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5 results about "SH3 domain" patented technology
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The SRC Homology 3 Domain (or SH3 domain) is a small protein domain of about 60 amino acid residues. Initially, SH3 was described as a conserved sequence in the viral adaptor protein v-Crk. This domain is also present in the molecules of phospholipase and several cytoplasmic tyrosine kinases such as Abl and Src. It has also been identified in several other protein families such as: PI3 Kinase, Ras GTPase-activating protein, CDC24 and cdc25. SH3 domains are found in proteins of signaling pathways regulating the cytoskeleton, the Ras protein, and the Src kinase and many others. The SH3 proteins interact with adaptor proteins and tyrosine kinases. Interacting with tyrosine kinases SH3 proteins usually bind far away from the active site. Approximately 300 SH3 domains are found in proteins encoded in the human genome. In addition to that, the SH3 domain was responsible for controlling protein-protein interactions in the signal transduction pathways and regulating the interactions of proteins involved in the cytoplasmic signaling.
SH3 domain derivatives
The present invention is directed to SH3 domain derivatives having a specific binding affinity to a target molecule. In this respect, the invention provides SH3 domain derivatives of nephrocystin (NPHP1) and the Tec kinase. The invention also provides a method for the production of a library comprising recombinant derivatives of NPHP1 or the Tec kinase SH3 domains and a method for selecting from the library one or more derivatives of the SH3 domain of nephrocystin (NPHP1) or the Tec kinase having a specific binding affinity to a target molecule.
Owner:NEXT BIOMED THERAPIES OY
A combination of axspa diagnostic biomarkers and its use in the assessment of the disease status of axspA
The application discloses an axSpA diagnosis biomarker combination and application thereof in judging axSpA diagnosis effect, relates to the biomedical field, and comprises the following four plasma proteins: LIM and SH3 domain protein 1 (LASP1), calponin binding protein 2 (CNN2), neuron protein kinase C and tyrosine protein kinase substrate 2 (PACSIN2) and tropomyosin 4 (TPM4). The expression levels of the four proteins in the plasma of axSpA light / severe group patients are all up-regulated relative to a healthy control group, and there is a significant difference between the severe group and the light group. Through deep proteomics, multi-algorithm statistics, machine learning models and independent queue immunological verification, the protein combination composed of LASP1, CNN2, PACSIN2 and TPM4 is first systematically identified and verified as an excellent performance of axSpA diagnosis biomarker.
Owner:ACADEMY OF MILITARY MEDICAL SCIENCES
Compound for treating thrombotic diseases
The present invention relates to a compound for treating thrombotic diseases. Specifically, the present invention provides a compound represented by formula I, or a pharmaceutically acceptable salt, or an enantiomer, or a diastereoisomer, or an atropisomer, or a racemate, or a polymorph, or a solvate, or an isotopically labeled derivative thereof. The compound disclosed in the present invention can be specifically combined with SH3 domain protein of Src kinase and then interfere the combination of integrin αIIbβ3 and Src kinase, so that outside-to-inside signal transduction is selectively inhibited and inside-to-outside signal transduction is not influenced; thus, while resisting thrombus, the compound of the present invention does not affect the normal physiological hemostatic function, prevents the occurrence of hemorrhagic side effect, and can be used as a new generation of effective medicine for preventing and treating thrombosis-related cardiovascular and cerebrovascular diseases.
Owner:SHANGHAI INSTITUTE OF MATERIA MEDICA CHINESE ACADEMY OF SCIENCES +2
A compound for treating thrombotic disorders
This invention relates to a compound for treating thrombotic diseases. Specifically, this invention provides a compound of Formula I, or a pharmaceutically acceptable salt thereof, or its enantiomer, diastereomer, transtransferase, racemic mixture, polymorph thereof, solvate thereof, or isotopically labeled derivative thereof. The compound of this invention specifically binds to the SH3 domain protein of Src kinase, interfering with the binding of integrin αIIbβ3 to Src kinase, thereby selectively inhibiting outward-to-inward signal transduction without affecting inward-to-outward signal transduction. This allows the compound of this invention to exert antithrombotic effects without affecting normal physiological hemostasis, avoiding bleeding side effects, and thus becoming a new generation of effective drugs for the prevention and treatment of thrombosis-related cardiovascular and cerebrovascular diseases.
Owner:SHANGHAI INSTITUTE OF MATERIA MEDICA CHINESE ACADEMY OF SCIENCES +2
A recombinant escherichia coli based on liquid-liquid phase separation, timing control and multi-enzyme dynamic assembly for synergistically improving the synthesis efficiency of beta-elemene and its application in the biosynthesis of beta-elemene
This invention discloses a recombinant *Escherichia coli* strain that synergistically enhances the synthesis efficiency of β-elemene based on liquid-liquid phase separation, temporal regulation, and dynamic multi-enzyme assembly, and its application in β-elemene biosynthesis. In the recombinant *E. coli* strain, a stable covalent dual-enzyme complex of IspA and GAS is first constructed using a SnoopTag / SnoopCatcher system, and the upstream key enzyme IDI is further introduced. Simultaneously, the RGGRGG repeat sequence, capable of forming membrane-free droplets, is used as a phase separation scaffold, with an SH3 ligand fused to its N-terminus. The SH3 domain is then linked to the C-terminus of both the IspA-GAS enzyme complex and IDI. Through the specific interaction of the SH3 ligand / SH3 domain, the key enzyme is directionally recruited and spatially enriched into the aggregates. A temporal regulation strategy is also introduced: the expression of the IspA-GAS enzyme complex and IDI is first induced by IPTG, followed by delayed induction of RGGRGG aggregate expression, thus recruiting the already formed enzyme complex into the aggregates. This invention not only reduces the amount of glycerol used and improves the glycerol conversion rate, but also increases the yield of β-elemene.
Owner:NANJING FORESTRY UNIV