Results 251 to 260 of about 288,999 (305)

Synthesis and Biological Evaluation of Well‐Defined M6P(n)‐Modified Glycopeptides for Targeted Protein Degradation

open access: yesChemistry – A European Journal, EarlyView.
A synthetic methodology has been developed to prepare multifunctional M6P and M6Pn ligands of different valency. The glycopeptides were conjugated to cetuximab and then examined to mediate cellular uptake of fluorescently labeled EGFRvIII. Only cetuximab modified by glycopeptides having 3 or 6 M6P or M6Pn residues demonstrated greater uptake.
Patrycja Lenartowicz   +6 more
wiley   +1 more source

Hybrid Macrocyclic Peptides — Synthetic Strategies to Diversify and Cyclize Peptide Libraries in Phage Display Selections

open access: yesChemistry – A European Journal, EarlyView.
Hybrid macrocyclic peptides unite genetically encoded peptide libraries with the structural complexity of synthetic small molecules. This Review critically analyzes phage‐compatible cyclization and diversification chemistries, highlights emerging opportunities beyond traditional cysteine‐based approaches, and outlines how future advances may enable the
Titia Rixt Oppewal, Clemens Mayer
wiley   +1 more source

TNFR1 signaling is positively regulated by Jak-2 and c-Src via tyrosine phosphorylation. [PDF]

open access: yesTurk J Biol
Hapil Zevkliler FZ   +5 more
europepmc   +1 more source

Expression of mutant TIE2 p.L914F during mouse development causes embryonic lethality and defects in vascular remodeling

open access: yesDevelopmental Dynamics, EarlyView.
Abstract Background Sporadic venous malformation (VM) is associated with the hyperactivating p.L914F mutation in TIE2, a receptor tyrosine kinase essential for vascular development. This mutation is not found in hereditary VM, suggesting incompatibility with life when expressed during early vascular development.
Lindsay J. Bischoff   +6 more
wiley   +1 more source

Tyrosine Phosphorylation of Caveolin-1 in the Endothelium

Experimental Cell Research, 1999
Caveolin-1, a scaffolding protein of caveolae, is known to be tyrosine-phosphorylated by Src kinases. Recently we generated a specific antibody to caveolin-1 phosphorylated at tyrosine-14 (PY14) (R. Nomura and T. Fujimoto, 1999, Mol. Biol. Cell 10, 975-986).
Toyoshi Fujimoto   +2 more
exaly   +3 more sources

Protein tyrosine phosphorylation in streptomycetes

FEMS Microbiology Letters, 1994
Using phosphotyrosine-specific antibodies, we demonstrate that in several Streptomyces spp. a variety of proteins are phosphorylated on tyrosine residues. Tyrosine phosphorylation was found in a number of Streptomyces species including Streptomyces lividans, Streptomyces hygroscopicus and Streptomyces lavendulae. Each species exhibited a unique pattern
Waters, Barbara   +3 more
openaire   +4 more sources

Tyrosine phosphorylation in human lymphomas

The Histochemical Journal, 2003
In a previous study, we showed that the high level of protein tyrosine phosphorylation present in lymphomas containing an anaplastic lymphoma kinase (ALK) can be demonstrated in routinely processed paraffin tissue sections using immunolabelling techniques.
Haralambieva, E   +18 more
openaire   +2 more sources

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