Substrate Specificity
Proto-Oncogene Proteins c-crk
Chaperonin 10
Chaperonin 60
Molecular Sequence Data
Amino Acid Sequence
Protein Binding
Chaperonins
Molecular Chaperones
Thiosulfate Sulfurtransferase
Binding Sites
Models, Molecular
Phosphorylation
Escherichia coli
Protein Structure, Tertiary
Oncogene Protein v-crk
Protein Conformation
Adenosine Triphosphate
Genetic Processes
Proteins
Crk-Associated Substrate Protein
Endopeptidase Clp
Catalysis
Insulin Receptor Substrate Proteins
Mutation
Ubiquitin
Ubiquitin-Protein Ligases
Sequence Homology, Amino Acid
Crystallography, X-Ray
Heat-Shock Proteins
Catalytic Domain
Amino Acid Motifs
Adenosine Triphosphatases
Tankyrases
Mutagenesis, Site-Directed
Protein Transport
Signal Transduction
Protein Kinases
SUMO-1 Protein
Oxidation-Reduction
Base Sequence
Membrane Proteins
Enzyme Activation
Ubiquitins
Disulfides
Structure-Activity Relationship
Tyrosine
Electrophoresis, Polyacrylamide Gel
Cattle
Protein Disulfide-Isomerases
Adaptor Proteins, Signal Transducing
Hydrogen-Ion Concentration
Ubiquitin-Conjugating Enzymes
src Homology Domains
Ligases
Oxidoreductases Acting on Sulfur Group Donors
HSP70 Heat-Shock Proteins
Saccharomyces cerevisiae
Intracellular Signaling Peptides and Proteins
Recombinant Fusion Proteins
Protein Structure, Quaternary
Citrate (si)-Synthase
Multiprotein Complexes
Proteasome Endopeptidase Complex
Peptides
Models, Biological
Temperature
Membrane Transport Proteins
Protein Structure, Secondary
Saccharomyces cerevisiae Proteins
Carrier Proteins
Endopeptidases
Peptide Hydrolases
Amino Acid Substitution
Sequence Alignment
Cloning, Molecular
Protein Processing, Post-Translational
Malate Dehydrogenase
Protein Denaturation
Small Ubiquitin-Related Modifier Proteins
Periplasm
Ribulose-Bisphosphate Carboxylase
Phosphotyrosine
Proto-Oncogene Proteins
Protein Kinase C
Retinoblastoma-Like Protein p130
Chromatography, High Pressure Liquid
Mass Spectrometry
Serine Endopeptidases
Cytosol
Protein-Tyrosine Kinases
HSP40 Heat-Shock Proteins
Transglutaminases
Mitochondrial Membrane Transport Proteins
Ubiquitination
Cell Membrane
Protein-Serine-Threonine Kinases
Plasmids
Hydrophobic and Hydrophilic Interactions
Polyubiquitin
Adenosine Diphosphate
Fluorescence Resonance Energy Transfer
Nuclear Proteins
Cysteine Endopeptidases
Allosteric Regulation
Chromatography, Gel
Guanine Nucleotide-Releasing Factor 2
Enzyme Inhibitors
Mutagenesis
DNA Primers
Biological Transport
Isoenzymes
Serine
Acyltransferases
HeLa Cells
Oxidoreductases
Calmodulin
Sumoylation
Subcellular Fractions
Thermus thermophilus
Cells, Cultured
Protein Interaction Domains and Motifs
Transfection
Thermodynamics
Peptide Fragments
Calnexin
Cross-Linking Reagents
Mitochondria
Blotting, Western
3T3 Cells
Proto-Oncogene Proteins c-abl
Mitochondrial Proteins
Macromolecular Substances
Immunoprecipitation
Conserved Sequence
Phosphatidylserines
Threonine
Myristic Acid
Protein Multimerization
Protein Subunits
Circular Dichroism
Dimerization
Retroviridae Proteins, Oncogenic
Plant Proteins
Cryoelectron Microscopy
Fluorescent Dyes
Insulin
Fluorescence Polarization
Precipitin Tests
Receptor, Insulin
Molecular Structure
Calcium
Models, Chemical
Protein Sorting Signals
Proto-Oncogene Proteins c-cbl
Swine
Stereoisomerism
Nuclear Magnetic Resonance, Biomolecular
Green Fluorescent Proteins
Endoplasmic Reticulum
Microscopy, Fluorescence
HSP90 Heat-Shock Proteins
Paxillin
Calcium-Binding Proteins
Substrate Cycling
Gene Expression
Arabidopsis Proteins
Electrophoresis, Gel, Two-Dimensional
Amino Acids
Enzyme Stability
GRB2 Adaptor Protein
Arabidopsis
ras Guanine Nucleotide Exchange Factors
Luciferases
Liver
DNA-Binding Proteins
Cellular Apoptosis Susceptibility Protein
Phosphatidylinositol 3-Kinases
Cell adhesion regulates the interaction between the docking protein p130(Cas) and the 14-3-3 proteins. (1/356)
Integrin ligand binding induces a signaling complex formation via the direct association of the docking protein p130(Cas) (Cas) with diverse molecules. We report here that the 14-3-3zeta protein interacts with Cas in the yeast two-hybrid assay. We also found that the two proteins associate in mammalian cells and that this interaction takes place in a phosphoserine-dependent manner, because treatment of Cas with a serine phosphatase greatly reduced its ability to bind 14-3-3zeta. Furthermore, the Cas-14-3-3zeta interaction was found to be regulated by integrin-mediated cell adhesion. Thus, when cells are detached from the extracellular matrix, the binding of Cas to 14-3-3zeta is greatly diminished, whereas replating the cells onto fibronectin rapidly induces the association. Consistent with these results, we found that the subcellular localization of Cas and 14-3-3 is also regulated by integrin ligand binding and that the two proteins display a significant co-localization during cell attachment to the extracellular matrix. In conclusion, our results demonstrate that 14-3-3 proteins participate in integrin-activated signaling pathways through their interaction with Cas, which, in turn, may contribute to important biological responses regulated by cell adhesion to the extracellular matrix. (+info)Alternatively spliced EDA segment regulates fibronectin-dependent cell cycle progression and mitogenic signal transduction. (2/356)
Fibronectin (FN) is comprised of multiple isoforms arising from alternative splicing of a single gene transcript. One of the alternatively spliced segments, EDA, is expressed prominently in embryonic development, malignant transformation, and wound healing. We showed previously that EDA+ FN was more potent than EDA- FN in promoting cell spreading and cell migration because of its enhanced binding affinity to integrin alpha5beta1 (Manabe, R., Oh-e, N., Maeda, T., Fukuda, T., and Sekiguchi, K. (1997) J. Cell Biol. 139, 295-307). In this study, we compared the cell cycle progression and its associated signal transduction events induced by FN isoforms with or without the EDA segment to examine whether the EDA segment modulates the cell proliferative potential of FN. We found that EDA+ FN was more potent than EDA- FN in inducing G1-S phase transition. Inclusion of the EDA segment potentiated the ability of FN to induce expression of cyclin D1, hyperphosphorylation of pRb, and activation of mitogen-activated protein kinase extracellular signal regulated kinase 2 (ERK2). EDA+ FN was also more potent than EDA- FN in promoting FN-mediated tyrosine phosphorylation of p130(Cas), but not focal adhesion kinase, which occurred in parallel with the activation of ERK2, suggesting that p130(Cas) may be involved in activation of ERK2. These results indicated that alternative splicing at the EDA region is a novel mechanism that promotes FN-induced cell cycle progression through up-regulation of integrin-mediated mitogenic signal transduction. (+info)Agonist-stimulated cytoskeletal reorganization and signal transduction at focal adhesions in vascular smooth muscle cells require c-Src. (3/356)
Thrombin and angiotensin II (angII) have trophic properties as mediators of vascular remodeling. Focal adhesions and actin cytoskeleton are involved in cell growth, shape, and movement and may be important in vascular remodeling. To characterize mechanisms by which thrombin and angII modulate vessel structure, we studied the effects of these G protein-coupled receptor ligands on focal adhesions in vascular smooth muscle cells (VSMCs). Both thrombin and angII stimulated bundling of actin filaments to form stress fibers, assembly of focal adhesions, and protein tyrosine phosphorylation at focal adhesions, such as p130Cas, paxillin, and tensin. To test whether c-Src plays a critical role in focal adhesion rearrangement, we analyzed cells with altered c-Src activity by retroviral transduction of wild-type (WT) and kinase-inactive (KI) c-Src into rat VSMCs, and by use of VSMCs from WT (src+/+) and Src-deficient (src-/-) mice. Tyrosine phosphorylation of Cas, paxillin, and tensin were markedly decreased in VSMCs expressing KI-Src and in src-/- VSMCs. Expression of KI-Src did not inhibit stress fiber formation by thrombin. Surprisingly, actin bundling was markedly decreased in VSMCs from src-/- mice both basally and after thrombin stimulation, compared with src+/+ mice. We also studied the effect of KI-Src and WT-Src on VSMC spreading. Expression of KI-Src reduced the rate of VSMC spreading on collagen, whereas WT-Src enhanced cell spreading. In conclusion, c-Src plays a critical role in agonist-stimulated cytoskeletal reorganization and signal transduction at focal adhesions in VSMCs. c-Src kinase activity is required for the cytoskeletal turnover that occurs in cell spreading, whereas c-Src appears to regulate actin bundling via a kinase-independent mechanism. (+info)NSP1 defines a novel family of adaptor proteins linking integrin and tyrosine kinase receptors to the c-Jun N-terminal kinase/stress-activated protein kinase signaling pathway. (4/356)
As part of a program to further understand the mechanism by which extracellular signals are coordinated and cell-specific outcomes are generated, we have cloned a novel class of related adaptor molecules (NSP1, NSP2, and NSP3) and have characterized in more detail one of the members, NSP1. NSP1 has an Shc-related SH2 domain and a putative proline/serine-rich SH3 interaction domain. Treatment of cells with epidermal growth factor or insulin leads to NSP1 phosphorylation and increased association with a hypophosphorylated adaptor protein, p130(Cas). In contrast, cell contact with fibronectin results in Cas phosphorylation and a transient dissociation of NSP1 from p130(Cas). Increased expression of NSP1 in 293 cells induces activation of JNK1, but not of ERK2. Consistent with this observation, NSP1 increases the activity of an AP-1-containing promoter. Thus, we have described a novel family of adaptor proteins, one of which may be involved in the process by which receptor tyrosine kinase and integrin receptors control the c-Jun N-terminal kinase/stress-activated protein kinase pathway. (+info)Rho-dependent and -independent tyrosine phosphorylation of focal adhesion kinase, paxillin and p130Cas mediated by Ret kinase. (5/356)
Glial cell line-derived neurotrophic factor (GDNF) signals through a unique receptor system that includes Ret receptor tyrosine kinase and a glycosyl-phosphatidylinositol-linked cell surface protein. In the present study, we have identified several proteins in neuroblastoma cells that are phosphorylated on tyrosine in response to GDNF. The phosphorylated proteins include focal adhesion kinase (FAK), paxillin and Crk-associated substrate, p130Cas, all of which are known to be associated with focal adhesions. Of these, paxillin and p130Cas interacted with Crk proteins in GDNF-treated neuroblastoma cells. GDNF also induced reorganization of the actin cytoskelton. Tyrosine phosphorylation of FAK, paxillin and p130Cas was inhibited by cytochalasin D or two specific inhibitors of phosphatidylinositol-3' kinase (PI-3' kinase), wortmannin and LY294002, indicating that their tyrosine phosphorylation depends on the formation of actin stress fiber and activation of PI-3' kinase. In addition, phosphorylation of FAK but not of paxillin and p130Cas was markedly impaired by the Clostridium botulinum C3 exoenzyme that specifically ADP-ribosylates and inactivates Rho. These results suggested the presence of Rho-dependent and -independent signaling pathways downstream of PI-3' kinase that mediate tyrosine phosphorylation of FAK, paxillin and p130Cas through Ret kinase. (+info)CMS: an adapter molecule involved in cytoskeletal rearrangements. (6/356)
Cas ligand with multiple Src homology (SH) 3 domains (CMS) is an ubiquitously expressed signal transduction molecule that interacts with the focal adhesion protein p130(Cas). CMS contains three SH3 in its NH2 terminus and proline-rich sequences in its center region. The latter sequences mediate the binding to the SH3 domains of p130(Cas), Src-family kinases, p85 subunit of phosphatidylinositol 3-kinase, and Grb2. The COOH-terminal region contains putative actin binding sites and a coiled-coil domain that mediates homodimerization of CMS. CMS is a cytoplasmic protein that colocalizes with F-actin and p130(Cas) to membrane ruffles and leading edges of cells. Ectopic expression of CMS in COS-7 cells resulted in alteration in arrangement of the actin cytoskeleton. We observed a diffuse distribution of actin in small dots and less actin fiber formation. Altogether, these features suggest that CMS functions as a scaffolding molecule with a specialized role in regulation of the actin cytoskeleton. (+info)Induced focal adhesion kinase (FAK) expression in FAK-null cells enhances cell spreading and migration requiring both auto- and activation loop phosphorylation sites and inhibits adhesion-dependent tyrosine phosphorylation of Pyk2. (7/356)
Focal adhesion kinase (FAK) is a nonreceptor protein tyrosine kinase involved in integrin-mediated control of cell behavior. Following cell adhesion to components of the extracellular matrix, FAK becomes phosphorylated at multiple sites, including tyrosines 397, 576, and 577. Tyr-397 is an autophosphorylation site that promotes interaction with c-Src or Fyn. Tyr-576 and Tyr-577 lie in the putative activation loop of the kinase domain, and FAK catalytic activity may be elevated through phosphorylation of these residues by associated Src family kinase. Recent studies have implicated FAK as a positive regulator of cell spreading and migration. To further study the mechanism of adhesion-induced FAK activation and the possible role and signaling requirements for FAK in cell spreading and migration, we utilized the tetracycline repression system to achieve inducible expression of either wild-type FAK or phosphorylation site mutants in fibroblasts derived from FAK-null mouse embryos. Using these Tet-FAK cells, we demonstrated that both the FAK autophosphorylation and activation loop sites are critical for maximum adhesion-induced FAK activation and FAK-enhanced cell spreading and migration responses. Negative effects on cell spreading and migration, as well as decreased phosphorylation of the substrate p130(Cas), were observed upon induced expression of the FAK autophosphorylation site mutant. These negative effects appear to result from an inhibition of integrin-mediated signaling by the FAK-related kinase Pyk2/CAKbeta/RAFTK/CadTK. (+info)Integrin-mediated activation of focal adhesion kinase is required for signaling to Jun NH2-terminal kinase and progression through the G1 phase of the cell cycle. (8/356)
The extracellular matrix exerts a stringent control on the proliferation of normal cells, suggesting the existence of a mitogenic signaling pathway activated by integrins, but not significantly by growth factor receptors. Herein, we provide evidence that integrins cause a significant and protracted activation of Jun NH2-terminal kinase (JNK), while several growth factors cause more modest or no activation of this enzyme. Integrin-mediated stimulation of JNK required the association of focal adhesion kinase (FAK) with a Src kinase and p130(CAS), the phosphorylation of p130(CAS), and subsequently, the recruitment of Crk. Ras and PI-3K were not required. FAK-JNK signaling was necessary for proper progression through the G1 phase of the cell cycle. These findings establish a role for FAK in both the activation of JNK and the control of the cell cycle, and identify a physiological stimulus for JNK signaling that is consistent with the role of Jun in both proliferation and transformation. (+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
Examples of mammary neoplasms in animals include:
* Mammary adenocarcinoma: A type of tumor that develops in the mammary gland of animals and is characterized by the growth of abnormal cells that produce milk.
* Mammary fibroadenoma: A benign tumor that develops in the mammary gland of animals and is characterized by the growth of fibrous and glandular tissue.
* Inflammatory mammary carcinoma: A type of tumor that develops in the mammary gland of animals and is characterized by the presence of inflammatory cells and abnormal cells.
These tumors can be caused by a variety of factors, including genetic mutations, hormonal imbalances, and exposure to certain environmental agents. They can also be induced experimentally using chemical carcinogens or viruses.
The study of mammary neoplasms in animals is important for understanding the molecular mechanisms underlying breast cancer development and progression, as well as for identifying potential therapeutic targets and developing new treatments.
Starvation is a condition where an individual's body does not receive enough nutrients to maintain proper bodily functions and growth. It can be caused by a lack of access to food, poverty, poor nutrition, or other factors that prevent the intake of sufficient calories and essential nutrients. Starvation can lead to severe health consequences, including weight loss, weakness, fatigue, and even death.
Types of Starvation:
There are several types of starvation, each with different causes and effects. These include:
1. Acute starvation: This occurs when an individual suddenly stops eating or has a limited access to food for a short period of time.
2. Chronic starvation: This occurs when an individual consistently does not consume enough calories and nutrients over a longer period of time, leading to gradual weight loss and other health problems.
3. Malnutrition starvation: This occurs when an individual's diet is deficient in essential nutrients, leading to malnutrition and other health problems.
4. Marasmus: This is a severe form of starvation that occurs in children, characterized by extreme weight loss, weakness, and wasting of muscles and organs.
5. Kwashiorkor: This is a form of malnutrition caused by a diet lacking in protein, leading to edema, diarrhea, and other health problems.
Effects of Starvation on the Body:
Starvation can have severe effects on the body, including:
1. Weight loss: Starvation causes weight loss, which can lead to a decrease in muscle mass and a loss of essential nutrients.
2. Fatigue: Starvation can cause fatigue, weakness, and a lack of energy, making it difficult to perform daily activities.
3. Weakened immune system: Starvation can weaken the immune system, making an individual more susceptible to illnesses and infections.
4. Nutrient deficiencies: Starvation can lead to a deficiency of essential nutrients, including vitamins and minerals, which can cause a range of health problems.
5. Increased risk of disease: Starvation can increase the risk of diseases such as tuberculosis, pellagra, and other infections.
6. Mental health issues: Starvation can lead to mental health issues such as depression, anxiety, and irritability.
7. Reproductive problems: Starvation can cause reproductive problems, including infertility and miscarriage.
8. Hair loss: Starvation can cause hair loss, which can be a sign of malnutrition.
9. Skin problems: Starvation can cause skin problems, such as dryness, irritation, and infections.
10. Increased risk of death: Starvation can lead to increased risk of death, especially in children and the elderly.
It is important to note that these effects can be reversed with proper nutrition and care. If you or someone you know is experiencing starvation, it is essential to seek medical attention immediately.
1) They share similarities with humans: Many animal species share similar biological and physiological characteristics with humans, making them useful for studying human diseases. For example, mice and rats are often used to study diseases such as diabetes, heart disease, and cancer because they have similar metabolic and cardiovascular systems to humans.
2) They can be genetically manipulated: Animal disease models can be genetically engineered to develop specific diseases or to model human genetic disorders. This allows researchers to study the progression of the disease and test potential treatments in a controlled environment.
3) They can be used to test drugs and therapies: Before new drugs or therapies are tested in humans, they are often first tested in animal models of disease. This allows researchers to assess the safety and efficacy of the treatment before moving on to human clinical trials.
4) They can provide insights into disease mechanisms: Studying disease models in animals can provide valuable insights into the underlying mechanisms of a particular disease. This information can then be used to develop new treatments or improve existing ones.
5) Reduces the need for human testing: Using animal disease models reduces the need for human testing, which can be time-consuming, expensive, and ethically challenging. However, it is important to note that animal models are not perfect substitutes for human subjects, and results obtained from animal studies may not always translate to humans.
6) They can be used to study infectious diseases: Animal disease models can be used to study infectious diseases such as HIV, TB, and malaria. These models allow researchers to understand how the disease is transmitted, how it progresses, and how it responds to treatment.
7) They can be used to study complex diseases: Animal disease models can be used to study complex diseases such as cancer, diabetes, and heart disease. These models allow researchers to understand the underlying mechanisms of the disease and test potential treatments.
8) They are cost-effective: Animal disease models are often less expensive than human clinical trials, making them a cost-effective way to conduct research.
9) They can be used to study drug delivery: Animal disease models can be used to study drug delivery and pharmacokinetics, which is important for developing new drugs and drug delivery systems.
10) They can be used to study aging: Animal disease models can be used to study the aging process and age-related diseases such as Alzheimer's and Parkinson's. This allows researchers to understand how aging contributes to disease and develop potential treatments.
There are different types of Breast Neoplasms such as:
1. Fibroadenomas: These are benign tumors that are made up of glandular and fibrous tissues. They are usually small and round, with a smooth surface, and can be moved easily under the skin.
2. Cysts: These are fluid-filled sacs that can develop in both breast tissue and milk ducts. They are usually benign and can disappear on their own or be drained surgically.
3. Ductal Carcinoma In Situ (DCIS): This is a precancerous condition where abnormal cells grow inside the milk ducts. If left untreated, it can progress to invasive breast cancer.
4. Invasive Ductal Carcinoma (IDC): This is the most common type of breast cancer and starts in the milk ducts but grows out of them and invades surrounding tissue.
5. Invasive Lobular Carcinoma (ILC): It originates in the milk-producing glands (lobules) and grows out of them, invading nearby tissue.
Breast Neoplasms can cause various symptoms such as a lump or thickening in the breast or underarm area, skin changes like redness or dimpling, change in size or shape of one or both breasts, discharge from the nipple, and changes in the texture or color of the skin.
Treatment options for Breast Neoplasms may include surgery such as lumpectomy, mastectomy, or breast-conserving surgery, radiation therapy which uses high-energy beams to kill cancer cells, chemotherapy using drugs to kill cancer cells, targeted therapy which uses drugs or other substances to identify and attack cancer cells while minimizing harm to normal cells, hormone therapy, immunotherapy, and clinical trials.
It is important to note that not all Breast Neoplasms are cancerous; some are benign (non-cancerous) tumors that do not spread or grow.
Embryonal fyn-associated substrate
NEDD9
CRKL
GRB2
CASS4
ABL (gene)
BCAR1
FYN
NPHP1
IRS4
Adapter molecule crk
RAPGEF1
PTK2
NCK1
Dock4
Dock180
List of MeSH codes (D12.644)
Integrin
PTK2B
CBL (gene)
Tropomyosin receptor kinase A
PTPN12
EPS15
RICS (gene)
Short linear motif
Cascade
IRS2
SH2 domain
Mussel
VAV2
GAB2
Cat communication
Ancient protein
2017 in archosaur paleontology
PAK1
Cellular respiration
Evolutionary history of plants
Black squirrel
Deep biosphere
CDC42
SOS1
Cephalopod
Caffeine
2021 in archosaur paleontology
Caddisfly
Seashell
Publication Detail
Biomarkers Search
HEF1 (NEDD9) (NM 006403) Human Recombinant Protein - TP307200 | OriGene
MH DELETED MN ADDED MN
MeSH Browser
Pesquisa | PrevenΓ§Γ£o e Controle de CΓ’ncer
DeCS
Interferon-Stimulated Gene Factor 3 | Profiles RNS
November | 2012 | A-Inhibitor
MH DELETED MN ADDED MN
MH DELETED MN ADDED MN
Pharos : Target Details - ABL2
MeSH Browser
MeSH Browser
NDF-RT Code NDF-RT Name
Oncogenic CDK13 mutations impede nuclear RNA surveillance - PubMed
The Journal of Cell Biology | Scholars@Duke
Tickborne Relapsing Fever, Bitterroot Valley, Montana, USA - Volume 21, Number 2-February 2015 - Emerging Infectious Diseases...
Download Broad Scale Coastal Simulation: New Techniques To Understand And Manage Shorelines In The Third Millennium 2015
Life at the extreme: lessons from the genome | Genome Biology | Full Text
Genatlas sheet
MeSH Browser
PROTEIN RPPA LIST
He cell lysates. Western blotting can then be performed making use of an antibody recognizing | rock inhibitor rockinhibitor.com
Gertrude Rainbow Fish - All About The Gertrude Fish | Spotted Blue Eye Rainbow Fish
Integrin - AbsoluteAstronomy.com
NWFSC Catalog Hierarchy | InPort
Uncategorized Archives - Northcentral Pennsylvania Conservancy
DailyMed - VYEPTI- eptinezumab-jjmr injection
Phosphorylation9
- 4. Phosphorylation of c-Abl by protein kinase Pak2 regulates differential binding of ABI2 and CRK. (nih.gov)
- 8. The C-terminal SH3 domain of the mouse c-Crk protein negatively regulates tyrosine-phosphorylation of Crk associated p130 in rat 3Y1 cells. (nih.gov)
- 11. Phosphorylation of Crk on tyrosine 251 in the RT loop of the SH3C domain promotes Abl kinase transactivation. (nih.gov)
- Engagement of the TCR by antigenic peptide bound to a histocompatibility molecule (in humans, an HLA molecule) leads to a complex set of biochemical events in which the initial activation of protein phosphorylation is critical. (nih.gov)
- These complexes contain enzymes that are regulated by protein phosphorylation and whose substrates are located at the membrane. (nih.gov)
- It undergoes tyrosine phosphorylation by C-SRC PROTEIN PP60 and plays a regulatory role in CAVEOLAE formation. (bvsalud.org)
- Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as CRK, CRKL, DOK1 or ARHGAP35. (nih.gov)
- Upon stimulation with relevant development variables, phosphorylation of downstream proteins was evaluated at a number of timepoints by probing lysate microarrays with phospho-specific antibodies. (rockinhibitor.com)
- 3.3 Proteomics Mass spectrometry-based proteomic approaches happen to be employed to identify protein phosphorylation targets downstream of development element stimulation and new technologies have allowed for the quantification of these post-translational modifications. (rockinhibitor.com)
Adapter protein2
Adaptor molecules1
- and in a group of small adaptor molecules, i.e Crk and Nck. (embl.de)
Peptides1
- Proteins and peptides are polymers of amino acids, and so the biological function of amino acids is quantitatively and qualitatively important. (nih.gov)
Pathways8
- The product of this gene has several SH2 and SH3 domains (src-homology domains) and is involved in several signaling pathways, recruiting cytoplasmic proteins in the vicinity of tyrosine kinase through SH2-phosphotyrosine interaction. (nih.gov)
- Members of this family are adhesion docking molecules that mediate protein-protein interactions for signal transduction pathways. (origene.com)
- ADP ribosylation factors (ARFs), which are members of the Ras superfamily of GTP-binding proteins, are critical components of vesicular trafficking pathways in eukaryotes. (embl.de)
- Activation of protein serine/threonine kinases and pathways coupled to small G proteins, and elevation of intracellular calcium, are examples of the events that follow. (nih.gov)
- The enhance of Separase proteolytic activity in BCR ABLpositive cells concurs with changes in respective regulatory pathways To handle the likely molecular mechanisms of how IM enhances the proteolytic activity of Separase in BCR ABL good cells, we analyzed the expression levels of respective pertinent regulatory proteins. (a-inhibitor.com)
- Similarly, complete cells lysates could be subjected to Western blotting with antibodies directed against several activated downstream effector proteins, for instance phospho-SAPK/JNK, phospho-Akt, phospho-p44/42 (Erk1/2), phospho-PLC, and so forth, to assess the status of these pathways downstream of receptor stimulation. (rockinhibitor.com)
- Non-receptor tyrosine-protein kinase implicated in the regulation of a variety of signaling pathways that control the differentiation and maintenance of normal epithelia, as well as tumor growth. (nih.gov)
- Associates also with a variety of proteins that are likely upstream of PTK6 in various signaling pathways, or for which PTK6 may play an adapter-like role. (nih.gov)
Kinase activity2
- Phosphoprotein with protein kinase activity that functions in the G2/M phase transition of the CELL CYCLE . (nih.gov)
- Diminished tyrosine protein kinase activity in T cells unresponsive to TCR stimulation. (joannecpratt.com)
Amino Acids1
- Technically, amino acids are obtained by the hydrolysis of proteins, and by chemical and microbial synthesis. (nih.gov)
Cytoplasmic1
- A number of potential nuclear and cytoplasmic substrates have been identified. (nih.gov)
Binds2
- PAPbeta, a protein that binds to and is phosphorylated by the non-receptor tyrosine kinase PYK2, contains several modular signaling domains including a pleckstrin homology domain, an SH3 domain, ankyrin repeats and an ARF-GAP domain. (embl.de)
- Tyrosine phosphorylated Cbl binds to Crk after T cell activation. (joannecpratt.com)
Tyrosine-protein Kinase1
- Non-receptor tyrosine-protein kinase that plays an ABL1-overlapping role in key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion and receptor endocytosis. (nih.gov)
Transcript1
- Unexpectedly, despite the observed decrease in separase transcript and Separase protein ranges, increased ranges of Separase proteolytic activity were measured. (a-inhibitor.com)
Biochemical2
- Proteins are biochemical compounds consisting of one or more polypeptides typically folded into a globular or fibrous form, facilitating a biological function. (absoluteastronomy.com)
- A complex protein which catalyzes a specific biochemical reaction without changing itself. (nih.gov)
Superfamily3
- The immunoglobulin superfamily is a large group of cell surface and soluble proteins that are involved in the recognition, binding, or adhesion processes of cells. (absoluteastronomy.com)
- The Ras-superfamily G-proteins play critical roles in cell growth and differentiation. (ucla.edu)
- Rheb is a novel and unique member of the Ras superfamily G-proteins. (ucla.edu)
Receptor2
- Western blotting was used to detect the relative protein expression of the sirtuin 6 (SIRT6) / NOD-like receptor thermal protein domain associated protein 3 (NLRP3) pathway. (bvsalud.org)
- 1996), LY294002 might be made use of to inhibit the receptor-binding protein PI3K (Vlahos et al. (rockinhibitor.com)
Transmembrane2
- Cadherins are a class of type-1 transmembrane proteins. (absoluteastronomy.com)
- Syndecans are single transmembrane domain proteins that are thought to act as coreceptors, especially for G protein-coupled receptors. (absoluteastronomy.com)
Sequence1
- The domains are frequently found as repeats in a single protein sequence and will then often bind both mono- and di-phosphorylated substrates. (embl.de)
Genes1
- Five subunits consisting of four different proteins from four different genes comprise the nicotinic acetylcholine receptors therefore their packaging and assembly is a very complicated process with many different factors. (growthexecutivecoaching.com)
Promotes2
Receptors2
- Following binding of the antigen-HLA complex to the TCR, receptors aggregate, associated protein tyrosine kinases (PTK) are activated, and TCR subunits and a number of linker or adapter molecules are phosphorylated on tyrosine residues. (nih.gov)
- Muscarinic receptors are G protein-coupled receptors that use a second messenger. (growthexecutivecoaching.com)
Vectors1
- 2013). Six isogenic ERK2 custom synthesis transformed human embryonic kidney cell lines expressing EGFR, FGFR1, IGF-1R, MET, PDGFR or TRKB were utilized in mixture with lentiviral shRNA expression vectors to alter the levels of intracellular signaling proteins. (rockinhibitor.com)
Apoptosis2
- This protein is a focal adhesion protein that acts as a scaffold to regulate signaling complexes important in cell attachment, migration and invasion as well as apoptosis and the cell cycle. (origene.com)
- Meanwhile, hesperetin could attenuate the expression of NLRP3, apoptosis-associated speck-like protein containing a CARD (ASC), thioredoxin-interacting protein (TXNIP), and caspase-1 p20 and upregulate the expression of SIRT6 in SCOP-induced mice. (bvsalud.org)
Complexes2
Adhesion2
- 2. Activation of the focal adhesion kinase signaling pathway by structural alterations in the carboxyl-terminal region of c-Crk II. (nih.gov)
- Cell Adhesion Molecules are proteins located on the cell surface involved with the binding with other cells or with the extracellular matrix in the process called cell adhesion. (absoluteastronomy.com)
Family5
- 12. CrkIII: a novel and biologically distinct member of the Crk family of adaptor proteins. (nih.gov)
- The protein encoded by this gene is a member of the CRK-associated substrates family. (origene.com)
- Protein tyrosine kinases of the Src family, Fyn and Lck, are associated with the TCR and TCR coreceptors, respectively. (nih.gov)
- We have identified Rheb homologues in a number of organisms including fruit fly and yeasts, and defined unique features of this family of G-protein. (ucla.edu)
- From 1985 to 1993, he was an Assistant Professor and then Associate Professor at the University of Chicago, where he initiated studies on lipid modification of the Ras family proteins. (ucla.edu)
Nucleotide2
- Crk proteins activate the Rap1 guanine nucleotide exchange factor C3G by segregated adaptor-dependent and -independent mechanisms. (nih.gov)
- The generic name for numerous enzymes that are specific for the transfer of an adenylyl group (adenosine[mono]phosphor group) from a donor molecule (usually adenosine triphosphate, ATP) to an acceptor, such as a nucleotide, a protein, and a sugar. (nih.gov)
Proline-rich1
- 14. Binding of the proline-rich segment of myelin basic protein to SH3 domains: spectroscopic, microarray, and modeling studies of ligand conformation and effects of posttranslational modifications. (nih.gov)
Initially2
- LAT, initially characterized by this laboratory, is an integral membrane protein with multiple tyrosine residues. (nih.gov)
- Cytosolic signaling adaptor proteins that were initially discovered by their role in the innate immunity ( IMMUNITY, INNATE ) response of organisms that lack an adaptive immune system. (nih.gov)
Data1
- treatment a computer our data' proteins. (quietisolation.de)
Nuclear2
Enzyme2
Inhibitors2
- Notably, these approaches can be combined with all the use of pharmacological inhibitors that let researchers to target RTK signaling pathway components at quite a few levels, with the caveat that quite a few of these inhibitors target more than 1 protein. (rockinhibitor.com)
- This led to the development of small molecule inhibitors of protein farnesyltransferase. (ucla.edu)
Homology1
- 13. Examining the specificity of Src homology 3 domain--ligand interactions with alkaline phosphatase fusion proteins. (nih.gov)
Role2
- Myocardial ischemia/reperfusion injury: the role of adaptor proteins Crk. (nih.gov)
- This protein has also been reported to have a role in cancer metastasis. (origene.com)
Regulatory1
- 9. Structure of a regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide. (nih.gov)
Cloning1
- Gu H, Pratt JC , Burakoff SJ, Neel BG Cloning of p97/Gab2, the major SHP-2 binding protein in hematopoietic cells, reveals a novel pathway for cytokine-induced gene activation. (joannecpratt.com)
Small2
- They have a preference for shallow, marginal zones of freshwater habitats including small sandy or muddy-bottomed creeks, swamps and marshes, shady rainforest streams, lily lagoons, backwaters, slow-moving streams, and overflows adjacent to larger rivers that are often less than 60cm (2ft) deep. (kayakgonflable.com)
- The small GTP-binding protein Rho potentiates AP-1 transcription in T cells. (joannecpratt.com)
Domain6
- The N-terminal SH2 domain of this protein functions as a positive regulator of transformation whereas the C-terminal SH3 domain functions as a negative regulator of transformation. (nih.gov)
- Taxonomic distribution of proteins containing SH2 domain. (embl.de)
- The complete taxonomic breakdown of all proteins with SH2 domain is also avaliable . (embl.de)
- Click on the protein counts, or double click on taxonomic names to display all proteins containing SH2 domain in the selected taxonomic class. (embl.de)
- Crystal structure of the ARF-GAP domain and ankyrin repeats of PYK2-associated protein beta. (embl.de)
- Consensus nomenclature for the human ArfGAP domain-containing proteins. (duke.edu)
Contrast1
- In contrast, p210BCR ABL expressing U937p210BCR ABL c6 On cells are much less sensitive, showing 56.8 212.3 decrease within the Separase protein amounts. (a-inhibitor.com)