 from libraries displaying combinatorial peptides fused to either a minor or major capsid protein. Direct affinity selection uses target protein bound to a microtiter plate followed by purification of selected phage by ELISA. Alternatively, there is a bead-based affinity selection method. These methods allow one to readily isolate peptide ligands that bind to a protein target of interest and use the consensus sequence to search proteomic databases for putative interacting proteins
Carl von Rokitansky and the Italian translation of the Handbuch der Pathologischen Anatomie: a linguistic and doctrinal enigma.
No full text
Promoter of a eukaryotic tRNAPro gene is composed of three noncontiguous regions. Proc. Natl. Acad. Sci.
No full textSelection of Ligands by Panning of Domain Libraries Displayed on Phage Lambda Reveals New Potential Partners of Synaptojanin 1
No full textPromoter of a eukaryotic tRNAPro gene is composed of three noncontiguous regions. Proc. Natl. Acad. Sci.
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