Class Ib Phosphatidylinositol 3-Kinase
Phosphotransferases (Alcohol Group Acceptor)
Histocompatibility Antigens Class I
MAP Kinase Signaling System
Proto-Oncogene Proteins c-akt
Calcium-Calmodulin-Dependent Protein Kinases
Molecular Sequence Data
Protein Kinase C
Amino Acid Sequence
Mitogen-Activated Protein Kinase 1
p38 Mitogen-Activated Protein Kinases
Cyclic AMP-Dependent Protein Kinases
Ribosomal Protein S6 Kinases
Mitogen-Activated Protein Kinase Kinases
Mitogen-Activated Protein Kinase 3
Type C Phospholipases
Role of the cAMP and MAPK pathways in the transformation of mouse 3T3 fibroblasts by a TSHR gene constitutively activated by point mutation. (1/144)Constitutive activating mutations of the TSHR gene, have been detected in about 30 per cent of hyperfunctioning human thyroid adenomas and in a minority of differentiated thyroid carcinomas. The mutations activating the TSHR gene(s) in the thyroid carcinomas, were located at the codon 623 changing an Ala to a Ser (GCC-->TCC) or in codon 632 changing a Thr to Ala or Ile (ACC-->GCC or ACC-->ATC). In order to study if the constitutively activated TSHR gene(s) has played a role in the determination of the malignant phenotype presented by these tumors, we investigated: (1) the transforming capacity after transfection of mouse 3T3 cells, of a TSHR cDNA activated by an Ala-->Ser mutation in codon 623 or an Thr-->Ile mutation in codon 632 and (2) the pathway(s) eventually responsible(s) for the malignant phenotype of the cells transformed by these constitutively activated TSHR cDNAs. Our results show that (1) the TSHR(M623) or (M632) cDNAs give rise to 3T3 clones presenting a fully neoplastic phenotype (growth in agar and nude mouse tumorigenesis); this phenotype was weaker in the cells transformed by the 632 cDNA; (2) suggest that the fully transformed phenotype of our 3T3 cells, may be the consequence of the additive effect of the activation of at least two different pathways: the cAMP pathway through G(alpha)s and the Ras dependent MAPK pathway through G(beta)gamma and PI3K and (3) show that the PI3K isoform playing a key role as an effector in the MAPK pathway activation in our 3T3-transformed cells is PI3Kgamma. Signaling from PI3Kgamma to MAPK appears to require in our murine cellular system a tyrosine kinase (still not characterized), Shc, Grb2, Sos, Ras and Raf. It is proposed that the constitutively activated TSHR genes detected in the thyroid carcinomas, may have played an oncogenic role, participating in their development through these two pathways. (+info)
Up-regulation of endothelial nitric-oxide synthase promoter by the phosphatidylinositol 3-kinase gamma /Janus kinase 2/MEK-1-dependent pathway. (2/144)Our recent study indicates that lysophosphatidylcholine (LPC) enhances Sp1 binding and Sp1-dependent endothelial nitric oxide synthase (eNOS) promoter activity via the mitogen-activated protein kinase/extracellular signal-regulated kinase kinase 1 (MEK-1) signaling pathway (Cieslik, K., Lee, C.-M., Tang, J.-L., and Wu, K. K. (1999) J. Biol. Chem. 274, 34669-34675). To identify upstream signaling molecules, we transfected human endothelial cells with dominant negative and active mutants of Ras and evaluated their effects on eNOS promoter activity. Neither mutant altered the basal or LPC-induced eNOS promoter function. By contrast, a dominant negative mutant of phosphatidylinositol 3-kinase gamma (PI-3Kgamma) blocked the promoter activity induced by LPC. Wortmannin and LY 294002 had a similar effect. AG-490, a selective inhibitor of Janus kinase 2 (Jak2), also reduced the LPC-induced Sp1 binding and eNOS promoter activity to the basal level. LPC induced Jak2 phosphorylation, which was abolished by LY 294002 and the dominant negative mutant of PI-3Kgamma. LY 294002 and AG-490 abrogated MEK-1 phosphorylation induced by LPC but had no effect on Raf-1. These results indicate that PI-3Kgamma and Jak2 are essential for LPC-induced eNOS promoter activity. This signaling pathway was sensitive to pertussis toxin, suggesting the involvement of a G(i) protein in PI-3Kgamma activation. These results indicate that LPC enhances Sp1-dependent eNOS promoter activity by a pertussis toxin-sensitive, Ras-independent novel pathway, PI-3Kgamma/Jak2/MEK-1/ERK1/2. (+info)
Leukocytes navigate by compass: roles of PI3Kgamma and its lipid products. (3/144)Morphologic polarity is necessary for the motility of mammalian cells. In leukocytes responding to a chemoattractant, this polarity is regulated by activities of small Rho guanosine triphosphatases (Rho GTPases) and the phosphoinositide 3-kinases (PI3Ks). Moreover, in neutrophils, lipid products of PI3Ks appear to regulate activation of Rho GTPases, are required for cell motility and accumulate asymmetrically to the plasma membrane at the leading edge of polarized cells. By spatially regulating Rho GTPases and organizing the leading edge of the cell, PI3Ks and their lipid products could play pivotal roles not only in establishing leukocyte polarity but also as compass molecules that tell the cell where to crawl. (+info)
Crystal structure and functional analysis of Ras binding to its effector phosphoinositide 3-kinase gamma. (4/144)Ras activation of phosphoinositide 3-kinase (PI3K) is important for survival of transformed cells. We find that PI3Kgamma is strongly and directly activated by H-Ras G12V in vivo or by GTPgammaS-loaded H-Ras in vitro. We have determined a crystal structure of a PI3Kgamma/Ras.GMPPNP complex. A critical loop in the Ras binding domain positions Ras so that it uses its switch I and switch II regions to bind PI3Kgamma. Mutagenesis shows that interactions with both regions are essential for binding PI3Kgamma. Ras also forms a direct contact with the PI3Kgamma catalytic domain. These unique Ras/PI3Kgamma interactions are likely to be shared by PI3Kalpha. The complex with Ras shows a change in the PI3K conformation that may represent an allosteric component of Ras activation. (+info)
A specific role of phosphatidylinositol 3-kinase gamma. A regulation of autonomic Ca(2)+ oscillations in cardiac cells. (5/144)Purinergic stimulation of cardiomyocytes turns on a Src family tyrosine kinase-dependent pathway that stimulates PLCgamma and generates IP(3), a breakdown product of phosphatidylinositol 4,5-bisphosphate (PIP2). This signaling pathway closely regulates cardiac cell autonomic activity (i.e., spontaneous cell Ca(2+) spiking). PIP2 is phosphorylated on 3' by phosphoinositide 3-kinases (PI3Ks) that belong to a broad family of kinase isoforms. The product of PI3K, phosphatidylinositol 3,4,5-trisphosphate, regulates activity of PLCgamma. PI3Ks have emerged as crucial regulators of many cell functions including cell division, cell migration, cell secretion, and, via PLCgamma, Ca(2+) homeostasis. However, although PI3Kalpha and -beta have been shown to mediate specific cell functions in nonhematopoietic cells, such a role has not been found yet for PI3Kgamma. We report that neonatal rat cardiac cells in culture express PI3Kalpha, -beta, and -gamma. The purinergic agonist predominantly activates PI3Kgamma. Both wortmannin and LY294002 prevent tyrosine phosphorylation, and membrane translocation of PLCgamma as well as IP(3) generation in ATP-stimulated cells. Furthermore, an anti-PI3Kgamma, but not an anti-PI3Kbeta, injected in the cells prevents the effect of ATP on cell Ca(2+) spiking. A dominant negative mutant of PI3Kgamma transfected in the cells also exerts the same action. The effect of ATP was observed on spontaneous Ca(2+) spiking of wild-type but not of PI3Kgamma(2/2) embryonic stem cell-derived cardiomyocytes. ATP activates the Btk tyrosine kinase, Tec, and induces its association with PLCgamma. A dominant negative mutant of Tec blocks the purinergic effect on cell Ca(2+) spiking. Tec is translocated to the T-tubes upon ATP stimulation of cardiac cells. Both an anti-PI3Kgamma antibody and a dominant negative mutant of PI3Kgamma injected or transfected into cells prevent the latter event. We conclude that PI3Kgamma activation is a crucial step in the purinergic regulation of cardiac cell spontaneous Ca(2+) spiking. Our data further suggest that Tec works in concert with a Src family kinase and PI3Kgamma to fully activate PLCgamma in ATP-stimulated cardiac cells. This cluster of kinases provides the cardiomyocyte with a tight regulation of IP(3) generation and thus cardiac autonomic activity. (+info)
Expression, purification, characterization and homology modeling of active Akt/PKB, a key enzyme involved in cell survival signaling. (6/144)Akt is a serine/threonine kinase that plays a critical role in cell survival signaling and its activation has been linked to tumorigenesis. Up-regulation of Akt as well as its upstream regulator phosphatidylinositol-3 kinase (PI3K) has been found in many tumors and the negative regulator of this pathway PTEN/MMAC is a tumor suppressor. As a target for drug discovery, we have expressed and purified an active Akt1 enzyme from a recombinant baculovirus-infected Sf9 cell culture. Coexpression of Akt1 with the catalytic subunit of PI3K or treatment with okadaic acid during expression was found to generate an active enzyme in the insect cell culture system. We have optimized the kinase activity and developed a simple quantitative kinase assay using biotinylated peptide substrates. Using the purified active enzyme, we have characterized its physical, catalytic and kinetic properties. Since Akt is closely related to protein kinase C (PKC) and protein kinase A, the issue of obtaining selective inhibitors of this enzyme was addressed by comparison of the structures of catalytic domains of Akt and PKC, derived by homology modeling methods. A number of amino acid differences in the ATP binding regions of these kinases were identified, suggesting that selective inhibitors of Akt can be discovered. However, the ATP binding regions are highly conserved in the three isoforms of Akt implying that the discovery of isoform-selective inhibitors would be very challenging. (+info)
Phosphoinositide 3-kinase gamma mediates angiotensin II-induced stimulation of L-type calcium channels in vascular myocytes. (7/144)Previous results have shown that in rat portal vein myocytes the betagamma dimer of the G(13) protein transduces the angiotensin II-induced stimulation of calcium channels and increase in intracellular Ca(2+) concentration through activation of phosphoinositide 3-kinase (PI3K). In the present work we determined which class I PI3K isoforms were involved in this regulation. Western blot analysis indicated that rat portal vein myocytes expressed only PI3Kalpha and PI3Kgamma and no other class I PI3K isoforms. In the intracellular presence of an anti-p110gamma antibody infused by the patch clamp pipette, both angiotensin II- and Gbetagamma-mediated stimulation of Ca(2+) channel current were inhibited, whereas intracellular application of an anti-p110alpha antibody had no effect. The anti-PI3Kgamma antibody also inhibited the angiotensin II- and Gbetagamma-induced production of phosphatidylinositol 3,4,5-trisphosphate. In Indo-1 loaded cells, the angiotensin II-induced increase in [Ca(2+)](i) was inhibited by intracellular application of the anti-PI3Kgamma antibody, whereas the anti-PI3Kalpha antibody had no effect. The specificity of the anti-PI3Kgamma antibody used in functional experiments was ascertained by showing that this antibody did not recognize recombinant PI3Kalpha in Western blot experiments. Moreover, anti-PI3Kgamma antibody inhibited the stimulatory effect of intracellularly infused recombinant PI3Kgamma on Ca(2+) channel current without altering the effect of recombinant PI3Kalpha. Our results show that, although both PI3Kgamma and PI3Kalpha are expressed in vascular myocytes, the angiotensin II-induced stimulation of vascular L-type calcium channel and increase of [Ca(2+)](i) involves only the PI3Kgamma isoform. (+info)
Resistance to thromboembolism in PI3Kgamma-deficient mice. (8/144)Platelet aggregation and subsequent thrombosis are the major cause of ischemic diseases such as heart attack and stroke. ADP, acting via G protein-coupled receptors (GPCRs), is an important signal in thrombus formation and involves activation of phosphoinositide 3-kinases (PI3K). When platelets from mice lacking the G protein-activated PI3Kgamma isoform were stimulated with ADP, aggregation was impaired. Collagen or thrombin, however, evoked a normal response. ADP stimulation of PI3Kgamma-deficient platelets resulted in decreased PKB/Akt phosphorylation and alpha(IIb)beta(3) fibrinogen receptor activation. These effects did not influence bleeding time but protected PI3Kgamma-null mice from death caused by ADP-induced platelet-dependent thromboembolic vascular occlusion. This result demonstrates an unsuspected, well-defined role for PI3Kgamma downstream of ADP and suggests that pharmacological targeting of PI3Kgamma has a potential use as antithrombotic therapy. (+info)
Class I phosphatidylinositol 3-kinase (PI3K) is a family of enzymes that play a critical role in cellular signaling pathways. These enzymes phosphorylate the inositol ring of phosphatidylinositol lipids, leading to the production of second messengers that regulate various cellular processes, including cell growth, survival, and metabolism. Class I PI3K is composed of a catalytic subunit (p110) and a regulatory subunit (p85 or p105). The regulatory subunit binds to various upstream signaling molecules, such as receptor tyrosine kinases, G protein-coupled receptors, and integrins, and recruits the catalytic subunit to the plasma membrane. Once activated, the catalytic subunit phosphorylates phosphatidylinositol 4,5-bisphosphate (PIP2) to produce phosphatidylinositol 3,4,5-trisphosphate (PIP3), which serves as a docking site for various downstream effector molecules, including Akt, mTOR, and PKC. Abnormal activation of Class I PI3K signaling has been implicated in various human diseases, including cancer, diabetes, and neurological disorders. Therefore, inhibitors of Class I PI3K are being developed as potential therapeutic agents for these diseases.
Phosphatidylinositol 3-kinases (PI3Ks) are a family of enzymes that play a critical role in cellular signaling pathways. They are involved in a wide range of cellular processes, including cell growth, proliferation, differentiation, survival, migration, and metabolism. PI3Ks are activated by various extracellular signals, such as growth factors, hormones, and neurotransmitters, and they generate second messengers by phosphorylating phosphatidylinositol lipids on the inner leaflet of the plasma membrane. This leads to the recruitment and activation of downstream effector molecules, such as protein kinases and phosphatases, which regulate various cellular processes. Dysregulation of PI3K signaling has been implicated in the development of various diseases, including cancer, diabetes, and neurological disorders. Therefore, PI3Ks are important targets for the development of therapeutic agents for these diseases.
Phosphatidylinositol phosphates (PIPs) are a group of signaling molecules that play important roles in various cellular processes, including cell growth, differentiation, and metabolism. They are composed of a phosphatidylinositol (PI) backbone with one or more phosphate groups attached to the inositol ring. There are several different types of PIPs, including phosphatidylinositol 4-phosphate (PI(4)P), phosphatidylinositol 3-phosphate (PI(3)P), phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3). Each of these molecules has distinct functions and is involved in different signaling pathways. In the medical field, PIPs are of interest because they play important roles in various diseases, including cancer, diabetes, and neurodegenerative disorders. For example, PI(3)P and PI(3,4,5)P3 are key signaling molecules in the PI3K/Akt/mTOR pathway, which is often dysregulated in cancer. Similarly, PIPs are involved in insulin signaling and glucose metabolism, making them relevant to the treatment of diabetes. Overall, PIPs are important signaling molecules that play critical roles in cellular processes and are of interest in the medical field due to their involvement in various diseases.
1-Phosphatidylinositol 4-kinase (PI4K) is an enzyme that plays a crucial role in the biosynthesis of phosphatidylinositol 4-phosphate (PI4P), a phospholipid that is involved in various cellular processes such as vesicle trafficking, signal transduction, and membrane organization. PI4K is a family of enzymes that are encoded by multiple genes and are found in different cellular compartments, including the endoplasmic reticulum, Golgi apparatus, plasma membrane, and endosomes. Dysregulation of PI4K activity has been implicated in various diseases, including cancer, neurodegenerative disorders, and immune system dysfunction. Therefore, PI4K is an important target for the development of new therapeutic strategies.
Phosphatidylinositol 4,5-bisphosphate (PIP2) is a phospholipid that is a major component of the plasma membrane of cells. It is composed of a glycerol backbone, two fatty acid chains, and a phosphate group attached to the inositol ring. PIP2 plays a crucial role in many cellular processes, including cell signaling, membrane trafficking, and cytoskeletal organization. It is also involved in the regulation of ion channels and the activity of enzymes. In the medical field, PIP2 is of interest because it is involved in the development and progression of various diseases, including cancer, cardiovascular disease, and neurodegenerative disorders.
Phosphatidylinositols (PtdIns) are a class of lipids that are important signaling molecules in the cell membrane. They are composed of a glycerol backbone, two fatty acid chains, and a phosphate group attached to the third carbon of the glycerol molecule. There are several different types of PtdIns, each with a unique structure and function. In the medical field, PtdIns play a crucial role in various cellular processes, including cell growth, differentiation, and apoptosis (programmed cell death). They are also involved in the regulation of the immune system, insulin signaling, and the development of cancer. PtdIns are often used as markers for various diseases, including cancer, cardiovascular disease, and neurological disorders. They are also used as targets for drug development, as they play a key role in many cellular signaling pathways. Overall, PtdIns are an important class of lipids that play a critical role in many cellular processes and are the subject of ongoing research in the medical field.
Protein-Serine-Threonine Kinases (PSTKs) are a family of enzymes that play a crucial role in regulating various cellular processes, including cell growth, differentiation, metabolism, and apoptosis. These enzymes phosphorylate specific amino acids, such as serine and threonine, on target proteins, thereby altering their activity, stability, or localization within the cell. PSTKs are involved in a wide range of diseases, including cancer, diabetes, cardiovascular disease, and neurodegenerative disorders. Therefore, understanding the function and regulation of PSTKs is important for developing new therapeutic strategies for these diseases.
Histocompatibility antigens class I (HLA class I) are a group of proteins found on the surface of almost all cells in the human body. These proteins play a crucial role in the immune system by presenting pieces of foreign substances, such as viruses or bacteria, to immune cells called T cells. HLA class I antigens are encoded by a group of genes located on chromosome 6. There are several different HLA class I antigens, each with a unique structure and function. The specific HLA class I antigens present on a person's cells can affect their susceptibility to certain diseases, including autoimmune disorders, infectious diseases, and cancer. In the context of transplantation, HLA class I antigens are important because they can trigger an immune response if the donor tissue is not a close match to the recipient's own tissue. This immune response, known as rejection, can lead to the rejection of the transplanted tissue or organ. Therefore, matching HLA class I antigens between the donor and recipient is an important consideration in transplantation.
Chromones are a class of organic compounds that contain a chromene ring structure. They are found in a variety of plants and have been shown to have a range of biological activities, including anti-inflammatory, antioxidant, and anticancer properties. In the medical field, chromones are of interest as potential therapeutic agents for the treatment of various diseases and conditions. Some examples of chromones that have been studied for their medicinal properties include quercetin, fisetin, and kaempferol. These compounds are often found in fruits, vegetables, and other plant-based foods and may be used as dietary supplements or incorporated into pharmaceuticals.
Androstadienes are a group of organic compounds that are derived from testosterone, a hormone produced by the testes in males. They are characterized by a six-membered ring structure with two double bonds, and are classified as a type of androgen. Androstadienes are found in a variety of plants, including yams, potatoes, and soybeans, and are also synthesized by the human body. In the medical field, androstadienes are sometimes used as a treatment for conditions such as prostate cancer and erectile dysfunction. They are also being studied for their potential use in the development of new drugs for the treatment of other diseases.
Protein kinases are enzymes that catalyze the transfer of a phosphate group from ATP (adenosine triphosphate) to specific amino acid residues on proteins. This process, known as phosphorylation, can alter the activity, localization, or stability of the target protein, and is a key mechanism for regulating many cellular processes, including cell growth, differentiation, metabolism, and signaling pathways. Protein kinases are classified into different families based on their sequence, structure, and substrate specificity. Some of the major families of protein kinases include serine/threonine kinases, tyrosine kinases, and dual-specificity kinases. Each family has its own unique functions and roles in cellular signaling. In the medical field, protein kinases are important targets for the development of drugs for the treatment of various diseases, including cancer, diabetes, and cardiovascular disease. Many cancer drugs target specific protein kinases that are overactive in cancer cells, while drugs for diabetes and cardiovascular disease often target kinases involved in glucose metabolism and blood vessel function, respectively.
Phosphatidylinositol 3-kinase (PI3K) is a family of enzymes that play a crucial role in cellular signaling pathways. PI3Ks are involved in a wide range of cellular processes, including cell growth, proliferation, survival, migration, and metabolism. In the medical field, PI3Ks are of particular interest because they are often dysregulated in various diseases, including cancer, diabetes, and cardiovascular disease. In cancer, for example, mutations in PI3K genes or overexpression of PI3K enzymes can lead to uncontrolled cell growth and proliferation, contributing to tumor development and progression. Therefore, PI3K inhibitors are being developed as potential therapeutic agents for the treatment of various cancers. These inhibitors target the activity of PI3K enzymes, thereby disrupting the signaling pathways that promote cancer cell growth and survival. Additionally, PI3K inhibitors are also being investigated for their potential to treat other diseases, such as diabetes and cardiovascular disease.
Morpholines are a class of organic compounds that contain a six-membered ring with four carbon atoms and two nitrogen atoms. They are often used as intermediates in the synthesis of various pharmaceuticals and other chemicals. In the medical field, morpholines have been studied for their potential use as antiviral, antifungal, and anti-inflammatory agents. Some specific examples of morpholine-based drugs that have been developed for medical use include the antiviral drug ribavirin and the antipsychotic drug risperidone.
Proto-oncogene proteins c-akt, also known as protein kinase B (PKB), is a serine/threonine kinase that plays a critical role in various cellular processes, including cell survival, proliferation, and metabolism. It is a member of the Akt family of kinases, which are activated by various growth factors and cytokines. In the context of cancer, c-akt has been shown to be frequently activated in many types of tumors and is often associated with poor prognosis. Activation of c-akt can lead to increased cell survival and resistance to apoptosis, which can contribute to tumor growth and progression. Additionally, c-akt has been implicated in the regulation of angiogenesis, invasion, and metastasis, further contributing to the development and progression of cancer. Therefore, the study of c-akt and its role in cancer has become an important area of research in the medical field, with the goal of developing targeted therapies to inhibit its activity and potentially treat cancer.
Calcium-calmodulin-dependent protein kinases (CaMKs) are a family of enzymes that play a crucial role in regulating various cellular processes in response to changes in intracellular calcium levels. These enzymes are activated by the binding of calcium ions to a regulatory protein called calmodulin, which then binds to and activates the CaMK. CaMKs are involved in a wide range of cellular functions, including muscle contraction, neurotransmitter release, gene expression, and cell division. They are also involved in the regulation of various diseases, including heart disease, neurological disorders, and cancer. In the medical field, CaMKs are the target of several drugs, including those used to treat heart disease and neurological disorders. For example, calcium channel blockers, which are used to treat high blood pressure and chest pain, can also block the activity of CaMKs. Similarly, drugs that target CaMKs are being developed as potential treatments for neurological disorders such as Alzheimer's disease and Parkinson's disease.
Ribonucleotide reductases (RNRs) are a family of enzymes that play a critical role in the biosynthesis of deoxyribonucleotides (dNTPs), which are the building blocks of DNA. RNRs catalyze the conversion of ribonucleotides (rNTPs) to their deoxyribonucleotide counterparts (dNTPs) by removing a phosphate group and reducing the ribose sugar to the deoxyribose form. There are two classes of RNRs: class I and class II. Class I RNRs are found in all organisms and are composed of two subunits: a large subunit (R1) and a small subunit (R2). Class II RNRs are found only in eukaryotes and are composed of four subunits: a large subunit (R1), a small subunit (R2), a third subunit (R3), and a fourth subunit (R4). RNRs are essential for DNA replication and repair, and mutations in the genes encoding RNRs can lead to various diseases, including cancer. In addition, RNRs are also important targets for the development of antiviral and antitumor drugs.
In the medical field, "src-family kinases" (SFKs) refer to a group of non-receptor tyrosine kinases that are involved in a variety of cellular processes, including cell growth, differentiation, migration, and survival. SFKs are activated by a variety of stimuli, including growth factors, cytokines, and hormones, and they play a critical role in regulating cell signaling pathways. SFKs are a subfamily of the larger tyrosine kinase family, which includes over 90 different kinases that are involved in a wide range of cellular processes. SFKs are characterized by their unique domain structure, which includes an N-terminal myristoylation site, a src homology 2 (SH2) domain, and a src homology 3 (SH3) domain. SFKs are involved in a variety of diseases, including cancer, cardiovascular disease, and inflammatory disorders. In cancer, SFKs are often overexpressed or activated, leading to uncontrolled cell growth and proliferation. In cardiovascular disease, SFKs are involved in the regulation of blood vessel function and the development of atherosclerosis. In inflammatory disorders, SFKs play a role in the activation of immune cells and the production of inflammatory mediators. Overall, SFKs are an important group of kinases that play a critical role in regulating cellular signaling pathways and are involved in a variety of diseases.
Protein kinase C (PKC) is a family of enzymes that play a crucial role in various cellular processes, including cell growth, differentiation, and apoptosis. In the medical field, PKC is often studied in relation to its involvement in various diseases, including cancer, cardiovascular disease, and neurodegenerative disorders. PKC enzymes are activated by the binding of diacylglycerol (DAG) and calcium ions, which leads to the phosphorylation of target proteins. This phosphorylation can alter the activity, localization, or stability of the target proteins, leading to changes in cellular signaling pathways. PKC enzymes are divided into several subfamilies based on their structure and activation mechanisms. The different subfamilies have distinct roles in cellular signaling and are involved in different diseases. For example, some PKC subfamilies are associated with cancer progression, while others are involved in the regulation of the immune system. Overall, PKC enzymes are an important area of research in the medical field, as they have the potential to be targeted for the development of new therapeutic strategies for various diseases.
HLA-G antigens are a group of non-classical human leukocyte antigen (HLA) molecules that are expressed on the surface of certain cells, including trophoblasts, placental cells, and some immune cells. These antigens play a role in regulating the immune response during pregnancy and may also be involved in other immune-related processes. HLA-G antigens are characterized by a unique structure and a distinct pattern of expression compared to classical HLA molecules. They are thought to play a role in protecting the developing fetus from the mother's immune system, as well as in regulating the immune response in other contexts. Abnormal expression or function of HLA-G antigens has been associated with a number of medical conditions, including recurrent miscarriage, preeclampsia, and certain autoimmune diseases.
Mexiletine is a medication that is primarily used to treat certain types of irregular heartbeats, such as atrial fibrillation and ventricular tachycardia. It works by blocking the sodium channels in the heart's cells, which helps to regulate the heartbeat and prevent abnormal rhythms. Mexiletine is also sometimes used to treat chronic pain, although it is not as effective as other pain medications and can cause side effects such as dizziness, nausea, and tremors. It is usually taken by mouth in the form of tablets or capsules.
In the medical field, an amino acid sequence refers to the linear order of amino acids in a protein molecule. Proteins are made up of chains of amino acids, and the specific sequence of these amino acids determines the protein's structure and function. The amino acid sequence is determined by the genetic code, which is a set of rules that specifies how the sequence of nucleotides in DNA is translated into the sequence of amino acids in a protein. Each amino acid is represented by a three-letter code, and the sequence of these codes is the amino acid sequence of the protein. The amino acid sequence is important because it determines the protein's three-dimensional structure, which in turn determines its function. Small changes in the amino acid sequence can have significant effects on the protein's structure and function, and this can lead to diseases or disorders. For example, mutations in the amino acid sequence of a protein involved in blood clotting can lead to bleeding disorders.
Proto-oncogenes are normal genes that are involved in regulating cell growth and division. When these genes are mutated or overexpressed, they can become oncogenes, which can lead to the development of cancer. Proto-oncogenes are also known as proto-oncogene proteins.
In the medical field, a cell line refers to a group of cells that have been derived from a single parent cell and have the ability to divide and grow indefinitely in culture. These cells are typically grown in a laboratory setting and are used for research purposes, such as studying the effects of drugs or investigating the underlying mechanisms of diseases. Cell lines are often derived from cancerous cells, as these cells tend to divide and grow more rapidly than normal cells. However, they can also be derived from normal cells, such as fibroblasts or epithelial cells. Cell lines are characterized by their unique genetic makeup, which can be used to identify them and compare them to other cell lines. Because cell lines can be grown in large quantities and are relatively easy to maintain, they are a valuable tool in medical research. They allow researchers to study the effects of drugs and other treatments on specific cell types, and to investigate the underlying mechanisms of diseases at the cellular level.
Mitogen-Activated Protein Kinase 1 (MAPK1), also known as Extracellular Signal-regulated Kinase 1 (ERK1), is a protein kinase enzyme that plays a crucial role in cellular signaling pathways. It is part of the mitogen-activated protein kinase (MAPK) family, which is involved in regulating various cellular processes such as cell proliferation, differentiation, survival, and apoptosis. MAPK1 is activated by a variety of extracellular signals, including growth factors, cytokines, and hormones, and it transduces these signals into the cell by phosphorylating and activating downstream target proteins. These target proteins include transcription factors, cytoskeletal proteins, and enzymes involved in metabolism. In the medical field, MAPK1 is of interest because it is involved in the development and progression of many diseases, including cancer, inflammatory disorders, and neurological disorders. For example, mutations in the MAPK1 gene have been associated with various types of cancer, including breast cancer, colon cancer, and glioblastoma. In addition, MAPK1 has been implicated in the pathogenesis of inflammatory diseases such as rheumatoid arthritis and psoriasis, as well as neurological disorders such as Alzheimer's disease and Parkinson's disease. Therefore, understanding the role of MAPK1 in cellular signaling pathways and its involvement in various diseases is important for the development of new therapeutic strategies for these conditions.
P38 Mitogen-Activated Protein Kinases (MAPKs) are a family of serine/threonine protein kinases that play a crucial role in regulating various cellular processes, including cell proliferation, differentiation, survival, and apoptosis. They are activated by a variety of extracellular stimuli, such as cytokines, growth factors, and stress signals, and are involved in the regulation of inflammation, immune responses, and metabolic processes. In the medical field, p38 MAPKs have been implicated in the pathogenesis of various diseases, including cancer, inflammatory disorders, and neurodegenerative diseases. Targeting p38 MAPKs with small molecule inhibitors or other therapeutic agents has been proposed as a potential strategy for the treatment of these diseases. However, further research is needed to fully understand the role of p38 MAPKs in disease pathogenesis and to develop effective therapeutic interventions.
Protein-tyrosine kinases (PTKs) are a family of enzymes that play a crucial role in various cellular processes, including cell growth, differentiation, metabolism, and signal transduction. These enzymes catalyze the transfer of a phosphate group from ATP to the hydroxyl group of tyrosine residues on specific target proteins, thereby modifying their activity, localization, or interactions with other molecules. PTKs are involved in many diseases, including cancer, cardiovascular disease, and neurological disorders. They are also targets for many drugs, including those used to treat cancer and other diseases. In the medical field, PTKs are studied to understand their role in disease pathogenesis and to develop new therapeutic strategies.
Cyclic AMP-dependent protein kinases (also known as cAMP-dependent protein kinases or PKA) are a family of enzymes that play a crucial role in regulating various cellular processes in the body. These enzymes are activated by the presence of cyclic AMP (cAMP), a second messenger molecule that is produced in response to various stimuli, such as hormones, neurotransmitters, and growth factors. PKA is a heterotetrameric enzyme composed of two regulatory subunits and two catalytic subunits. The regulatory subunits bind to cAMP and prevent the catalytic subunits from phosphorylating their target proteins. When cAMP levels rise, the regulatory subunits are activated and release the catalytic subunits, allowing them to phosphorylate their target proteins. PKA is involved in a wide range of cellular processes, including metabolism, gene expression, cell proliferation, and differentiation. It phosphorylates various proteins, including enzymes, transcription factors, and ion channels, leading to changes in their activity and function. In the medical field, PKA plays a critical role in various diseases and disorders, including cancer, diabetes, and cardiovascular disease. For example, PKA is involved in the regulation of insulin secretion in pancreatic beta cells, and its dysfunction has been implicated in the development of type 2 diabetes. PKA is also involved in the regulation of blood pressure and heart function, and its dysfunction has been linked to the development of hypertension and heart disease.
Ribosomal Protein S6 Kinases (S6Ks) are a family of protein kinases that play a crucial role in regulating cell growth, proliferation, and survival. They are activated by the PI3K/Akt signaling pathway, which is a key regulator of cellular metabolism and growth. In the context of the medical field, S6Ks have been implicated in various diseases, including cancer, diabetes, and neurodegenerative disorders. For example, the activation of S6Ks has been shown to promote the growth and survival of cancer cells, making them a potential target for cancer therapy. In addition, dysregulation of S6Ks has been linked to insulin resistance and the development of type 2 diabetes. Overall, the study of S6Ks has important implications for the understanding and treatment of a wide range of diseases, and ongoing research in this area is likely to yield new insights and therapeutic strategies in the future.
Mitogen-Activated Protein Kinase Kinases (MAPKKs), also known as Mitogen-Activated Protein Kinase Activators (MAPKAs), are a family of enzymes that play a crucial role in regulating various cellular processes, including cell proliferation, differentiation, survival, and apoptosis. MAPKKs are responsible for activating Mitogen-Activated Protein Kinases (MAPKs), which are a group of serine/threonine kinases that transmit signals from the cell surface to the nucleus. MAPKKs are activated by various extracellular signals, such as growth factors, cytokines, and hormones, and they in turn activate MAPKs by phosphorylating them on specific residues. MAPKKs are involved in a wide range of cellular processes, including cell cycle progression, differentiation, and apoptosis. They are also involved in the regulation of inflammation, immune responses, and cancer development. Dysregulation of MAPKK signaling has been implicated in various diseases, including cancer, autoimmune disorders, and neurodegenerative diseases. In the medical field, MAPKKs are being studied as potential therapeutic targets for the treatment of various diseases. For example, inhibitors of MAPKKs are being developed as potential anti-cancer agents, as they can block the activation of MAPKs and prevent cancer cell proliferation and survival. Additionally, MAPKKs are being studied as potential targets for the treatment of inflammatory and autoimmune disorders, as they play a key role in regulating immune responses.
Mitogen-Activated Protein Kinase 3 (MAPK3), also known as extracellular signal-regulated kinase 1 (ERK1), is a protein kinase enzyme that plays a crucial role in cellular signaling pathways. It is part of the mitogen-activated protein kinase (MAPK) family, which is involved in regulating various cellular processes such as cell proliferation, differentiation, survival, and apoptosis. MAPK3 is activated by a variety of extracellular signals, including growth factors, cytokines, and hormones, and it transduces these signals into the cell by phosphorylating and activating downstream target proteins. These target proteins include transcription factors, cytoskeletal proteins, and enzymes involved in metabolism. In the medical field, MAPK3 is of interest because it has been implicated in the development and progression of various diseases, including cancer, neurodegenerative disorders, and inflammatory diseases. For example, dysregulation of MAPK3 signaling has been observed in many types of cancer, and targeting this pathway has been proposed as a potential therapeutic strategy. Additionally, MAPK3 has been shown to play a role in the pathogenesis of conditions such as Alzheimer's disease and Parkinson's disease, as well as in the regulation of immune responses and inflammation.
In the medical field, "Cells, Cultured" refers to cells that have been grown and maintained in a controlled environment outside of their natural biological context, typically in a laboratory setting. This process is known as cell culture and involves the isolation of cells from a tissue or organism, followed by their growth and proliferation in a nutrient-rich medium. Cultured cells can be derived from a variety of sources, including human or animal tissues, and can be used for a wide range of applications in medicine and research. For example, cultured cells can be used to study the behavior and function of specific cell types, to develop new drugs and therapies, and to test the safety and efficacy of medical products. Cultured cells can be grown in various types of containers, such as flasks or Petri dishes, and can be maintained at different temperatures and humidity levels to optimize their growth and survival. The medium used to culture cells typically contains a combination of nutrients, growth factors, and other substances that support cell growth and proliferation. Overall, the use of cultured cells has revolutionized medical research and has led to many important discoveries and advancements in the field of medicine.
Type C phospholipases are a family of enzymes that hydrolyze phospholipids, which are important components of cell membranes. These enzymes are characterized by the presence of a catalytic cysteine residue in their active site, which is involved in the hydrolysis of the phospholipid substrate. Type C phospholipases are involved in a variety of cellular processes, including signal transduction, membrane trafficking, and cell growth and differentiation. They are also involved in the pathogenesis of several diseases, including cancer, neurodegenerative disorders, and inflammatory diseases. There are several subtypes of type C phospholipases, including phospholipase C (PLC), which hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to produce inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG), and phospholipase D (PLD), which hydrolyzes phosphatidylcholine (PC) to produce phosphatidic acid (PA) and choline.
Tyrosine is an amino acid that is essential for the production of certain hormones, neurotransmitters, and other important molecules in the body. It is a non-essential amino acid, which means that it can be synthesized by the body from other amino acids or from dietary sources. In the medical field, tyrosine is often used as a dietary supplement to support the production of certain hormones and neurotransmitters, particularly dopamine and norepinephrine. These hormones play important roles in regulating mood, motivation, and other aspects of brain function. Tyrosine is also used in the treatment of certain medical conditions, such as phenylketonuria (PKU), a genetic disorder that affects the metabolism of phenylalanine, another amino acid. In PKU, tyrosine supplementation can help to prevent the buildup of toxic levels of phenylalanine in the body. In addition, tyrosine has been studied for its potential benefits in the treatment of other conditions, such as depression, anxiety, and fatigue. However, more research is needed to confirm these potential benefits and to determine the optimal dosage and duration of tyrosine supplementation.
In the medical field, isoenzymes refer to different forms of enzymes that have the same chemical structure and catalytic activity, but differ in their amino acid sequence. These differences can arise due to genetic variations or post-translational modifications, such as phosphorylation or glycosylation. Isoenzymes are often used in medical diagnosis and treatment because they can provide information about the function and health of specific organs or tissues. For example, the presence of certain isoenzymes in the blood can indicate liver or kidney disease, while changes in the levels of specific isoenzymes in the brain can be indicative of neurological disorders. In addition, isoenzymes can be used as biomarkers for certain diseases or conditions, and can be targeted for therapeutic intervention. For example, drugs that inhibit specific isoenzymes can be used to treat certain types of cancer or heart disease.
JNK Mitogen-Activated Protein Kinases (JNK MAPKs) are a family of serine/threonine protein kinases that play a crucial role in cellular signaling pathways. They are activated in response to various cellular stresses, including oxidative stress, UV radiation, and cytokines. JNK MAPKs are involved in the regulation of cell proliferation, differentiation, and apoptosis, as well as the inflammatory response. Dysregulation of JNK MAPK signaling has been implicated in a variety of diseases, including cancer, neurodegenerative disorders, and inflammatory diseases. Therefore, JNK MAPKs are an important target for the development of new therapeutic strategies.
Insulin-like growth factor 1 receptor
Thomas P. Stossel
DeCS 2020 - June 23, 2020 version
China's PI3K Inhibitors Have Made New Progress Since the Approval of Bayer's Copanlisib - Chiatai Tianqing's TQ-B3525 Is...
DeCS 2019 - June 12, 2019 version
DeCS 2018 - July 31, 2018 version
DeCS 2017 - July 04, 2017 version
DeCS 2018 - July 31, 2018 version
Volume 131 Issue 1 | Acta Haematologica | Karger Publishers
positive regulation of nitric oxide biosynthetic process - Ontology Report - Rat Genome Database
Results for cd05175
Endocytosis in the adaptation to cellular stress
Beating 'Guangdong cancer': a review and update on nasopharyngeal cancer | HKMJ
Non-Hodgkin Lymphoma (NHL): Practice Essentials, Background, Pathophysiology
Pesquisa | Portal Regional da BVS
Molecular Medicine of Rheumatoid Arthritis: From Molecular Pathphysiology to Novel Therapeutics and Evidence-Based Practice
Platelet Disorders: Overview of Platelet Disorders, Pathophysiology of Platelet Disorders, Autoimmune Thrombocytopenias
Antiangiogenic therapy for breast cancer | Breast Cancer Research | Full Text
Corticotropin-Releasing Factor2 Receptors - How NF-B is activated: the role of the IB kinase (IKK) complex
Biomedicines | Free Full-Text | Association between Immunosuppressive Therapy Utilized in the Treatment of Autoimmune Disease...
August | 2013 | Deubiquitinase
GSE22886 IGM MEMORY BCELL VS BM PLASMA CELL DN
NEW (2008) DeCS DESCRIPTORS WITH SCOPE NOTES (UNIT RECORD FORMAT; 21/02/2008
NEW (2008) DeCS DESCRIPTORS WITH SCOPE NOTES (UNIT RECORD FORMAT; 21/02/2008
NEW (2008) DeCS DESCRIPTORS WITH SCOPE NOTES (UNIT RECORD FORMAT; 21/02/2008
Cancer Therapeutics & Host Response Program Co-Leaders » Cancer Center » UF Health Cancer Center » University of Florida
Effect of the Insulin Mimetic L-783,281 on Intracellular [Ca2+] and Insulin Secretion From Pancreatic β-Cells | Diabetes |...
TGFBR1 transforming growth factor beta receptor 1 [Homo sapiens (human)] - Gene - NCBI
SMART: LIM domain annotation
Magi-1c | Journal of Cell Biology | Rockefeller University Press
Tyrosine kinase activity1
- Small molecular inhibitors of VEGF tyrosine kinase activity, such as sorafenib, appear promising. (biomedcentral.com)
- The PI3K family is divided into four different classes: Class I, Class II, Class III, and Class IV. (wikipedia.org)
- The PI3K is activated by G protein-coupled receptors and tyrosine kinase receptors. (wikipedia.org)
- TQ-B3525 is a new phosphatidyl inositol 3-kinase (PI3K) α/δ dual inhibitor developed by Chiatai Tianqing, which inhibits the expression of PI3K protein and reduces AKT protein phosphorylation levels to induce cell apoptosis and then inhibit the proliferation of malignant tumor cells. (pharmasources.com)
- PI3K (full name: phosphatidyl inositol 3-kinase) is an intracellular lipid phosphokinase composed of the p85 regulatory subunit, p55 regulatory subunit, and p110 catalytic subunit. (pharmasources.com)
- Based on the different structures and substrates, PI3K can be divided into class I, class II, and class III. (pharmasources.com)
- Class I PI3K is a heterodimer composed of PI3K catalytic subunits and regulatory subunits, which is currently the most deeply and extensively studied subtype and has the closest relationship with tumors. (pharmasources.com)
- Class I PI3K can be further divided into class IA and class IB by the catalytic subunits. (pharmasources.com)
- The catalytic subunits in class IA PI3K include three proteins, i.e., p110α, p110β, and p110δ, while class IB PI3K only contains the p110γ catalytic subunit. (pharmasources.com)
- Class IA PI3K is closely related to the occurrence and development of tumors, among which PIK3CA, the gene that compiles PI3Kα, is the most common mutation in tumors. (pharmasources.com)
- PI3K is a key regulatory kinase in the PI3K/AKT/mTOR signaling pathway, which is involved in regulating cell proliferation, differentiation, apoptosis, and angiogenesis. (pharmasources.com)
- The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases. (umbc.edu)
- Class IA enzymes contain an N-terminal p85 binding domain, a Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, and a C-terminal ATP-binding cataytic domain. (umbc.edu)
- The encoded protein is a serine/threonine protein kinase. (nih.gov)
- Nurden provides reported that platelet glycoprotein dysfunction and signaling defects might occur in myeloproliferative neoplasms (MPNs), including CML . (cancercurehere.com)
- This is corroborated from the observation that utilizing tyrosine kinase inhibitors H 89 dihydrochloride irreversible inhibition for use in individuals with CML could improve platelet dysfunction . (cancercurehere.com)
- glycoprotein Ib platelet subu. (gsea-msigdb.org)
- It is composed of ataxia telangiectasia mutated (ATM), ataxia telangiectasia and Rad3 related (ATR), DNA-dependent protein kinase (DNA-PK) and mammalian target of rapamycin (mTOR). (wikipedia.org)
- This review focusses on clinical aspects of treatment of breast cancer with monoclonal antibodies, and tyrosine kinase and mammalian target of rapamycin (mTOR) inhibitors. (biomedcentral.com)
- Additional focus will be placed on the main classes of immune inhibitor therapy utilized in transplant patients and in autoimmune disease including TNF-alpha, Calcineurin, mTOR, purine synthesis antagonists and IMPDH inhibitors. (mdpi.com)
- Moreover, these studies confirmed several important observations: the inhibitor binding site exists only following the 3 control of vDNA and the hydrophobic tail binds within the hydrophobic pocket formed mostly from the flexible active site loop. (deubiquitinase.com)
- Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. (umbc.edu)
- Class III seems to be primarily involved in the trafficking of proteins and vesicles. (wikipedia.org)
- L-783,281-induced activation of IRTK stimulates downstream signaling proteins, including insulin receptor substrate 1 (IRS-1), Akt, and phosphatidylinositol 3-kinase (PI3-K). L-783,281 also induces glucose uptake in a dose-dependent manner from rat primary adipocytes and soleus muscle tissue from lean mice. (diabetesjournals.org)
- LIM domains coordinate one or more zinc atoms, and are named after the three proteins (LIN-11, Isl1 and MEC-3) in which they were first found. (embl.de)
- 0.05) of control values by the phosphatidylinositol 3-kinase (PI3-K) inhibitors LY294002 (25 μmol/l) and wortmannin (100 nmol/l), respectively. (diabetesjournals.org)
- Phosphoinositide 3-kinases (PI3Ks), also called phosphatidylinositol 3-kinases, are a family of enzymes involved in cellular functions such as cell growth, proliferation, differentiation, motility, survival and intracellular trafficking, which in turn are involved in cancer. (wikipedia.org)
- The discovery of PI3Ks by Lewis Cantley and colleagues began with their identification of a previously unknown phosphoinositide kinase associated with the polyoma middle T protein. (wikipedia.org)
- They observed unique substrate specificity and chromatographic properties of the products of the lipid kinase, leading to the discovery that this phosphoinositide kinase had the unprecedented ability to phosphorylate phosphoinositides on the 3' position of the inositol ring. (wikipedia.org)
- Subsequently, Cantley and colleagues demonstrated that in vivo the enzyme prefers PtdIns(4,5)P2 as a substrate, producing the novel phosphoinositide PtdIns(3,4,5)P3 previously identified in neutrophils. (wikipedia.org)
- This compound stimulates insulin receptor tyrosine kinase (IRTK) activity in CHO cells that overexpress human insulin receptors by binding to the β-subunit of the insulin receptor ( 1 ). (diabetesjournals.org)
- Class IA PI3Ks are composed of a heterodimer between a p110 catalytic subunit and a shorter regulatory subunit (often p85). (wikipedia.org)
- The regulatory p101 and catalytic p110γ subunits comprise the class IB PI3Ks and are encoded by a single gene each (Pik3cg for p110γ and Pik3r5 for p101). (wikipedia.org)
- PI3Ks are a family of related intracellular signal transducer enzymes capable of phosphorylating the 3 position hydroxyl group of the inositol ring of phosphatidylinositol (PtdIns). (wikipedia.org)
- PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. (umbc.edu)
- Methods of making the same, and methods for using the same in the treatment of cancer, autoimmune, inflammatory and other Pim kinase-associated diseases, disorders or conditions are also disclosed. (justia.com)
- Class I PI3Ks catalyze the conversion of phosphatidylinositol (4,5)-bisphosphate (PI(4,5)P2) into phosphatidylinositol (3,4,5)-trisphosphate (PI(3,4,5)P3) in vivo. (wikipedia.org)
- Class III PI3Ks produce only PI(3)P from PI but are more similar to Class I in structure, as they exist as heterodimers of a catalytic (Vps34) and a regulatory (Vps15/p150) subunits. (wikipedia.org)
- Class I PI3Ks are the only enzymes capable of converting PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. (umbc.edu)
- A group of more distantly related enzymes is sometimes referred to as class IV PI3Ks. (wikipedia.org)
- The SH2 domains bind preferentially to phosphorylated tyrosine residues in the amino acid sequence context Y-X-X-M. Class II and III PI3Ks are differentiated from the Class I by their structure and function. (wikipedia.org)
- The distinct feature of Class II PI3Ks is the C-terminal C2 domain. (wikipedia.org)
- This domain lacks critical Asp residues to coordinate binding of Ca2+, which suggests class II PI3Ks bind lipids in a Ca2+-independent manner. (wikipedia.org)
- Platelets play a primary role in this process, interacting with subendothelium-bound von Willebrand factor (vWf) via the membrane glycoprotein (GP) Ib complex. (medscape.com)
- PI(3,4)P2 has, however, been shown to play a role in the invagination phase of clathrin-mediated endocytosis. (wikipedia.org)
- They are further classified into class IA (alpha, beta and delta) and IB (gamma). (umbc.edu)
- Description: A sandwich quantitative ELISA assay kit for detection of Human Casein Kinase 1 Delta (CSNK1d) in samples from tissue homogenates or other biological fluids. (1elisakits.com)
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Casein Kinase 1 Delta (CSNK1d) in Tissue homogenates and other biological fluids. (1elisakits.com)
- Description: A sandwich ELISA kit for detection of Casein Kinase 1 Delta from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (1elisakits.com)
- They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. (embl.de)
- On May 25, the CDE official website revealed that the marketing application for the first-in-class 'TQ-B3525 tablets' by Chiatai Tianqing was proposed to be included in the priority review for the treatment of recurrent or refractory follicular lymphoma (FL) patients who have previously received at least two systemic therapies. (pharmasources.com)
- The improvement of this tactic by induced fit docking shown that raltegravir binding involved a mechanism and close interactions with the terminal adenine of the 3 processed viral DNA, consistent Dasatinib clinical trial with the results of bio-chemical tests. (deubiquitinase.com)