CRADD Signaling Adaptor Protein: A death domain receptor signaling adaptor protein that plays a role in signaling the activation of INITIATOR CASPASES such as CASPASE 2. It contains a death domain that is specific for RIP SERINE-THEONINE KINASES and a caspase-binding domain that binds to and activates CASPASES such as CASPASE 2.Adaptor Proteins, Signal Transducing: A broad category of carrier proteins that play a role in SIGNAL TRANSDUCTION. They generally contain several modular domains, each of which having its own binding activity, and act by forming complexes with other intracellular-signaling molecules. Signal-transducing adaptor proteins lack enzyme activity, however their activity can be modulated by other signal-transducing enzymesAdaptor Proteins, Vesicular Transport: A class of proteins involved in the transport of molecules via TRANSPORT VESICLES. They perform functions such as binding to the cell membrane, capturing cargo molecules and promoting the assembly of CLATHRIN. The majority of adaptor proteins exist as multi-subunit complexes, however monomeric varieties have also been found.GRB2 Adaptor Protein: A signal transducing adaptor protein that links extracellular signals to the MAP KINASE SIGNALING SYSTEM. Grb2 associates with activated EPIDERMAL GROWTH FACTOR RECEPTOR and PLATELET-DERIVED GROWTH FACTOR RECEPTORS via its SH2 DOMAIN. It also binds to and translocates the SON OF SEVENLESS PROTEINS through its SH3 DOMAINS to activate PROTO-ONCOGENE PROTEIN P21(RAS).Shc Signaling Adaptor Proteins: A family of signaling adaptor proteins that contain SRC HOMOLOGY DOMAINS. Many members of this family are involved in transmitting signals from CELL SURFACE RECEPTORS to MITOGEN-ACTIVATED PROTEIN KINASES.Adaptor Protein Complex 2: An adaptor protein complex primarily involved in the formation of clathrin-related endocytotic vesicles (ENDOSOMES) at the CELL MEMBRANE.Adaptor Protein Complex 3: An adaptor protein complex found primarily on perinuclear compartments.Adaptor Protein Complex 1: A clathrin adaptor protein complex primarily involved in clathrin-related transport at the TRANS-GOLGI NETWORK.Chordata, Nonvertebrate: A portion of the animal phylum Chordata comprised of the subphyla CEPHALOCHORDATA; UROCHORDATA, and HYPEROTRETI, but not including the Vertebrata (VERTEBRATES). It includes nonvertebrate animals having a NOTOCHORD during some developmental stage.Chordata: Phylum in the domain Eukarya, comprised of animals either with fully developed backbones (VERTEBRATES), or those with notochords only during some developmental stage (CHORDATA, NONVERTEBRATE).Fas-Associated Death Domain Protein: A signal-transducing adaptor protein that associates with TNF RECEPTOR complexes. It contains a death effector domain that can interact with death effector domains found on INITIATOR CASPASES such as CASPASE 8 and CASPASE 10. Activation of CASPASES via interaction with this protein plays a role in the signaling cascade that leads to APOPTOSIS.Caspase 8: A long pro-domain caspase that contains a death effector domain in its pro-domain region. Caspase 8 plays a role in APOPTOSIS by cleaving and activating EFFECTOR CASPASES. Activation of this enzyme can occur via the interaction of its N-terminal death effector domain with DEATH DOMAIN RECEPTOR SIGNALING ADAPTOR PROTEINS.Ciona intestinalis: The only species of a cosmopolitan ascidian.Apoptosis: One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.Receptors, TNF-Related Apoptosis-Inducing Ligand: Tumor necrosis factor receptor family members that are widely expressed and play a role in regulation of peripheral immune responses and APOPTOSIS. The receptors are specific for TNF-RELATED APOPTOSIS-INDUCING LIGAND and signal via conserved death domains that associate with specific TNF RECEPTOR-ASSOCIATED FACTORS in the CYTOPLASM.Volvox: A genus of GREEN ALGAE in the family Volvocaceae. They form spherical colonies of hundreds or thousands of bi-flagellated cells in a semi-transparent gelatinous ball.Biological Evolution: The process of cumulative change over successive generations through which organisms acquire their distinguishing morphological and physiological characteristics.Cell Death: The termination of the cell's ability to carry out vital functions such as metabolism, growth, reproduction, responsiveness, and adaptability.Caspases: A family of intracellular CYSTEINE ENDOPEPTIDASES that play a role in regulating INFLAMMATION and APOPTOSIS. They specifically cleave peptides at a CYSTEINE amino acid that follows an ASPARTIC ACID residue. Caspases are activated by proteolytic cleavage of a precursor form to yield large and small subunits that form the enzyme. Since the cleavage site within precursors matches the specificity of caspases, sequential activation of precursors by activated caspases can occur.Caspase 3: A short pro-domain caspase that plays an effector role in APOPTOSIS. It is activated by INITIATOR CASPASES such as CASPASE 9. Isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.Apoptosis Regulatory Proteins: A large group of proteins that control APOPTOSIS. This family of proteins includes many ONCOGENE PROTEINS as well as a wide variety of classes of INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS such as CASPASES.Caenorhabditis elegans: A species of nematode that is widely used in biological, biochemical, and genetic studies.Cysteine Endopeptidases: ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.Caenorhabditis elegans Proteins: Proteins from the nematode species CAENORHABDITIS ELEGANS. The proteins from this species are the subject of scientific interest in the area of multicellular organism MORPHOGENESIS.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Tumor Necrosis Factor Receptor-Associated Peptides and Proteins: Intracellular signaling peptides and proteins that bind directly or indirectly to the cytoplasmic portion of TUMOR NECROSIS FACTOR RECEPTORS.TNF Receptor-Associated Factor 6: A signal transducing tumor necrosis factor receptor associated factor that is involved in regulation of NF-KAPPA B signalling and activation of JNK MITOGEN-ACTIVATED PROTEIN KINASES.TNF Receptor-Associated Factor 2: A signal transducing tumor necrosis factor receptor associated factor that is involved in TNF RECEPTOR feedback regulation. It is similar in structure and appears to work in conjunction with TNF RECEPTOR-ASSOCIATED FACTOR 1 to inhibit APOPTOSIS.TNF Receptor-Associated Factor 1: A signal transducing tumor necrosis factor receptor associated factor that is involved in TNF RECEPTOR feedback regulation. It is similar in structure and appears to work in conjunction with TNF RECEPTOR-ASSOCIATED FACTOR 2 to inhibit APOPTOSIS.TNF Receptor-Associated Factor 3: A signal transducing tumor necrosis factor receptor associated factor that is involved in regulation of NF-KAPPA B signaling and activation of MITOGEN-ACTIVATED PROTEIN KINASES.TNF Receptor-Associated Factor 4: A widely expressed member of the TNF receptor-associated family that may play a role in neuronal development and EMBRYOGENESIS. Although TNF receptor-associated factor 4 does not strongly associate with TUMOR NECROSIS FACTOR RECEPTORS it may be a signaling partner with the GLUCOCORTICOID-INDUCED TNFR-RELATED PROTEIN that plays a role in the activation of JNK MITOGEN-ACTIVATED PROTEIN KINASES and NF-KAPPA B.Meningioma: A relatively common neoplasm of the CENTRAL NERVOUS SYSTEM that arises from arachnoidal cells. The majority are well differentiated vascular tumors which grow slowly and have a low potential to be invasive, although malignant subtypes occur. Meningiomas have a predilection to arise from the parasagittal region, cerebral convexity, sphenoidal ridge, olfactory groove, and SPINAL CANAL. (From DeVita et al., Cancer: Principles and Practice of Oncology, 5th ed, pp2056-7)TATA-Box Binding Protein: A general transcription factor that plays a major role in the activation of eukaryotic genes transcribed by RNA POLYMERASES. It binds specifically to the TATA BOX promoter element, which lies close to the position of transcription initiation in RNA transcribed by RNA POLYMERASE II. Although considered a principal component of TRANSCRIPTION FACTOR TFIID it also takes part in general transcription factor complexes involved in RNA POLYMERASE I and RNA POLYMERASE III transcription.TATA Box: A conserved A-T rich sequence which is contained in promoters for RNA polymerase II. The segment is seven base pairs long and the nucleotides most commonly found are TATAAAA.Antibodies: Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).Antibody Specificity: The property of antibodies which enables them to react with some ANTIGENIC DETERMINANTS and not with others. Specificity is dependent on chemical composition, physical forces, and molecular structure at the binding site.Antibodies, Viral: Immunoglobulins produced in response to VIRAL ANTIGENS.Antibodies, Monoclonal: Antibodies produced by a single clone of cells.Antibodies, Bacterial: Immunoglobulins produced in a response to BACTERIAL ANTIGENS.Amido Black: A dye used to stain proteins in electrophoretic techniques. It is used interchangeably with its acid form.Neurochemistry: The study of the composition, chemical structures, and chemical reactions of the NERVOUS SYSTEM or its components.Glyceraldehyde-3-Phosphate Dehydrogenases: Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD.Rabbits: The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.Publications: Copies of a work or document distributed to the public by sale, rental, lease, or lending. (From ALA Glossary of Library and Information Science, 1983, p181)Hashimoto Disease: Chronic autoimmune thyroiditis, characterized by the presence of high serum thyroid AUTOANTIBODIES; GOITER; and HYPOTHYROIDISM.Thyroiditis, Autoimmune: Inflammatory disease of the THYROID GLAND due to autoimmune responses leading to lymphocytic infiltration of the gland. It is characterized by the presence of circulating thyroid antigen-specific T-CELLS and thyroid AUTOANTIBODIES. The clinical signs can range from HYPOTHYROIDISM to THYROTOXICOSIS depending on the type of autoimmune thyroiditis.Immunogenetics: A subdiscipline of genetics which deals with the genetic basis of the immune response (IMMUNITY).Thyroiditis, Subacute: Spontaneously remitting inflammatory condition of the THYROID GLAND, characterized by FEVER; MUSCLE WEAKNESS; SORE THROAT; severe thyroid PAIN; and an enlarged damaged gland containing GIANT CELLS. The disease frequently follows a viral infection.Graves Disease: A common form of hyperthyroidism with a diffuse hyperplastic GOITER. It is an autoimmune disorder that produces antibodies against the THYROID STIMULATING HORMONE RECEPTOR. These autoantibodies activate the TSH receptor, thereby stimulating the THYROID GLAND and hypersecretion of THYROID HORMONES. These autoantibodies can also affect the eyes (GRAVES OPHTHALMOPATHY) and the skin (Graves dermopathy).Thyroid Gland: A highly vascularized endocrine gland consisting of two lobes joined by a thin band of tissue with one lobe on each side of the TRACHEA. It secretes THYROID HORMONES from the follicular cells and CALCITONIN from the parafollicular cells thereby regulating METABOLISM and CALCIUM level in blood, respectively.Thyroglobulin

Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria. (1/30)

Caspase-2 is one of the earliest identified caspases, but the mechanism of caspase-2-induced apoptosis remains unknown. We show here that caspase-2 engages the mitochondria-dependent apoptotic pathway by inducing the release of cytochrome c (Cyt c) and other mitochondrial apoptogenic factors into the cell cytoplasm. In support of these observations we found that Bcl-2 and Bcl-xL can block caspase-2- and CRADD (caspase and RIP adaptor with death domain)-induced cell death. Unlike caspase-8, which can process all known caspase zymogens directly, caspase-2 is completely inactive toward other caspase zymogens. However, like caspase-8, physiological levels of purified caspase-2 can cleave cytosolic Bid protein, which in turn can trigger the release of Cyt c from isolated mitochondria. Interestingly, caspase-2 can also induce directly the release of Cyt c, AIF (apoptosis-inducing factor), and Smac (second mitochondria-derived activator of caspases protein) from isolated mitochondria independent of Bid or other cytosolic factors. The caspase-2-released Cyt c is sufficient to activate the Apaf-caspase-9 apoptosome in vitro. In combination, our data suggest that caspase-2 is a direct effector of the mitochondrial apoptotic pathway.  (+info)

Delineation of RAID1, the RACK1 interaction domain located within the unique N-terminal region of the cAMP-specific phosphodiesterase, PDE4D5. (2/30)

BACKGROUND: The cyclic AMP specific phosphodiesterase, PDE4D5 interacts with the beta-propeller protein RACK1 to form a signaling scaffold complex in cells. Two-hybrid analysis of truncation and mutant constructs of the unique N-terminal region of the cAMP-specific phosphodiesterase, PDE4D5 were used to define a domain conferring interaction with the signaling scaffold protein, RACK1. RESULTS: Truncation and mutagenesis approaches showed that the RACK1-interacting domain on PDE4D5 comprised a cluster of residues provided by Asn-22/Pro-23/Trp-24/Asn-26 together with a series of hydrophobic amino acids, namely Leu-29, Val-30, Leu-33, Leu-37 and Leu-38 in a 'Leu-Xaa-Xaa-Xaa-Leu' repeat. This was done by 2-hybrid analyses and then confirmed in biochemical pull down analyses using GST-RACK1 and mutant PDE4D5 forms expressed in COS cells. Mutation of Arg-34, to alanine, in PDE4D5 attenuated its interaction with RACK1 both in 2-hybrid screens and in pull down analyses. A 38-mer peptide, whose sequence reflected residues 12 through 49 of PDE4D5, bound to RACK1 with similar affinity to native PDE4D5 itself (Ka circa 6 nM). CONCLUSIONS: The RACK1 Interaction Domain on PDE4D5, that we here call RAID1, is proposed to form an amphipathic helical structure that we suggest may interact with the C-terminal beta-propeller blades of RACK1 in a manner akin to the interaction of the helical G-gamma signal transducing protein with the beta-propeller protein, G-beta.  (+info)

RAIDD aggregation facilitates apoptotic death of PC12 cells and sympathetic neurons. (3/30)

In human cell lines, the caspase 2 adaptor RAIDD interacts selectively with caspase 2 through its caspase recruitment domain (CARD) and leads to caspase 2-dependent death. Whether RAIDD induces such effects in neuronal cells is unknown. We have previously shown that caspase 2 is essential for apoptosis of trophic factor-deprived PC12 cells and rat sympathetic neurons. We report here that rat RAIDD, cloned from PC12 cells, interacts with rat caspase 2 CARD. RAIDD overexpression induced caspase 2 CARD- and caspase 9-dependent apoptosis of PC12 cells and sympathetic neurons. Apoptosis correlated with the formation of discrete perinuclear aggregates. Both death and aggregates required the expression of full-length RAIDD. Such aggregates may enable more effective activation of caspase 2 through close proximity. Following trophic deprivation, RAIDD overexpression increased death and aggregate formation. Therefore, RAIDD aggregation is important for its death-promoting effects and may play a role in trophic factor withdrawal-induced neuronal apoptosis.  (+info)

The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress. (4/30)

Apoptosis is triggered by activation of initiator caspases upon complex-mediated clustering of the inactive zymogen, as occurs in the caspase-9-activating apoptosome complex. Likewise, caspase-2, which is involved in stress-induced apoptosis, is recruited into a large protein complex, the molecular composition of which remains elusive. We show that activation of caspase-2 occurs in a complex that contains the death domain-containing protein PIDD, whose expression is induced by p53, and the adaptor protein RAIDD. Increased PIDD expression resulted in spontaneous activation of caspase-2 and sensitization to apoptosis by genotoxic stimuli. Because PIDD functions in p53-mediated apoptosis, the complex assembled by PIDD and caspase-2 is likely to regulate apoptosis induced by genotoxins.  (+info)

Association of caspase-2 with the promyelocytic leukemia protein nuclear bodies. (5/30)

Apoptotic cell death is executed by a family of cysteine proteases known as caspases. Synthesized as inactive precursors, caspases become activated sequentially in cascades. Activation of apical or initiator caspases in these cascades occurs in macromolecular complexes located in various compartments. One such complex is the plasma membrane-bound death-inducing signaling complex (DISC), formed upon engagement of death receptors, which recruits and activates caspase-8 and -10. Another complex is the cytosolic apoptosome, assembled in response to the release of mitochondrial cytochrome c, which recruits caspase-9. The other major human initiator caspase is caspase-2, which is activated in response to various lethal stimuli and has recently been shown to be required for DNA damage-induced apoptosis. The regulation of caspase-2 is not well understood. Here we present evidence that caspase-2 is localized to the promyelocytic leukemia protein nuclear bodies (PML-NBs), nuclear macro-molecular complexes that are involved in many scenarios of apoptosis including DNA damage. The localization of caspase-2 requires both the prodomain and protease domain but appears to be independent of its adaptor protein, CRADD/RAIDD. These data suggest the existence of a nuclear apoptosis pathway that involves both caspase-2 and the PML-NBs.  (+info)

RAIDD is required for apoptosis of PC12 cells and sympathetic neurons induced by trophic factor withdrawal. (6/30)

Caspase 2 has been implicated in trophic deprivation-induced neuronal death. We have shown that overexpression of the caspase 2-binding protein RAIDD induces neuronal apoptosis, acting synergistically with trophic deprivation. Currently, we examine the role of endogenous RAIDD in apoptosis of PC12 cells and sympathetic neurons. Expression of a truncated caspase recruitment domain-only form of caspase 2, which presumably disrupts the RAIDD interaction with endogenous caspase 2, attenuated trophic deprivation-induced apoptosis. Furthermore, downregulation of RAIDD by small interfering RNA led to inhibition of trophic deprivation-induced death, whereas death induced by DNA damage, which is not caspase 2-mediated, was not inhibited. Therefore, RAIDD, likely through interaction with caspase 2, is involved in trophic deprivation-induced neuronal apoptosis. This is the first demonstration of the involvement of RAIDD in apoptosis, and provides further support for the idea that apoptotic pathways in the same system may differ depending on the initiating stimulus.  (+info)

Apoptosis caused by p53-induced protein with death domain (PIDD) depends on the death adapter protein RAIDD. (7/30)

The p53 tumor suppressor promotes cell cycle arrest or apoptosis in response to diverse stress stimuli. p53-mediated cell death depends in large part on transcriptional up-regulation of target genes. One of these targets, P53-induced protein with a death domain (PIDD), was shown to function as a mediator of p53-dependent apoptosis. Here we show that PIDD is a cytoplasmic protein, and that PIDD-induced apoptosis and growth suppression in embryonic fibroblasts depend on the adaptor protein receptor-interacting protein (RIP)-associated ICH-1/CED-3 homologous protein with a death domain (RAIDD). We provide evidence that PIDD-induced cell death is associated with the early activation of caspase-2 and later activation of caspase-3 and -7. Our results also show that caspase-2(-/-), in contrast to RAIDD(-/-), mouse embryonic fibroblasts, are only partially resistant to PIDD. Our findings suggest that caspase-2 contributes to PIDD-mediated cell death, but that it is not the sole effector of this pathway.  (+info)

PIDD mediates NF-kappaB activation in response to DNA damage. (8/30)

Activation of NF-kappaB following genotoxic stress allows time for DNA-damage repair and ensures cell survival accounting for acquired chemoresistance, an impediment to effective cancer therapy. Despite this clinical relevance, little is known about pathways that enable genotoxic-stress-induced NF-kappaB induction. Previously, we reported a role for the p53-inducible death-domain-containing protein, PIDD, in caspase-2 activation and apoptosis in response to DNA damage. We now demonstrate that PIDD plays a critical role in DNA-damage-induced NF-kappaB activation. Upon genotoxic stress, a complex between PIDD, the kinase RIP1, and a component of the NF-kappaB-activating kinase complex, NEMO, is formed. PIDD expression enhances genotoxic-stress-induced NF-kappaB activation through augmented sumoylation and ubiquitination of NEMO. Depletion of PIDD and RIP1, but not caspase-2, abrogates DNA-damage-induced NEMO modification and NF-kappaB activation. We propose that PIDD acts as a molecular switch, controlling the balance between life and death upon DNA damage.  (+info)

Daxx (phospho Ser739) antibody (death-domain associated protein) for WB. Anti-Daxx (phospho Ser739) pAb (GTX55302) is tested in Human, Mouse, Rat samples. 100% Ab-Assurance.
09:39, 30 April 2015 Homo sapiens:Apoptosis Modulation and Signaling‎ (Corrected ID for AIFM1,CASP4,CASP2,CASP1,HSPA1A,PIDD,TP53,PRKD1,NAIP,XIAP,AIFM2,RIPK1 and PEA15 genes) ...
DAXX(death-domain associated protein) also known as DAP6(Death-associated protein 6) or BING2, was first discovered through its cytoplasmic…
Primary humoral immunodeficiency or primary immune deficiency diseases (PIDD) is a group of disorders in which the immune system of an individual does not function properly. In PIDD patients, the number of antibodies produced in the body is not sufficient, or the ones produced are defective. PIDDs are thus often characterized by increased vulnerability to infections. According to the International Union of Immunological Societies (IUIS), PIDD is a compilation of more than 150 different diseases.. Request for Sample Report: http://www.mrrse.com/sample/3381. This report on the Subcutaneous Immunoglobulin Market analyzes the current and future prospects of the market. The report comprises an elaborate executive summary, including a market snapshot that provides overall information of various segments and sub-segments. The research is a combination of primary and secondary research. Detailed qualitative analysis of factors responsible for driving and restraining market growth and opportunities has ...
Vol 70: Purification, crystallization and preliminary X-ray crystallographic studies of Rv3705c from Mycobacterium tuberculosis.. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
rdf:RDF xmlns:dcterms="http://purl.org/dc/terms/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#" xmlns:foaf="http://xmlns.com/foaf/0.1/" xmlns:void="http://rdfs.org/ns/void#" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" , ,rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/20913", ,dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/20913/2/4%20se0220%20edit.pdf"/, ,dc:contributor,Zeth, Kornelius,/dc:contributor, ,foaf:homepage rdf:resource="http://localhost:8080/jspui"/, ,dc:creator,Zeth, Kornelius,/dc:creator, ,dc:contributor,Diederichs, Kay,/dc:contributor, ,dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/, ,dc:creator,Schnaible, Volker,/dc:creator, ,dc:creator,Diederichs, Kay,/dc:creator, ,dc:contributor,Engelhardt, ...
American Health & Drug Benefits® examines drug and other healthcare intervention value from the separate and unified vantage points of each stakeholder group to the process: payers, purchasers, providers, patients, manufacturers, regulators, distributors, and evaluators. Directly or indirectly, all parties to healthcare benefits influence policy and demand satisfaction of their interests.
The Division of Immunology provides diagnostic and therapeutic services for both children and adults with a suspected or known primary immune deficiency disorder (PIDD). We see patients referred from throughout the WWAMI region (Washington, Wyoming, Alaska, Montana, and Idaho) and serve as a tertiary referral base for a regional population of more than 10 million. We also evaluate and treat PIDD patients referred from throughout the U.S. and abroad.. Members of our faculty each have active research programs within the Center for Immunity and Immunotherapies (CII) at Seattle Childrens Research Institute. Our faculty have played key roles in identifying the molecular basis for many of the now more than 140 molecularly defined PIDDs, and in pioneering clinical care for these diseases. Our faculty also work closely with members of Fred Hutchinson Cancer Research Center (FHCRC) and Seattle Cancer Care Alliance (SCCA) to coordinate care for PIDD patients undergoing hematopoietic stem cell ...
NIH clinicians have cared for people with unusual and difficult-to-treat immune disorders for decades," says NIAID Director Anthony S. Fauci, M.D. "This study exemplifies their commitment to improving the lives of people with these diseases by trying to uncover the causes of these disorders and thereby better understanding how to treat them.". Combined immunodeficiency is a type of primary immune deficiency disease (PIDD) in which several parts of the immune system are affected. This inherited disorder is characterized by increased susceptibility to bacterial, viral and fungal infections of various organs of the body. In some cases, susceptibility to cancers also may be seen.. There are 150 known PIDDs. Approximately 500,000 people in the United States have been diagnosed with a PIDD, while many more remain undiagnosed.. The NIAID and NCI investigators recognized that certain patients with an undefined form of combined immunodeficiency shared enough clinical features to make it likely that the ...
Mitochondrial antiviral-signaling protein also known as CARD adapter inducing interferon-beta (Cardif/IPS-1) [13] CRADD: ... The adaptor protein VISA further activates the IKK-protein-kinase family members. Although the canonical IKK family members ... Death adaptor molecule RAIDD-2 [15] RIG-I: Retinoic acid-inducible gene 1 protein, also known as DEAD-box protein 58 (DDX58) [ ... Recently, studies on the NLR protein Ipaf-1 have provided insight into how CARD proteins participate in the immune response. ...
To activate IKK, TAB2 and TAB3 adaptor proteins recruit TAK1 or MEKK3, which phosphorylate the complex. This results in the ... Distinct domains for nuclear factor-kappaB activation and association with tumor necrosis factor signaling proteins". The ... Ahmad M, Srinivasula SM, Wang L, Talanian RV, Litwack G, Fernandes-Alnemri T, Alnemri ES (February 1997). "CRADD, a novel human ... Chen D, Li X, Zhai Z, Shu HB (May 2002). "A novel zinc finger protein interacts with receptor-interacting protein (RIP) and ...
... CASP2 and RIPK1 domain containing adaptor with death domain". Tinel A, Tschopp J (May 2004). "The PIDDosome, a protein ... Through its CARD domain, this protein interacts with, and thus recruits, caspase 2/ICH1 to the cell death signal transduction ... Death domain-containing protein CRADD is a protein that in humans is encoded by the CRADD gene. The protein encoded by this ... Human CRADD genome location and CRADD gene details page in the UCSC Genome Browser. Lennon G, Auffray C, Polymeropoulos M, ...
Lin Q, Liu Y, Moore DJ, Elizer SK, Veach RA, Hawiger J, Ruley HE (2012). "Cutting edge: the "death" adaptor CRADD/RAIDD targets ... which are thought to function as upstream regulators in NF-kappaB signaling. This protein is found to form a complex with the ... This protein is reported to interact with other CARD domain containing proteins including CARD9, 10, 11 and 14, ... "c-E10 is a caspase-recruiting domain-containing protein that interacts with components of death receptors signaling pathway and ...
... which bound to the adaptor proteins CRADD or TRAF6 (tumor necrosis factor receptor-associated factor 6) to convey distinct ... especially given that amphioxus contains 14 DR proteins and hundreds of death domain (DD)-containing adaptor proteins. To ... Science Signaling. 14 Sep 2010. : ra66 Death domain-dependent signaling in the basal chordate amphioxus suggests that extrinsic ... Science Signaling. 14 Sep 2010. : ra66 Death domain-dependent signaling in the basal chordate amphioxus suggests that extrinsic ...
A death domain receptor signaling adaptor protein that plays a role in signaling the activation of INITIATOR CASPASES such as ... CRADD Signaling Adaptor Protein. Known as: CRADD Signaling Adaptor Protein [Chemical/Ingredient], RAIDD Signaling Adaptor ... RIP Associated Protein With a Death Domain Expand. A death domain receptor signaling adaptor protein that plays a role in ... An antimicrobial protein of the Riptortus pedestris salivary gland was cleaved by a virulence factor of Serratia marcescens ...
Death adaptor molecule RAIDD antibody. *Death domain containing protein CRADD antibody. *Death domain-containing protein CRADD ... In the presence of RIP and TRADD, CRADD recruits caspase-2 to the TNFR-1 signalling complex. ... Apoptotic adaptor molecule specific for caspase-2 and FASL/TNF receptor-interacting protein RIP. ... Proteins and Peptides. Proteomics tools. Agonists, activators, antagonists and inhibitors. Lysates. Multiplex miRNA assays. By ...
Intracellular adaptor proteins (such as TRADD, FADD/MORT1, RIP, RAIDD/CRADD and Reaper) have death domain homologous regions* ... that bind to the DDs of Fas and TNFR1,16-19 thereby relaying signals to a further series of proteins, variously known as the ... The first line proteins are those containing a so-called death domain (DD). Some of these are trans-membrane proteins with a ... Rb, (retinoblastoma protein) and other functionally related proteins, are critical regulators of cell proliferation and ...
... signal transduction by interacting with a variety of signaling adaptor proteins such as CRADD SIGNALING ADAPTOR PROTEIN; TNF ... Forkhead Box Protein O1. A forkhead box transcription factor that is a major target of INSULIN signaling and regulator of ... The aim of the study is to investigate the effects of blocking IL-6 signaling with tocilizumab on lipid, glucose and protein ... Although they were initially described as death domain-binding adaptor proteins, members of this family may contain other ...
CRADD (caspase and RIP adapter with death domain), which binds to the prodomain of caspase-2 and recruits it to the signalling ... receptor-interacting protein (RIP)-associated ICH-1/CED-3-homologous protein with a death domain]/ ... These proteins are characterized by almost absolute specificity for aspartic acid in the P1 position. All the caspases (ICE- ... In the nematode Caenorhabditis elegans, the gene ced-3 encodes a protein required for developmental cell death. Since the ...
CRADD: Caspase and RIP adapter with death domain also known as RIP-associated protein with a death domain (RAIDD) [14] ... MAVS: Mitochondrial antiviral-signaling protein also known as CARD adapter inducing interferon-beta (Cardif) [13] ... RAIDD-2: Death adaptor molecule RAIDD-2 [15]. *RIG-I: Retinoic acid-inducible gene 1 protein, also known as DEAD-box protein 58 ... Antiviral signaling. Recently, a subset of CARD proteins has been shown to participate in recognition of intracellular double- ...
To activate IKK, TAB2 and TAB3 adaptor proteins recruit TAK1 or MEKK3, which phosphorylate the complex. This results in the ... Distinct domains for nuclear factor-kappaB activation and association with tumor necrosis factor signaling proteins". The ... Ahmad M, Srinivasula SM, Wang L, Talanian RV, Litwack G, Fernandes-Alnemri T, Alnemri ES (February 1997). "CRADD, a novel human ... Chen D, Li X, Zhai Z, Shu HB (May 2002). "A novel zinc finger protein interacts with receptor-interacting protein (RIP) and ...
Mitochondrial antiviral-signaling protein also known as CARD adapter inducing interferon-beta (Cardif/IPS-1) [13] CRADD: ... The adaptor protein VISA further activates the IKK-protein-kinase family members. Although the canonical IKK family members ... Death adaptor molecule RAIDD-2 [15] RIG-I: Retinoic acid-inducible gene 1 protein, also known as DEAD-box protein 58 (DDX58) [ ... Recently, studies on the NLR protein Ipaf-1 have provided insight into how CARD proteins participate in the immune response. ...
CRADD Signaling Adaptor Protein - genetics Cognitive Dysfunction - epidemiology - genetics Cohort Studies DNA Copy Number ... DNA-Binding Proteins - genetics - metabolism Epigenesis, Genetic Female Finland Genetic Predisposition to Disease Germ-Line ... Proto-Oncogene Proteins - genetics - metabolism RNA, Small Interfering - metabolism Whole Genome Sequencing Abstract. Clonal ... we identify a Finland enriched homozygote variant in the CRADD ID associated gene. ...
Death adaptor molecule RAIDD. *Death domain containing protein CRADD. *Death domain-containing protein CRADD ... In the presence of RIP and TRADD, CRADD recruits caspase-2 to the TNFR-1 signalling complex. ... Apoptotic adaptor molecule specific for caspase-2 and FASL/TNF receptor-interacting protein RIP. ... The Universal Protein Resource (UniProt) in 2010. Nucleic Acids Res. 38:D142-D148 (2010) . ...
Caspase and RIP adapter with death domain) (RIP-associated protein with a death domain) ... Bioclone provides recombinant protein codon optimized cDNA clone for P78560 CRADD Death domain-containing protein CRADD ( ... Signal Transduction. *CD Marker. *Drug metabolism * Neuroscience *Common Disease. *Cytokine. *Allergy & Toxin Protein. * much ... CRADD Protein Source. Recombinant protein.. Recombinant CRADD Protein Applications. Western Blot, may be used for other ...
CRADD Signaling Adaptor Protein. *Edar-Associated Death Domain Protein. *Fas-Associated Death Domain Protein ... Adaptor Proteins, Signal Transducing [D12.644.360.024]. *Death Domain Receptor Signaling Adaptor Proteins [D12.644.360.024.296] ... Adaptor Proteins, Signal Transducing [D12.776.157.057]. *Death Domain Receptor Signaling Adaptor Proteins [D12.776.157.057.024] ... Adaptor Proteins, Signal Transducing [D12.776.476.024]. *Death Domain Receptor Signaling Adaptor Proteins [D12.776.476.024.375] ...
CRADD. Death domain-containing protein CRADD ; Apoptotic adaptor molecule specific for caspase-2 and FASL/TNF receptor- ... interacting protein RIP. In the presence of RIP and TRADD, CRADD recruits caspase-2 to the TNFR-1 signalling complex (By ... CRADD. ANK1. ENSPPYP00000005515. ENSPPYP00000020798. Death domain-containing protein CRADD ; Apoptotic adaptor molecule ... CRADD. ANKRD44. ENSPPYP00000005515. ENSPPYP00000014573. Death domain-containing protein CRADD ; Apoptotic adaptor molecule ...
2000) 14‐3‐3 interacts with regulator of G protein signaling proteins and modulates their activity. The Journal of Biological ... 1997) CRADD, a novel human apoptotic adaptor molecule for caspase‐2, and FasL/tumor necrosis factor receptor‐interacting ... 2005) A human proteinprotein interaction network: a resource for annotating the proteome. Cell 122 (6): 957-968. ... Al‐Tawashi A, Jung SY, Liu D, Su B and Qin J (2012) Protein implicated in nonsyndromic mental retardation regulates protein ...
CRADD Signaling Adaptor Protein D12.644.360.24.296.50 D12.644.360.24.285.50 D12.776.157.57.04.186 D12.776.157.57.06.186 CREB- ... GRB2 Adaptor Protein D12.644.360.24.297 D12.644.360.24.290 GRB7 Adaptor Protein D12.644.360.24.298 D12.644.360.24.299 Great ... Nod Signaling Adaptor Proteins D12.644.360.24.307 D12.644.360.24.313 D12.776.157.57.68 D12.644.360.539.500 D12.776.157.57.78 ... Nod1 Signaling Adaptor Protein D12.644.360.24.307.249 D12.644.360.24.313.249 D12.776.157.57.04.249 D12.644.360.539.500.249 ...
CRADD Signaling Adaptor Protein. *Edar-Associated Death Domain Protein. *Fas-Associated Death Domain Protein ... Adaptor Proteins, Signal Transducing [D12.644.360.024]. *Tumor Necrosis Factor Receptor-Associated Peptides and Proteins [ ... Adaptor Proteins, Signal Transducing [D12.776.157.057]. *Tumor Necrosis Factor Receptor-Associated Peptides and Proteins [ ... Adaptor Proteins, Signal Transducing [D12.776.476.024]. *Tumor Necrosis Factor Receptor-Associated Peptides and Proteins [ ...
CRADD, caspase 2 and receptor-interacting serine-threonine kinase domain-containing adaptor with death domain; FMR, fragile X ... A schematic representation of the FAK and Shc/Fyn pathways in integrin signaling. The proteins are color-coded to reflect their ... Signaling pathways. Animals rely on cell-cell signaling for cellular coordination during and after development (64). Various ... Origins of developmental signaling pathway components inferred in the eumetazoan ancestor. ERK, extracellular signal-regulated ...
Anti-TATA binding protein TBP antibody [1TBP18] - ChIP Grade (ab818) has been cited in 161 publications. References for Human, ... Qiao H et al. The adaptor CRADD/RAIDD controls activation of endothelial cells by proinflammatory stimuli. J Biol Chem 289: ... Epigenetics and Nuclear Signaling Transcription Polymerase associated factors Pol II Transcription TFIID ... Gjyshi O et al. Activated Nrf2 Interacts with Kaposis Sarcoma-Associated Herpesvirus Latency Protein LANA-1 and Host Protein ...
1); this is supported by nuclear magnetic resonance structure analysis and mutagenesis studies (28). An adapter protein called ... TNFR1 can engage an adapter called RAIDD or CRADD (50). RAIDD binds through a death domain to the death domain of RIP and ... TRADD functions as a platform adapter that recruits several signaling molecules to the activated receptor: TNFR-associated ... A family of viral proteins called vFLIPs and a related cellular protein called cFLIP (also called Casper, I-FLICE, FLAME, or ...
CRADD Signaling Adaptor Protein. Proteína Adaptadora de Sinalização CRADD. Proteína Adaptadora de Señalización CRADD. ... Death Domain Receptor Signaling Adaptor Proteins. Proteínas Adaptadoras de Sinalização de Receptores de Domínio de Morte. ... CARD Signaling Adaptor Proteins. Proteínas Adaptadoras de Sinalização CARD. Proteínas Adaptadoras de Señalización CARD. ... Nod Signaling Adaptor Proteins. Proteínas Adaptadoras de Sinalização Nod. Proteínas Adaptadoras de Señalización Nod. ...
CRADD Signaling Adaptor Protein. *Nod1 Signaling Adaptor Protein. *Nod2 Signaling Adaptor Protein ... CARD Signaling Adaptor Proteins*CARD Signaling Adaptor Proteins. *Caspase Activation and Recruitment Domain Signaling Proteins ... "CARD Signaling Adaptor Proteins" by people in this website by year, and whether "CARD Signaling Adaptor Proteins" was a major ... "CARD Signaling Adaptor Proteins" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH ( ...
... revealed a homozygous frameshift variant in CRADD, which encodes an adaptor protein that interacts with PIDD and caspase-2 to ... axon regeneration promoted by suppression of CASP2 and CASP6 is CNTF-dependent and mediated through the JAK/STAT signalling ... Caspases mediate cellular apoptosis through the proteolytic cleavage of specific protein substrates. The encoded protein may ... neural precursor cell expressed developmentally down-regulated protein 2 , protein phosphatase 1, regulatory subunit 57 , ...
CRADD CASP2 and RIPK1 domain containing adaptor with death domain". Tinel A, Tschopp J (May 2004). "The PIDDosome, a protein ... Through its CARD domain, this protein interacts with, and thus recruits, caspase 2/ICH1 to the cell death signal transduction ... Death domain-containing protein CRADD is a protein that in humans is encoded by the CRADD gene. The protein encoded by this ... Human CRADD genome location and CRADD gene details page in the UCSC Genome Browser. Lennon G, Auffray C, Polymeropoulos M, ...
Lin Q, Liu Y, Moore DJ, Elizer SK, Veach RA, Hawiger J, Ruley HE (2012). "Cutting edge: the "death" adaptor CRADD/RAIDD targets ... which are thought to function as upstream regulators in NF-kappaB signaling. This protein is found to form a complex with the ... This protein is reported to interact with other CARD domain containing proteins including CARD9, 10, 11 and 14, ... "c-E10 is a caspase-recruiting domain-containing protein that interacts with components of death receptors signaling pathway and ...
  • To understand how the extrinsic apoptotic pathway was originally established and what the differences in signaling are between invertebrates and vertebrates, we performed functional studies of several genes that encode DDs in the amphioxus Branchiostoma belcheri tsingtauense (Bbt). (sciencemag.org)
  • Thus, our study not only reveals the evolutionary origin of the extrinsic apoptotic pathway in a basal chordate but also adds to our understanding of the similarities and differences between invertebrate and vertebrate FADD signaling. (sciencemag.org)
  • Survival signals from the cell's environment and internal sensors for cellular integrity normally keep a cell's apoptotic machinery in check. (sciencemag.org)
  • We demonstrate here that HSV induces an apoptotic response in microglial cells which is mediated through TLR2 signaling. (biomedcentral.com)
  • This gene encodes an integral outer mitochondrial membrane protein that blocks the apoptotic death of some cells such as lymphocytes. (antibodies-online.com)
  • Anti-apoptotic signalling that may increase cell survival and promote tumourigenesis was also evident. (beds.ac.uk)
  • This results in the recruit of the IKK complex activating proteins (TAK1, TAB1 and TAB2) so eventually NF-kB can now too migrate to the nucleus. (wikipedia.org)
  • Independently, PIDD was also described as a DD-containing protein with unknown function. (abcam.com)
  • The N-terminal region of PIDD contains seven leucine-rich repeats (LRRs), a protein interaction motif found in various proteins with diverse functions, followed by two ZU-5 domains and a C-terminal DD. (abcam.com)
  • The consequence of such non-homeostatic immune system activation, characterised using whole blood leukocyte transcriptome, highlight changes in major canonical signalling pathways of cellular function, metabolism, in both innate and adaptive immune systems. (ox.ac.uk)
  • Extrinsic death receptor pathways are induced through ligands that bind to a family of death receptor proteins (e.g. the FAS and TRAIL receptors) containing a cytoplasmic death domain. (antibodies-online.com)
  • This processing makes the CARD domains available for interaction with the CARD motif of IPS-1/MAVS/VISA/Cardif, a downstream adapter anchored in the mitochondria. (wikidoc.org)
  • RIPK2 is involved in this TLR-mediated signalling, which suggests that there might be a regulation of cell survival or death (the two possible outcomes) through the mutual interaction between the two RIPK family members. (wikipedia.org)
  • CARD domains are a subclass of protein motif known as the death fold , which features an arrangement of six to seven antiparallel alpha helices with a hydrophobic core and an outer face composed of charged residues. (wikidoc.org)
  • This antibody gave a positive signal in human liver tissue lysate. (abcam.com)
  • Immunologically, the transition from infection to sepsis represents an inflection point in the race between the human immune system devised to detect danger signals and overwhelm pathogens, ideally without causing a non-homeostatic systemic activation of immune cells. (ox.ac.uk)