Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P10636 (tau protein)
 5,110 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Neurofibrillary tangles as a neuropathological hallmark of Alzheimer's disease are mainly composed of abnormally phosphorylated microtubule-associated protein tau. The present work was primarily focused on the immunohistochemical characterization of recently developed monoclonal antibodies directed against disease-associated epitopes. Anti-phospho-threonine 212/phospho-serine 214 (HPT-1), anti-phospho-threonine 231/phospho-serine 235 (HPT-101) and their biotinylated derivatives were shown to be sensitive markers for the immunohistochemical detection of neuropathological alterations during Alzheimer's disease. Triple carbocyanine immunofluorescence labelling was based on digoxigenylated, fluoresceinated and biotinylated primary antibodies. AT8-immunolabelling of phospho-serine 202 and phospho-threonine 205 combined with HPT-1 and HPT-101-staining revealed similar distribution patterns of the three double-phosphorylated tau epitopes in the neocortex of patients with Alzheimer's disease.
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PMID:Simultaneous detection of tau phospho-epitopes with haptenylated antibodies. 1673 78

In Alzheimer's disease (AD) neurofibrillary tangles (NFT) are formed by hyperphosphorylated microtubule-associated tau protein. It is still a matter of controversy which phosphorylation sites are AD-specific and how these might be linked to the cause or progress of the disease. Whereas most research projects in this field rely on phosphorylation-dependent tau-specific monoclonal antibodies (mAbs), the phosphorylation patterns recognized by these mAbs are often not characterized in detail. Therefore, we synthesized unphosphorylated, two monophosphorylated (pThr231, pSer235), and the bisphosphorylated (pThr231+pSer235) tau226-240 peptides. The phosphopeptides were ligated via an N-terminal cysteine to the thioester-activated C-terminus of human aldo/keto reductase AKR1A1. After purification by preparative gel electrophoresis, the ligation products were analyzed by Western blotting and probed with phosphorylation-dependent anti-tau mAbs HPT-101, HPT-103, HPT-104, and HPT-110. The obtained specificities were very similar to the data obtained by ELISA, showing that ELISA-based epitope mapping studies are also valid for immunoblot analyses.
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PMID:Mapping of phosphorylation-dependent anti-tau monoclonal antibodies in immunoblots using human tau-constructs synthesized by native chemical ligation. 1816 72