Probes for Transient Kinase Complexes

瞬时激酶复合物探针

基本信息

批准号：
7800495
负责人：
Benjamin P Warner
金额：
$ 9.89万
依托单位：
ICAGEN, INC.
依托单位国家：
美国
项目类别：
财政年份：
2010
资助国家：
美国
起止时间：
2010-03-01 至 2011-08-31
项目状态：
已结题

来源：
https://reporter.nih.gov/project-details/7800495
关键词：
Active Sites Behavior Binding Binding Sites Biological Assay Calcium Cancerous Cell physiology Cells Characteristics Chemicals Chronic Color Complex Crystallography Cysteine Data Edetic Acid Fluorescence Fluorescent Probes Goals Incubated Label Left Libraries Ligands Ligation MAP Kinase Gene MAPK1 gene MAPK14 gene Measurement Measures Metals Modification Molecular Nature Nuclear Pathway interactions Peptides Pharmacologic Substance Phase Phosphoric Monoester Hydrolases Phosphorus Phosphorylation Phosphotransferases Play Positioning Attribute Property Protein Isoforms Protein Kinase Protein Structure Initiative Protein-Serine-Threonine Kinases Proteins Protocols documentation Reading Relative (related person)Reporting Research Personnel Role Sales Sampling Scanning Screening procedure Structure Structure-Activity Relationship Substrate Specificity Sulfur System Technology Terbium Testing Tissues United States National Institutes of Health Work base cofactor commercialization design in vitro testing in vivo interest member prolylglycine protein complex public health relevance success

项目摘要

DESCRIPTION (provided by applicant): Most cellular processes are regulated by reversible protein phosphorylation, which is controlled by protein kinases and phosphatases. Caldera Pharmaceuticals and MedChem Partners propose to develop new probes for characterizing transient protein complexes. MAPK pathways play important roles in cellular differentiation and survival. MAPKs are serine/threonine protein kinases that can phoshorylate both cytoplasmic and nuclear targets. MAPKs are associated with aberrant, chronic or hyper-phosphorylation found in cancerous and other diseased tissues. MAPK complexes are difficult to characterize due to the transient nature of kinase-substrate binding interactions. PUBLIC HEALTH RELEVANCE: Caldera Pharmaceuticals and MedChem Partners propose to develop new probes for characterizing transient protein complexes. MAPK complexes are difficult to characterize due to the transient nature of kinase-substrate binding interactions.

描述（由申请人提供）：大多数细胞过程受到可逆蛋白磷酸化的调节，该蛋白质磷酸化受蛋白激酶和磷酸酶的控制。 Caldera Pharmaceuticals和Medchem Partners建议开发用于表征瞬时蛋白质复合物的新探针。 MAPK途径在细胞分化和存活中起着重要作用。 MAPK是丝氨酸/苏氨酸蛋白激酶，可以将细胞质和核靶标呈圆锥状。 MAPK与在癌性组织和其他患病组织中发现的异常，慢性或高磷酸化有关。由于激酶 - 基底结合相互作用的瞬时性质，MAPK复合物很难表征。公共卫生相关性：Caldera Pharmaceuticals和Medchem Partners建议开发用于表征瞬时蛋白质复合物的新探针。由于激酶 - 基底结合相互作用的瞬时性质，MAPK复合物很难表征。