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transferred nuclear Overhauser effects (trNOEs) have been employed in the docking program HADDOCK to generate models for the LAR-fondaparinux complex. These models are further analyzed by postprocessing energetic analysis to identify key binding interactions.
PTPRF may have value as a predictive marker to identify which patients can obtain the greatest benefit from erlotinib in the post-first-line setting.
Homozygous truncating PTPRF mutation causes athelia.
PTPRF is down-regulated in hepatocellular carcinoma-facilitated tumor development.
Interaction between the tripartite NGL-1, netrin-G1 and LAR adhesion complex promotes development of excitatory synapses.
LAR functions as a negative regulator of adipogenesis.
Trans-synaptic adhesions between netrin-G ligand-3 (NGL-3) and receptor tyrosine phosphatases LAR, protein-tyrosine phosphatase delta (PTPdelta), and PTPsigma via specific domains regulate excitatory synapse formation.
regulation of expression by cell density through functional E-cadherin complexes
interactions between RPTP-domain1s and RPTP-domain 2s are a common but specific mechanism that is likely to be regulated- domain2s and the wedge structures are crucial determinants of binding specificity, thus regulating cross-talk between RPTPs
LAR PTPase domains play distinct functional roles in phosphorylation and dephosphorylation
LAR as a crucial regulator of the sensitivity of two key insulin signalling pathways to insulin
Results identify a protein tyrosine phosphatase as a potential substrate of TACE and describe proteolytic processing of PTP-LAR as a means of regulating phosphatase activity downstream and thus under the control of EGFR-mediated signaling pathways.
PS/gamma-secretase-mediated cleavage of LAR controls LAR-beta-catenin interaction, suggesting an essential role for PS/gamma-secretase in the regulation of LAR signaling
Regulated degradation of liprinalpha1 is important for proper LAR receptor distribution, and could provide a mechanism for localized control of dendrite and synapse morphogenesis by activity and CaMKII.
LAR and Src are identified as Death-associated protein kinase (DAPK) regulators through their reciprocal modification of DAPK Y491/492 residues and establishes a functional link of this DAPK-regulatory circuit to tumor progression.
the PTPase activity in patients with insulin receptor gene mutation and severe insulin resistance may differ from that in ordinary type 2 diabetes
We show that PTP-3, a LAR homolog in Caenorhabditis elegans, participates in Sema2A-regulated axon guidance. PTPdelta, a member of vertebrate LAR class PTPs, is involved in Sema3A-regulated cortical dendritic growth. In Sema3A signaling, PTPdelta activates Fyn and Src kinases by dephosphorylating their C-terminal Tyr residues.
loss of LAR activity resulted in reduced activity of CDK1.
Study has identified LAR as a regulator of key signaling pathways, including mTOR and JNK, and has significantly expanded the number of proteins regulated downstream of LAR phosphatase activity.
Chondroitin Sulfate Proteoglycans Negatively Modulate Spinal Cord Neural Precursor Cells by Signaling Through LAR and RPTPsigma and Modulation of the Rho/ROCK Pathway.
This study demonstrates the crucial role of LAR in restricting regrowth of injured CNS axons
Ptprs and Ptprf deficiency affects mandibular cell proliferation.
Inhibition of LAR attenuates palmitate-induced insulin resistance in myotubes.
Deletion of LAR in knock-out mice or blockade of LAR with sequence-selective peptides significantly overcomes neurite growth restrictions of chondroitin sulfate proteoglycan in neuronal cultures.
the crystal structures of the first and second immunoglobulin-like domains of the Drosophila type IIa receptor Dlar and its mouse homolog LAR were reported.
LAR reduces the basal c-Abl activity thereby allowing for platelet derived growth factor beta receptor kinase activation
LAR deficiency affected the differentiation & expansion of immature thymocytes, positive & negative selection, & a lower Ca2+ response. LAR is an important modulator of TCR signaling that controls thymocyte differentiation.
PTP alpha is required for integrin-proximal events and phosphorylates FAK
In conclusion, behavioural testing of the LAR tyrosine phosphatase-deficient mice revealed a spatial learning impairment and a significant increase in activity.
LAR enhances retinal ganglion cell neurite initiation whilst suppressing retinal ganglion cell survival
Results introduce leukocyte common antigen-related (LAR) protein tyrosine phosphatase (PTP) as the first PTP found to be expressed in dentate progenitors and point to inhibition of LAR as a potential strategy for promoting neurogenesis.
Here, we report rapid and efficient construction of PTPRF and NWC TgVs without using restriction endonucleases.
Presynaptic PTPsigma controls the number of olfactory sensory neuron and mitral cell synapses by suppressing excessive increase of axon terminals.
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region, a single transmembrane region, and two tandem intracytoplasmic catalytic domains, and thus represents a receptor-type PTP. The extracellular region contains three Ig-like domains, and nine non-Ig like domains similar to that of neural-cell adhesion molecule. This PTP was shown to function in the regulation of epithelial cell-cell contacts at adherents junctions, as well as in the control of beta-catenin signaling. An increased expression level of this protein was found in the insulin-responsive tissue of obese, insulin-resistant individuals, and may contribute to the pathogenesis of insulin resistance. Two alternatively spliced transcript variants of this gene, which encode distinct proteins, have been reported.
, leukocyte antigen-related (LAR) PTP receptor
, leukocyte antigen-related tyrosine phosphatase
, leukocyte common antigen related
, protein tyrosine phosphatase, receptor type, F polypeptide
, receptor-linked protein-tyrosine phosphatase LAR
, receptor-type tyrosine-protein phosphatase F
, protein tyrosine phosphatase receptor-type F