Tyrosine
Protein Tyrosine Phosphatases
Tyrosine 3-Monooxygenase
Phosphorylation
Phosphotyrosine
Signal Transduction
Protein Tyrosine Phosphatase, Non-Receptor Type 11
Receptor Protein-Tyrosine Kinases
Protein Tyrosine Phosphatase, Non-Receptor Type 6
Protein Tyrosine Phosphatase, Non-Receptor Type 1
Molecular Sequence Data
Enzyme Activation
Amino Acid Sequence
Lymphocyte Specific Protein Tyrosine Kinase p56(lck)
Genistein
Vanadates
src Homology Domains
Proto-Oncogene Proteins
Receptor, Epidermal Growth Factor
Proto-Oncogene Proteins pp60(c-src)
Proto-Oncogene Proteins c-fyn
Enzyme Inhibitors
Tyrosine Decarboxylase
Intracellular Signaling Peptides and Proteins
Tyrosine Phenol-Lyase
Tyrphostins
Cells, Cultured
Proto-Oncogene Proteins c-abl
Protein Binding
SH2 Domain-Containing Protein Tyrosine Phosphatases
Focal Adhesion Protein-Tyrosine Kinases
Mutation
Transfection
Adaptor Proteins, Signal Transducing
Pyrimidines
Receptor-Like Protein Tyrosine Phosphatases, Class 3
Paxillin
Focal Adhesion Kinase 1
Protein Tyrosine Phosphatase, Non-Receptor Type 2
Phospholipase C gamma
3T3 Cells
Focal Adhesion Kinase 2
Receptor-Like Protein Tyrosine Phosphatases, Class 4
fms-Like Tyrosine Kinase 3
Phenylalanine
Precipitin Tests
GRB2 Adaptor Protein
Quinones
Benzoquinones
Proteins
Base Sequence
Binding Sites
Protein Tyrosine Phosphatases, Non-Receptor
Recombinant Fusion Proteins
Janus Kinase 2
Tumor Cells, Cultured
Receptor, Insulin
Mutagenesis, Site-Directed
Protein Structure, Tertiary
Phosphatidylinositol 3-Kinases
Type C Phospholipases
Protein Tyrosine Phosphatase, Non-Receptor Type 12
Blotting, Western
Epidermal Growth Factor
Isoflavones
Mitogen-Activated Protein Kinases
Receptor-Like Protein Tyrosine Phosphatases, Class 5
Cell Division
COS Cells
Shc Signaling Adaptor Proteins
Immunoblotting
Tetranitromethane
Substrate Specificity
Calcium-Calmodulin-Dependent Protein Kinases
Proto-Oncogene Proteins c-met
Receptors, Platelet-Derived Growth Factor
Cytoskeletal Proteins
Membrane Proteins
Proto-Oncogene Proteins c-kit
Protein Processing, Post-Translational
Sequence Homology, Amino Acid
Isoenzymes
Cell Adhesion Molecules
Protein Kinases
Crk-Associated Substrate Protein
RNA, Messenger
Receptor Tyrosine Kinase-like Orphan Receptors
Genes, src
Fusion Proteins, bcr-abl
Trans-Activators
Receptors, Cell Surface
Janus Kinase 1
Cell Membrane
Cell Movement
Calcium
DNA-Binding Proteins
Indoles
STAT3 Transcription Factor
Jurkat Cells
Mitogen-Activated Protein Kinase 1
Insulin Receptor Substrate Proteins
STAT5 Transcription Factor
Receptor, trkA
TYK2 Kinase
Cloning, Molecular
Ligands
Proto-Oncogene Proteins c-crk
Structure-Activity Relationship
Dose-Response Relationship, Drug
Adaptor Proteins, Vesicular Transport
Protein-Serine-Threonine Kinases
Receptors, Antigen, B-Cell
Immunoprecipitation
Protein Tyrosine Phosphatase, Non-Receptor Type 13
Oncogene Proteins v-abl
Receptor, Platelet-Derived Growth Factor beta
Platelet-Derived Growth Factor
Receptors, Antigen, T-Cell
Cell Transformation, Neoplastic
Milk Proteins
Models, Molecular
Electrophoresis, Polyacrylamide Gel
T-Lymphocytes
Amino Acid Substitution
Janus Kinase 3
Amino Acids
Proto-Oncogene Proteins c-vav
Receptor Aggregation
Amino Acid Motifs
Gene Expression
Proto-Oncogene Proteins c-hck
DNA Primers
Proto-Oncogene Proteins c-ret
Peptide Mapping
Peptide Fragments
Mitogen-Activated Protein Kinase 3
Cricetinae
PC12 Cells
Models, Biological
Apoptosis
Cell Differentiation
Down-Regulation
Insulin
Serine
Peptides
Cytoplasm
STAT1 Transcription Factor
Rats, Sprague-Dawley
Cortactin
Fibroblasts
Point Mutation
Receptor, erbB-2
Mice, Knockout
CHO Cells
Receptor, EphB2
DNA, Complementary
Cell Line, Transformed
Protein Conformation
Oncogene Proteins
Dihydroxyphenylalanine
Receptors, Growth Factor
Gene Expression Regulation
Leukemia, Myelogenous, Chronic, BCR-ABL Positive
Antigens, CD
Immunohistochemistry
MAP Kinase Signaling System
Sperm Capacitation
Carrier Proteins
Receptor-Like Protein Tyrosine Phosphatases, Class 7
Neurons
Nitriles
Nerve Growth Factors
Dopamine
Hepatocyte Growth Factor
Proto-Oncogene Proteins c-akt
Antigens, CD45
Receptor, trkB
Gene Expression Regulation, Enzymologic
Glutathione Transferase
The hematopoietic-specific adaptor protein gads functions in T-cell signaling via interactions with the SLP-76 and LAT adaptors. (1/13395)
BACKGROUND: The adaptor protein Gads is a Grb2-related protein originally identified on the basis of its interaction with the tyrosine-phosphorylated form of the docking protein Shc. Gads protein expression is restricted to hematopoietic tissues and cell lines. Gads contains a Src homology 2 (SH2) domain, which has previously been shown to have a similar binding specificity to that of Grb2. Gads also possesses two SH3 domains, but these have a distinct binding specificity to those of Grb2, as Gads does not bind to known Grb2 SH3 domain targets. Here, we investigated whether Gads is involved in T-cell signaling. RESULTS: We found that Gads is highly expressed in T cells and that the SLP-76 adaptor protein is a major Gads-associated protein in vivo. The constitutive interaction between Gads and SLP-76 was mediated by the carboxy-terminal SH3 domain of Gads and a 20 amino-acid proline-rich region in SLP-76. Gads also coimmunoprecipitated the tyrosine-phosphorylated form of the linker for activated T cells (LAT) adaptor protein following cross-linking of the T-cell receptor; this interaction was mediated by the Gads SH2 domain. Overexpression of Gads and SLP-76 resulted in a synergistic augmentation of T-cell signaling, as measured by activation of nuclear factor of activated T cells (NFAT), and this cooperation required a functional Gads SH2 domain. CONCLUSIONS: These results demonstrate that Gads plays an important role in T-cell signaling via its association with SLP-76 and LAT. Gads may promote cross-talk between the LAT and SLP-76 signaling complexes, thereby coupling membrane-proximal events to downstream signaling pathways. (+info)Tyrosine phosphorylation is required for actin-based motility of vaccinia but not Listeria or Shigella. (2/13395)
Studies of the actin-based motility of pathogens have provided important insights into the events occurring at the leading edge of motile cells [1] [2] [3]. To date, several actin-cytoskeleton-associated proteins have been implicated in the motility of Listeria or Shigella: vasodilator-stimulated phosphoprotein (VASP), vinculin and the actin-related protein complex of Arp2 and Arp3 [4] [5] [6] [7]. To further investigate the underlying mechanism of actin-tail assembly, we examined the localization of components of the actin cytoskeleton including Arp3, VASP, vinculin and zyxin during vaccinia, Listeria and Shigella infections. The most striking difference between the systems was that a phosphotyrosine signal was observed only at the site of vaccinia actin-tail assembly. Micro-injection experiments demonstrated that a phosphotyrosine protein plays an important role in vaccinia actin-tail formation. In addition, we observed a phosphotyrosine signal on clathrin-coated vesicles that have associated actin-tail-like structures and on endogenous vesicles in Xenopus egg extracts which are able to nucleate actin tails [8] [9]. Our observations indicate that a host phosphotyrosine protein is required for the nucleation of actin filaments by vaccinia and suggest that this phosphoprotein might be associated with cellular membranes that can nucleate actin. (+info)Tyrosine phosphorylation and complex formation of Cbl-b upon T cell receptor stimulation. (3/13395)
Cbl-b, a mammalian homolog of Cbl, consists of an N-terminal region (Cbl-b-N) highly homologous to oncogenic v-Cbl, a Ring finger, and a C-terminal region containing multiple proline-rich stretches and potential tyrosine phosphorylation sites. In the present study, we demonstrate that upon engagement of the T cell receptor (TCR), endogenous Cbl-b becomes rapidly tyrosine-phosphorylated. In heterogeneous COS-1 cells, Cbl-b was phosphorylated on tyrosine residues by both Syk- (Syk/Zap-70) and Src- (Fyn/Lck) family kinases, with Syk kinase inducing the most prominent effect. Syk associates and phosphorylates Cbl-b in Jurkat T cells. A Tyr-316 Cbl-binding site in Syk was required for the association with and for the maximal tyrosine phosphorylation of Cbl-b. Mutation at a loss-of-function site (Gly-298) in Cbl-b-N disrupts its interaction with Syk. Cbl-b constitutively binds Grb2 and becomes associated with Crk-L upon TCR stimulation. The Grb2- and the Crk-L-binding regions were mapped to the C-terminus of Cbl-b. The Crk-L-binding sites were further determined to be Y655DVP and Y709KIP, with the latter being the primary binding site. Taken together, these results implicate that Cbl-b is involved in TCR-mediated intracellular signaling pathways. (+info)Identification of a novel family of targets of PYK2 related to Drosophila retinal degeneration B (rdgB) protein. (4/13395)
The protein tyrosine kinase PYK2 has been implicated in signaling pathways activated by G-protein-coupled receptors, intracellular calcium, and stress signals. Here we describe the molecular cloning and characterization of a novel family of PYK2-binding proteins designated Nirs (PYK2 N-terminal domain-interacting receptors). The three Nir proteins (Nir1, Nir2, and Nir3) bind to the amino-terminal domain of PYK2 via a conserved sequence motif located in the carboxy terminus. The primary structures of Nirs reveal six putative transmembrane domains, a region homologous to phosphatidylinositol (PI) transfer protein, and an acidic domain. The Nir proteins are the human homologues of the Drosophila retinal degeneration B protein (rdgB), a protein implicated in the visual transduction pathway in flies. We demonstrate that Nirs are calcium-binding proteins that exhibit PI transfer activity in vivo. Activation of PYK2 by agents that elevate intracellular calcium or by phorbol ester induce tyrosine phosphorylation of Nirs. Moreover, PYK2 and Nirs exhibit similar expression patterns in several regions of the brain and retina. In addition, PYK2-Nir complexes are detected in lysates prepared from cultured cells or from brain tissues. Finally, the Nir1-encoding gene is located at human chromosome 17p13.1, in proximity to a locus responsible for several human retinal diseases. We propose that the Nir and rdgB proteins represent a new family of evolutionarily conserved PYK2-binding proteins that play a role in the control of calcium and phosphoinositide metabolism downstream of G-protein-coupled receptors. (+info)Identification of a new Pyk2 target protein with Arf-GAP activity. (5/13395)
Protein tyrosine kinase Pyk2 is activated by a variety of G-protein-coupled receptors and by extracellular signals that elevate intracellular Ca2+ concentration. We have identified a new Pyk2 binding protein designated Pap. Pap is a multidomain protein composed of an N-terminal alpha-helical region with a coiled-coil motif, followed by a pleckstrin homology domain, an Arf-GAP domain, an ankyrin homology region, a proline-rich region, and a C-terminal SH3 domain. We demonstrate that Pap forms a stable complex with Pyk2 and that activation of Pyk2 leads to tyrosine phosphorylation of Pap in living cells. Immunofluorescence experiments demonstrate that Pap is localized in the Golgi apparatus and at the plasma membrane, where it is colocalized with Pyk2. In addition, in vitro recombinant Pap exhibits strong GTPase-activating protein (GAP) activity towards the small GTPases Arf1 and Arf5 and weak activity towards Arf6. Addition of recombinant Pap protein to Golgi preparations prevented Arf-dependent generation of post-Golgi vesicles in vitro. Moreover, overexpression of Pap in cultured cells reduced the constitutive secretion of a marker protein. We propose that Pap functions as a GAP for Arf and that Pyk2 may be involved in regulation of vesicular transport through its interaction with Pap. (+info)BLNK required for coupling Syk to PLC gamma 2 and Rac1-JNK in B cells. (6/13395)
Signaling through the B cell receptor (BCR) is essential for B cell function and development. Despite the key role of Syk in BCR signaling, little is known about the mechanism by which Syk transmits downstream effectors. BLNK (B cell LiNKer protein), a substrate for Syk, is now shown to be essential in activating phospholipase C (PLC)gamma 2 and JNK. The BCR-induced PLC gamma 2 activation, but not the JNK activation, was restored by introduction of PLC gamma 2 membrane-associated form into BLNK-deficient B cells. As JNK activation requires both Rac1 and PLC gamma 2, our results suggest that BLNK regulates the Rac1-JNK pathway, in addition to modulating PLC gamma 2 localization. (+info)Role of nitric oxide in lipopolysaccharide-induced hepatic injury in D-galactosamine-sensitized mice as an experimental endotoxic shock model. (7/13395)
The role of nitric oxide (NO) in lipopolysaccharide (LPS)-induced hepatic injury was studied in D-galactosamine (D-GalN)-sensitized mice. The inducible isoform of NO synthase (iNOS) was immunohistochemically detected on hepatocytes around blood vessels in livers of mice injected with D-GalN and LPS not on hepatocytes in mice injected with D-GalN or LPS alone, although mRNA for iNOS was found in those mice. Nitrotyrosine (NT) was also found in livers of mice injected with D-GalN and LPS. The localization of NT was consistent with that of iNOS, and the time courses of NT and iNOS expression were almost the same. Expression of iNOS and NT was detected exclusively in the hepatic lesions of mice injected with D-GalN and LPS. Anti-tumor necrosis factor alpha neutralizing antibody inhibited iNOS and NT expression and hepatic injury. The results suggested that NO from iNOS may play a role in LPS-induced hepatic injury on D-GalN-sensitized mice as an experimental endotoxic shock model. (+info)Yops of Yersinia enterocolitica inhibit receptor-dependent superoxide anion production by human granulocytes. (8/13395)
The virulence plasmid-borne genes encoding Yersinia adhesin A (YadA) and several Yersinia secreted proteins (Yops) are involved in the inhibition of phagocytosis and killing of Yersinia enterocolitica by human granulocytes. One of these Yops, YopH, dephosphorylates multiple tyrosine-phosphorylated proteins in eukaryotic cells and is involved in the inhibition of phagocytosis of Y. enterocolitica by human granulocytes. We investigated whether antibody- and complement-opsonized plasmid-bearing (pYV+) Y. enterocolitica inhibits O2- production by human granulocytes in response to various stimuli and whether YopH is involved. Granulocytes were preincubated with mutant strains unable to express YadA or to secrete Yops or YopH. O2- production by granulocytes during stimulation was assessed by measuring the reduction of ferricytochrome c. PYV+ Y. enterocolitica inhibited O2- production by granulocytes incubated with opsonized Y. enterocolitica or N-formyl-Met-Leu-Phe (f-MLP). This inhibitory effect mediated by pYV did not affect receptor-independent O2- production by granulocytes in response to phorbol myristate acetate, indicating that NADPH activity remained unaffected after activation of protein kinase C. The inhibition of f-MLP-induced O2- production by granulocytes depends on the secretion of Yops and not on the expression of YadA. Insertional inactivation of the yopH gene abrogated the inhibition of phagocytosis of antibody- and complement-opsonized Y. enterocolitica by human granulocytes but not of the f-MLP-induced O2- production by granulocytes or tyrosine phosphorylation of granulocyte proteins. These findings suggest that the specific targets for YopH are not present in f-MLP receptor-linked signal transduction and that other Yop-mediated mechanisms are involved. (+info)Explanation: Neoplastic cell transformation is a complex process that involves multiple steps and can occur as a result of genetic mutations, environmental factors, or a combination of both. The process typically begins with a series of subtle changes in the DNA of individual cells, which can lead to the loss of normal cellular functions and the acquisition of abnormal growth and reproduction patterns.
Over time, these transformed cells can accumulate further mutations that allow them to survive and proliferate despite adverse conditions. As the transformed cells continue to divide and grow, they can eventually form a tumor, which is a mass of abnormal cells that can invade and damage surrounding tissues.
In some cases, cancer cells can also break away from the primary tumor and travel through the bloodstream or lymphatic system to other parts of the body, where they can establish new tumors. This process, known as metastasis, is a major cause of death in many types of cancer.
It's worth noting that not all transformed cells will become cancerous. Some forms of cellular transformation, such as those that occur during embryonic development or tissue regeneration, are normal and necessary for the proper functioning of the body. However, when these transformations occur in adult tissues, they can be a sign of cancer.
See also: Cancer, Tumor
Word count: 190
The BCR-ABL gene is a fusion gene that is present in the majority of cases of CML. It is created by the translocation of two genes, called BCR and ABL, which leads to the production of a constitutively active tyrosine kinase protein that promotes the growth and proliferation of abnormal white blood cells.
There are three main phases of CML, each with distinct clinical and laboratory features:
1. Chronic phase: This is the earliest phase of CML, where patients may be asymptomatic or have mild symptoms such as fatigue, night sweats, and splenomegaly (enlargement of the spleen). The peripheral blood count typically shows a high number of blasts in the blood, but the bone marrow is still functional.
2. Accelerated phase: In this phase, the disease progresses to a higher number of blasts in the blood and bone marrow, with evidence of more aggressive disease. Patients may experience symptoms such as fever, weight loss, and pain in the joints or abdomen.
3. Blast phase: This is the most advanced phase of CML, where there is a high number of blasts in the blood and bone marrow, with significant loss of function of the bone marrow. Patients are often symptomatic and may have evidence of spread of the disease to other organs, such as the liver or spleen.
Treatment for CML typically involves targeted therapy with drugs that inhibit the activity of the BCR-ABL protein, such as imatinib (Gleevec), dasatinib (Sprycel), or nilotinib (Tasigna). These drugs can slow or stop the progression of the disease, and may also produce a complete cytogenetic response, which is defined as the absence of all Ph+ metaphases in the bone marrow. However, these drugs are not curative and may have significant side effects. Allogenic hematopoietic stem cell transplantation (HSCT) is also a potential treatment option for CML, but it carries significant risks and is usually reserved for patients who are in the blast phase of the disease or have failed other treatments.
In summary, the clinical course of CML can be divided into three phases based on the number of blasts in the blood and bone marrow, and treatment options vary depending on the phase of the disease. It is important for patients with CML to receive regular monitoring and follow-up care to assess their response to treatment and detect any signs of disease progression.
There are several types of lung neoplasms, including:
1. Adenocarcinoma: This is the most common type of lung cancer, accounting for approximately 40% of all lung cancers. It is a malignant tumor that originates in the glands of the respiratory tract and can be found in any part of the lung.
2. Squamous cell carcinoma: This type of lung cancer accounts for approximately 25% of all lung cancers and is more common in men than women. It is a malignant tumor that originates in the squamous cells lining the airways of the lungs.
3. Small cell lung cancer (SCLC): This is a highly aggressive form of lung cancer that accounts for approximately 15% of all lung cancers. It is often found in the central parts of the lungs and can spread quickly to other parts of the body.
4. Large cell carcinoma: This is a rare type of lung cancer that accounts for only about 5% of all lung cancers. It is a malignant tumor that originates in the large cells of the respiratory tract and can be found in any part of the lung.
5. Bronchioalveolar carcinoma (BAC): This is a rare type of lung cancer that originates in the cells lining the airways and alveoli of the lungs. It is more common in women than men and tends to affect older individuals.
6. Lymphangioleiomyomatosis (LAM): This is a rare, progressive, and often fatal lung disease that primarily affects women of childbearing age. It is characterized by the growth of smooth muscle-like cells in the lungs and can lead to cysts, lung collapse, and respiratory failure.
7. Hamartoma: This is a benign tumor that originates in the tissue of the lungs and is usually found in children. It is characterized by an overgrowth of normal lung tissue and can be treated with surgery.
8. Secondary lung cancer: This type of cancer occurs when cancer cells from another part of the body spread to the lungs through the bloodstream or lymphatic system. It is more common in people who have a history of smoking or exposure to other carcinogens.
9. Metastatic cancer: This type of cancer occurs when cancer cells from another part of the body spread to the lungs through the bloodstream or lymphatic system. It is more common in people who have a history of smoking or exposure to other carcinogens.
10. Mesothelioma: This is a rare and aggressive form of cancer that originates in the lining of the lungs or abdomen. It is caused by asbestos exposure and can be treated with surgery, chemotherapy, and radiation therapy.
Lung diseases can also be classified based on their cause, such as:
1. Infectious diseases: These are caused by bacteria, viruses, or other microorganisms and can include pneumonia, tuberculosis, and bronchitis.
2. Autoimmune diseases: These are caused by an overactive immune system and can include conditions such as sarcoidosis and idiopathic pulmonary fibrosis.
3. Genetic diseases: These are caused by inherited mutations in genes that affect the lungs and can include cystic fibrosis and primary ciliary dyskinesia.
4. Environmental diseases: These are caused by exposure to harmful substances such as tobacco smoke, air pollution, and asbestos.
5. Radiological diseases: These are caused by exposure to ionizing radiation and can include conditions such as radiographic breast cancer and lung cancer.
6. Vascular diseases: These are caused by problems with the blood vessels in the lungs and can include conditions such as pulmonary embolism and pulmonary hypertension.
7. Tumors: These can be benign or malignant and can include conditions such as lung metastases and lung cancer.
8. Trauma: This can include injuries to the chest or lungs caused by accidents or other forms of trauma.
9. Congenital diseases: These are present at birth and can include conditions such as bronchopulmonary foregut malformations and congenital cystic adenomatoid malformation.
Each type of lung disease has its own set of symptoms, diagnosis, and treatment options. It is important to seek medical attention if you experience any persistent or severe respiratory symptoms, as early diagnosis and treatment can improve outcomes and quality of life.
People with agammaglobulinemia are more susceptible to infections, particularly those caused by encapsulated bacteria, such as Streptococcus pneumoniae and Haemophilus influenzae type b. They may also experience recurrent sinopulmonary infections, ear infections, and gastrointestinal infections. The disorder can be managed with intravenous immunoglobulin (IVIG) therapy, which provides antibodies to help prevent infections. In severe cases, a bone marrow transplant may be necessary.
Agammaglobulinemia is an autosomal recessive disorder, meaning that a person must inherit two mutated copies of the BTK gene (one from each parent) to develop the condition. It is relatively rare, affecting approximately one in 1 million people worldwide. The disorder can be diagnosed through genetic testing and a complete blood count (CBC) that shows low levels of immunoglobulins.
Treatment for ag
The term "basophilic" refers to the staining properties of these abnormal cells, which have a distinctive appearance under a microscope. The disease is often referred to as "acute" because it progresses rapidly and can be fatal within weeks or months if left untreated.
There are two main subtypes of basophilic leukemia: acute and chronic. Acute basophilic leukemia is the more aggressive and common form of the disease, accounting for approximately 75% of all cases. It typically affects adults in their 40s and 50s and is characterized by a high white blood cell count, anemia, and splenomegaly (enlargement of the spleen).
Chronic basophilic leukemia, on the other hand, is a rarer form of the disease that progresses more slowly and typically affects adults in their 60s and 70s. It is characterized by a lower white blood cell count, splenomegaly, and an increased risk of developing myelodysplastic syndrome (a precancerous condition).
The exact cause of basophilic leukemia is not known, but it is believed to be linked to genetic mutations and exposure to certain chemicals or radiation. Treatment typically involves chemotherapy and/or bone marrow transplantation, and the prognosis varies depending on the subtype and overall health of the patient.
Tyrosine
Tyrosine aminotransferase
Tyrosine hydroxylase
Tyrosine sulfation
Tyrosine phosphorylation
Tyrosine kinase
Tyrosine decarboxylase
Tyrosine ammonia-lyase
Tyrosine kinase inhibitor
Receptor tyrosine phosphatase
TEK tyrosine kinase
Tyrosine phenol-lyase
Tyrosine hydroxylase deficiency
Tyrosine-tRNA ligase
Tyrosine-arginine ligase
Tubulin-tyrosine ligase
Tyrosine kinase 2
Protein tyrosine phosphatase
Tyrosine (data page)
Receptor tyrosine kinase
Tyrosine N-monooxygenase
Bruton's tyrosine kinase
Tyrosine-ester sulfotransferase
AXL receptor tyrosine kinase
Tyrosine-protein kinase BLK
Tyrosine 2,3-aminomutase
Megakaryocyte-associated tyrosine kinase
Non-receptor tyrosine kinase
Fluoroethyl-L-tyrosine (18F)
Tyrosine-protein kinase SYK
Tyrosine hydroxylase deficiency: MedlinePlus Genetics
Protein-tyrosine-phosphatase (zebrafish) | Protein Target - PubChem
Tyrosine news and latest updates
BTK (Bruton agammaglobulinemia tyrosine kinase)
Treatment Free Remission After Combination Therapy With Ruxolitinib Plus Tyrosine Kinase Inhibitors - No Study Results Posted -...
Schnitzler Syndrome Medication: Antineoplastics, Tyrosine Kinase Inhibitor, Interleukin-1 Receptor Antagonist, Anti-Interleukin...
RCSB PDB - 1R0P: Crystal structure of the tyrosine kinase domain of the hepatocyte growth factor receptor c-Met in complex with...
Diverting tyrosine: Data from untargeted metabolic analysis of tomato fruit accumulating L-DOPA. | John Innes Centre
For Ph-like acute lymphoblastic leukemia (ALL), tyrosine kinase inhibitors (TKIs) may be effective - Oncology Nurse Advisor
Distribution intracellulaire et trafic des récepteurs à tyrosine kinase EphA4 et EphB2 à la synapse mature dans le système...
Nitration of tyrosine by hydrogen peroxide and nitrite. | Scholars@Duke
enQuireBio™ Recombinant Mouse Tyrosine-protein kinase JAK1 Protein 1mg enQuireBio™ Recombinant Mouse Tyrosine-protein kinase...
CD16-mediated p21ras activation is associated with Shc and p36 tyrosine phosphorylation and their binding with Grb2 in human...
Tyrosine | Axxeleration
Tyrosine | Ginasiovirtual.com
Tyrosine | Northwestern Medicine
Buy Acetyl tyrosine - Venogen
Tyrosine Transaminase | Profiles RNS
l-tyrosine - The Bioneer
Phenylalanine and tyrosine levels are rate-limiting factors in production of health promoting metabolites in Vitis vinifera cv....
Functional proteomic analysis of long-term growth factor stimulation and receptor tyrosine kinase coactivation in Swiss 3T3...
Galactosylated L-tyrosine - Dextra UK
SMED30004568
Top 20 tyrosine supplement in 2023
SSCLTY I
"Tyrosine Phosphorylation Based Homo-dimerization of Arabidopsis RACK1A" by Mercy Sabila, Nabanita Kundu et al.
L-tyrosine catabolism in Azospirillum brasilense Sp245
Inhibitors7
- Introduction and lung tyrosine kinase inhibitors / T. Moody and G. Giaccone. (nih.gov)
- 100% of patients received prior platinum-based chemotherapy, 43% received prior immunotherapy, and 25% received prior EGFR tyrosine kinase inhibitors. (curetoday.com)
- According to findings presented at the American Association for Cancer Research special conference Hematologic Malignancies: Translating Discoveries to Novel Therapies in Philadelphia, Pennsylvania, tyrosine kinase inhibitors (TKIs) may be effective for the treatment of children and young adults with Philadelphia chromosome (Ph)-like acute lymphoblastic leukemia (ALL) . (oncologynurseadvisor.com)
- Tyrosine kinase inhibitors (TKIs) may improve treatment outcome for children and young adults with Ph-like acute lymphoblastic leukemia (Ph-like ALL), a disease with dismal prognosis, according to data presented at the American Association for Cancer Research special conference Hematologic Malignancies: Translating Discoveries to Novel Therapies, held Sept. 20-23. (oncologynurseadvisor.com)
- We wanted to examine whether these alterations contribute to the development of Ph-like ALL, and determine if they could be targeted with tyrosine kinase inhibitors. (oncologynurseadvisor.com)
- Recently, we have discovered that Eph tyrosine kinase receptors control the growth and survival of colorectal cancer cells and have exploited this discovery to develop small molecule tyrosine kinase inhibitors (TKI) that effectively reduce the growth or induce cell death in colorectal cancer cells. (nih.gov)
- Validation and specificity experiments performed in wild-type (WT) and STEP knockout (KO) cortical cells and in vivo in WT and STEP KO mice suggest specificity of inhibitors towards STEP compared to highly homologous tyrosine phosphatases. (nih.gov)
Phosphorylation11
- Phosphorylation of tyrosine residues in signaling proteins by protein tyrosine kinases mediates a variety of cellular processes, including cell growth, differentiation, adhesion, motility, death, and metabolism. (rndsystems.com)
- Dysregulation of tyrosine phosphorylation has been implicated in the development of many human diseases, such as diabetes and cancer. (rndsystems.com)
- Antibodies specific for phospho-tyrosine have been invaluable reagents in the studies of signaling pathways initiated by tyrosine phosphorylation. (rndsystems.com)
- Two tyrosine phosphorylation sites are located at the positions Y223 and Y551, which are located in the SH3 and kinase domain, respectively. (atlasgeneticsoncology.org)
- Here, we have described a mechanism of NLRP3 inflammasome regulation by tyrosine phosphorylation of NLRP3 at Tyr861. (uzh.ch)
- Together, our results identify tyrosine phosphorylation as an important regulatory mechanism for NLRP3 that prevents aberrant inflammasome activation. (uzh.ch)
- Then insulin-stimulated IR and IRS tyrosine phosphorylation, and Akt pathway activation were measured. (minervamedica.it)
- Compared with control cells, INS-1 cells overexpressing PTP1B showed decrease in insulin-stimulated tyrosine phosphorylation of the insulin receptor (IR) and insulin receptor substrate-1(IRS-1) by 56.4% and 53.1%, respectively. (minervamedica.it)
- CD16-mediated p21ras activation is associated with Shc and p36 tyrosine phosphorylation and their binding with Grb2 in human natural killer cells. (rupress.org)
- Accumulation of guanosine triphosphate-bound Ras was detected within 1 minute and occurred with kinetics similar to inductive protein tyrosine phosphorylation and Grb2 association of Shc and p36 adaptor proteins. (rupress.org)
- In cell-based secondary assays, TC-2153 increased tyrosine phosphorylation of STEP substrates ERK1/2, Pyk2, and GluN2B, and exhibited no toxicity in cortical cultures. (nih.gov)
Hydroxylase deficiency2
- Furukawa Y, Kish S. Tyrosine Hydroxylase Deficiency. (medlineplus.gov)
- Furukawa Y, Kish SJ, Fahn S. Dopa-responsive dystonia due to mild tyrosine hydroxylase deficiency. (medlineplus.gov)
Spleen tyrosine kinase2
Residues2
- This interaction can initiate nitration and hydroxylation of aromatic molecules such as tyrosine residues and may thereby contribute to the biochemical and toxic effects of the molecules. (duke.edu)
- 2010). Tyrosine residues are oxidized by hypochlorite at the ortho positions resulting in two stable chlorine adducts, 3-chlorotyrosine (Cl-Tyr) and 3,5-dichlorotyrosine (Cl2-Tyr) that can be used as biomarkers of chlorine gas exposure (Hureiki et. (cdc.gov)
Kinase receptor1
- The Axl tyrosine kinase receptor is important in hematopoiesis, platelet aggregation, engulfment of apoptotic cells and cell survival. (nih.gov)
Receptor9
- instructions for making a protein called fms-like tyrosine kinase 3 (FLT3), which is part of a family of proteins called receptor tyrosine kinases (RTKs). (nih.gov)
- Mediated by both on-target inhibition of BTK and variable off-target inhibition of other kinases including interleukin-2-inducible T-cell kinase (ITK), tyrosine-protein kinase (TEC), and endothelial growth factor receptor (EGFR), the toxicity profile of BTKis is closely linked to their pattern of kinase binding. (nih.gov)
- The protooncogene c-met codes for the hepatocyte growth factor receptor tyrosine kinase. (rcsb.org)
- We demonstrated that protein tyrosine phosphatase non-receptor 22 (PTPN22), variants in which are associated with chronic inflammatory disorders, dephosphorylates NLRP3 upon inflammasome induction, allowing efficient NLRP3 activation and subsequent IL-1β release. (uzh.ch)
- STEP (STriatal-Enriched protein tyrosine Phosphatase) is a neuron-specific phosphatase that regulates N-methyl-D-aspartate receptor (NMDAR) and a-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) trafficking, as well as ERK1/ 2, p38, Fyn, and Pyk2 activity. (nih.gov)
- C-Abl is a ubiquitous non-receptor tyrosine kinase involved in signal transduction. (nih.gov)
- Cocaine reward is reduced by decreased expression of receptor-type protein tyrosine phosphatase D (PTPRD) and by a novel PTPRD antagonist. (nih.gov)
- Receptor-type protein tyrosine phosphatase D (PTPRD) is a neuronal cell-adhesion molecule that has been associated with psychostimulant addiction in humans. (nih.gov)
- [email protected].}, abstract = {Receptor-type protein tyrosine phosphatase D (PTPRD) is a neuronal cell-adhesion molecule/synaptic specifier that has been implicated in addiction vulnerability and stimulant reward by human genomewide association and mouse cocaine-conditioned place-preference data. (nih.gov)
Kinases5
- The translocation to the membrane brings the BTK protein in close proximity to the Lyn en Syk kinases that transphosphorylate BTK at tyrosine Y551. (atlasgeneticsoncology.org)
- BTK belongs to the TEC family of cytoplasmic tyrosine kinases. (atlasgeneticsoncology.org)
- The researchers introduced genetic mutations to tyrosine kinases in normal mouse blood cells and found that the cells developed Ph-like ALL. (oncologynurseadvisor.com)
- Furthermore, they found that the signal transducer and activator of transcription (STAT) signaling pathway associated with the genetic alterations involving tyrosine kinases was suppressed. (oncologynurseadvisor.com)
- We recently described a subtype of B-cell acute lymphoblastic leukemia with very poor outcome that is characterized by genetic alterations involving tyrosine kinases, termed Ph-like ALL," said Kathryn Roberts, PhD, postdoctoral research associate in the Department of Pathology at St. Jude Children's Research Hospital in Memphis, Tennessee. (oncologynurseadvisor.com)
Small molecule1
- Small molecule that selectively inhibits the tyrosine kinase activity of c-kit, bcr-abl, and PDGFR. (medscape.com)
Receptors1
- Because the signaling pathways activated by several tyrosine kinase receptors have been shown to be involved in lung fibrosis, it has been suggested that the inhibition of these receptors may slow the progression of idiopathic pulmonary fibrosis. (nih.gov)
Bruton's1
- Inhibition of Bruton's tyrosine kinase (BTK) has revolutionized the treatment landscape for patients with chronic lymphocytic leukemia (CLL). (nih.gov)
Amino acid3
- Tyrosine hydroxylase helps convert the protein building block (amino acid) tyrosine to a catecholamine called dopamine . (medlineplus.gov)
- L-DOPA, also known as Levodopa or L-3,4-dihydroxyphenylalanine, is synthesised in plants from the amino acid tyrosine, through oxidation. (jic.ac.uk)
- From NCIt: The levorotatory isomer of the aromatic amino acid tyrosine. (nih.gov)
Biomarkers1
- Briefly, calibrators, quality controls, a matrix blank, blind QCs, and NHANES samples were prepared by performing a protein digestion using pronase to release the chlorinated tyrosine biomarkers. (cdc.gov)
Pathways1
- These agents inhibit tyrosine kinase, which, in turn, inhibit activation of intracellular pathways that can promote deregulated cell proliferation. (medscape.com)
Inhibition1
- Inhibition of human sperm motility and capacitation by ziram is mediated by decreasing tyrosine protein kinase. (bvsalud.org)
Phenylalanine2
EGFR1
- Mobocertinib is an orally administered tyrosine kinase inhibitor that is specifically being developed for the treatment of (patients with) EGFR (exon) 20 insertion mutations," added Ramalingam, who is also deputy director and director of the Lung Cancer Program of Winship Cancer Institute of Emory University. (curetoday.com)
Inhibits1
- In conclusion, ziram irreversibly inhibits human sperm motility , forward motility, and capacitation by reducing the level of tyrosine protein kinase and damaging the ultrastructure of mitochondria . (bvsalud.org)
Inhibitor2
- In a 12-month, phase 2 trial, we assessed the efficacy and safety of four different oral doses of the tyrosine kinase inhibitor BIBF 1120 as compared with placebo in patients with idiopathic pulmonary fibrosis. (nih.gov)
- Panniculitis in a patient with metastatic renal cell carcinoma on a tyrosine kinase inhibitor. (physiciansweekly.com)
Phosphatase1
- BACKGROUND: Protein tyrosine phosphatase 1B (PTP1B) has been implicated as a negative regulator of insulin signaling. (minervamedica.it)
Vivo1
- In vivo, tyrosine plays a role in protein synthesis and serves as a precursor for the synthesis of catecholamines, thyroxine, and melanin. (nih.gov)
Gene provides instructions1
- The TH gene provides instructions for making the enzyme tyrosine hydroxylase, which is important for normal functioning of the nervous system. (medlineplus.gov)
Belongs1
- a protein that belongs to the PTP (protein tyrosine phosphatases) family. (nih.gov)
Cells2
- Shc immunoprecipitates from lysates of CD16- or IL-2-stimulated NK cells contained Grb2 and an unidentified 145-kD tyrosine phosphoprotein. (rupress.org)
- Grb2 immunoprecipitates from anti-CD16-stimulated NK cells contained not only Shc, but also a 36-kD tyrosine phosphoprotein (p36). (rupress.org)
Results1
- Phospho-Tyrosine " has 6 results in Products. (rndsystems.com)
Important1
- Mounting evidence points to the role of the Abl tyrosine kinase family as an important player in Alzheimer's Disease, and thus a potential therapeutic target to delay and ameliorate neurodegeneration. (nih.gov)
Studies1
- Further studies have shown that ziram inhibited the level of tyrosine protein kinase with an IC50 value of about 10 µM, without affecting p21-activated kinase 4, and it caused damage to the mitochondrial structure of normal spermatozoa at 2.5 and 5 µM. (bvsalud.org)
Data2
- Diverting tyrosine: Data from untargeted metabolic analysis of tomato fruit accumulating L-DOPA. (jic.ac.uk)
- These data can be used to study the impact of diversion of tyrosine in fruit, accompanied by the accumulation of L-DOPA in planta and to identify new biological roles associated with the accumulation of these metabolites. (jic.ac.uk)
Mouse1
- A DNA sequence encoding the Mus musculus (Mouse) Tyrosine-protein kinase JAK1, was expressed in the hosts and tags indicated. (fishersci.dk)
Products1
- Nitration and hydroxylation products of tyrosine and salicyclic acid were separated with an HPLC column and measured using ultraviolet and electrochemical detectors. (duke.edu)
Type1
- Kathryn Roberts, PhD, postdoctoral research associate at St. Jude Children's Research Hospital in Memphis, Tennessee, and her colleagues recently described a type of B-cell ALL characterized by tyrosine kinase mutations associated with poor outcomes. (oncologynurseadvisor.com)
Domain1
- A tyrosine-kinase catalytic domain is located at the C-terminal end. (atlasgeneticsoncology.org)
Activity2
- Mutations in the TH gene result in reduced activity of the tyrosine hydroxylase enzyme. (medlineplus.gov)
- Modelling and cell-based structure-activity relationships were used to guide the optimization and diversification of ligands that are capable of crossing the blood brain barrier (BBB), and bind to the myristate pocket on the c-Abl tyrosine kinase. (nih.gov)
Form1
- Stathmin and tubulin tyrosine ligase (TTL) each form stable complexes with tubulin and inhibit tubulin polymerization. (nih.gov)
Step1
- Conversion of tyrosine to L-DOPA constitues the first step of betalain biosynthesis in plants. (jic.ac.uk)