A member of the Bcl-2 protein family that reversibly binds MEMBRANES. It is a pro-apoptotic protein that is activated by caspase cleavage.
Membrane proteins encoded by the BCL-2 GENES and serving as potent inhibitors of cell death by APOPTOSIS. The proteins are found on mitochondrial, microsomal, and NUCLEAR MEMBRANE sites within many cell types. Overexpression of bcl-2 proteins, due to a translocation of the gene, is associated with follicular lymphoma.
A member of the Bcl-2 protein family and homologous partner of C-BCL-2 PROTO-ONCOGENE PROTEIN. It regulates the release of CYTOCHROME C and APOPTOSIS INDUCING FACTOR from the MITOCHONDRIA. Several isoforms of BCL2-associated X protein occur due to ALTERNATIVE SPLICING of the mRNA for this protein.
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.

Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis. (1/724)

Here we report that in staurosporine-induced apoptosis of HeLa cells, Bid, a BH3 domain containing protein, translocates from the cytosol to mitochondria. This event is associated with a change in conformation of Bax which leads to the unmasking of its NH2-terminal domain and is accompanied by the release of cytochrome c from mitochondria. A similar finding is reported for cerebellar granule cells undergoing apoptosis induced by serum and potassium deprivation. The Bax-conformational change is prevented by Bcl-2 and Bcl-xL but not by caspase inhibitors. Using isolated mitochondria and various BH3 mutants of Bid, we demonstrate that direct binding of Bid to Bax is a prerequisite for Bax structural change and cytochrome c release. Bcl-xL can inhibit the effect of Bid by interacting directly with Bax. Moreover, using mitochondria from Bax-deficient tumor cell lines, we show that Bid- induced release of cytochrome c is negligible when Bid is added alone, but dramatically increased when Bid and Bax are added together. Taken together, our results suggest that, during certain types of apoptosis, Bid translocates to mitochondria and binds to Bax, leading to a change in conformation of Bax and to cytochrome c release from mitochondria.  (+info)

Solution structure of BID, an intracellular amplifier of apoptotic signaling. (2/724)

We report the solution structure of BID, an intracellular cross-talk agent that can amplify FAS/TNF apoptotic signal through the mitochondria death pathway after Caspase 8 cleavage. BID contains eight alpha helices where two central hydrophobic helices are surrounded by six amphipathic ones. The fold resembles poreforming bacterial toxins and shows similarity to BCL-XL although sequence homology to BCL-XL is limited to the 16-residue BH3 domain. Furthermore, we modeled a complex of BCL-XL and BID by aligning the BID and BAK BH3 motifs in the known BCL-XL-BAK BH3 complex. Additionally, we show that the overall structure of BID is preserved after cleavage by Caspase 8. We propose that BID has both BH3 domain-dependent and -independent modes of action in inducing mitochondrial damage.  (+info)

Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists. (3/724)

Members of the BCL2 family of proteins are key regulators of programmed cell death, acting either as apoptotic agonists or antagonists. Here we describe the solution structure of BID, presenting the structure of a proapoptotic BCL2 family member. An analysis of sequence/structure of BCL2 family members allows us to define a structural superfamily, which has implications for general mechanisms for regulating proapoptotic activity. It appears two criteria must be met for proapoptotic function within the BCL2 family: targeting of molecules to intracellular membranes, and exposure of the BH3 death domain. BID's activity is regulated by a Caspase 8-mediated cleavage event, exposing the BH3 domain and significantly changing the surface charge and hydrophobicity, resulting in a change of cellular localization.  (+info)

Caspases induce cytochrome c release from mitochondria by activating cytosolic factors. (4/724)

We investigated the ability of caspases (cysteine proteases with aspartic acid specificity) to induce cytochrome c release from mitochondria. When Jurkat cells were induced to undergo apoptosis by Fas receptor ligation, cytochrome c was released from mitochondria, an event that was prevented by the caspase inhibitor, zVAD-fmk (zVal-Ala-Asp-CH2F). Purified caspase-8 triggered rapid cytochrome c release from isolated mitochondria in vitro. The effect was indirect, as the presence of cytosol was required, suggesting that caspase-8 cleaves and activates a cytosolic substrate, which in turn is able to induce cytochrome c release from mitochondria. The cytochrome c releasing activity was not blocked by caspase inhibition, but was antagonized by Bcl-2 or Bcl-xL. Caspase-8 and caspase-3 cleaved Bid, a proapoptotic Bcl-2 family member, which gains cytochrome c releasing activity in response to caspase cleavage. However, caspase-6 and caspase-7 did not cleave Bid, although they initiated cytochrome c release from mitochondria in the presence of cytosol. Thus, effector caspases may cleave and activate another cytosolic substrate (other than Bid), which then promotes cytochrome c release from mitochondria. Mitochondria significantly amplified the caspase-8 initiated DEVD-specific cleavage activity. Our data suggest that cytochrome c release, initiated by the action of caspases on a cytosolic substrates, may act to amplify a caspase cascade during apoptosis.  (+info)

Ion channel activity of the BH3 only Bcl-2 family member, BID. (5/724)

BID is a member of the BH3-only subgroup of Bcl-2 family proteins that displays pro-apoptotic activity. The NH(2)-terminal region of BID contains a caspase-8 (Casp-8) cleavage site and the cleaved form of BID translocates to mitochondrial membranes where it is a potent inducer of cytochrome c release. Secondary structure and fold predictions suggest that BID has a high degree of alpha-helical content and structural similarity to Bcl-X(L), which itself is highly similar to bacterial pore-forming toxins. Moreover, circular dichroism analysis confirmed a high alpha-helical content of BID. Amino-terminal truncated BIDDelta1-55, mimicking the Casp-8-cleaved molecule, formed channels in planar bilayers at neutral pH and in liposomes at acidic pH. In contrast, full-length BID displayed channel activity only at nonphysiological pH 4.0 (but not at neutral pH) in planar bilayers and failed to form channels in liposomes even under acidic conditions. On a single channel level, BIDDelta1-55 channels were voltage-gated and exhibited multiconductance behavior at neutral pH. When full-length BID was cleaved by Casp-8, it too demonstrated channel activity similar to that seen with BIDDelta1-55. Thus, BID appears to share structural and functional similarity with other Bcl-2 family proteins known to have channel-forming activity, but its activity exhibits a novel form of activation: proteolytic cleavage.  (+info)

A novel BH3-like domain in BID is required for intramolecular interaction and autoinhibition of pro-apoptotic activity. (6/724)

Upon activation of the Fas apoptotic signaling pathway, Bid, a "BH3 domain-only" pro-apoptotic molecule, is cleaved by caspase-8 into a 6.5-kDa N-terminal and a 15-kDa BH3 domain-containing C-terminal fragment, referred to as t(n)-Bid and t(c)-Bid, respectively. t(c)-Bid is a more potent inducer of apoptosis than full-length Bid, suggesting that the N-terminal region of Bid has an inhibitory effect on its pro-apoptotic activity. Here, we report the identification of a novel BH3-like motif (amino acid residues 35-43) in t(n)-Bid. Although Bid does not homodimerize, t(n)-Bid is able to associate avidly with t(c)-Bid. Site-directed mutagenesis revealed that both the novel BH3-like and BH3 domains are necessary for direct binding between t(n)-Bid and t(c)-Bid. While full-length Bid does not associate with t(n)-Bid, substitution of Leu(35), a critical residue in mediating t(n)-Bid/t(c)-Bid interaction, with Ala in full-length Bid is sufficient to establish Bid/t(n)-Bid interaction. Interestingly, the L35A Bid mutant is as effective as t(c)-Bid in inducing apoptosis and binding Bcl-X(L). We propose that the intramolecular interaction involving the BH3-like and BH3 domains serves to regulate the pro-apoptotic potential of Bid.  (+info)

The tyrosine kinase lck is required for CD95-independent caspase-8 activation and apoptosis in response to ionizing radiation. (7/724)

Induction of apoptosis is a hallmark of cytostatic drug and radiation-induced cell death in human lymphocytes and lymphoma cells. However, the mechanisms leading to apoptosis are not well understood. We provide evidence that ionizing radiation induces a rapid activation of caspase-8 (FLICE) followed by apoptosis independently of CD95 ligand/receptor interaction. The radiation induced cleavage pattern of procaspase-8 into mature caspase-8 resembled that following CD95 crosslinking and resulted in cleavage of the proapoptotic substrate BID. Overexpression of dominant-negative caspase-8 interfered with radiation-induced apoptosis. Caspase-8 activation by ionizing radiation was not observed in cells genetically defective for the Src-like tyrosine kinase Lck. Cells lacking Lck also displayed a marked resistance towards apoptosis induction upon ionizing radiation. After retransfection of Lck, caspase-8 activation and the capability to undergo apoptosis in response to ionizing radiation was restored. We conclude that radiation activates caspase-8 via an Lck-controlled pathway independently of CD95 ligand expression. This is a novel signaling event required for radiation induced apoptosis in T lymphoma cells.  (+info)

Evidence for a function of death-receptor-related, death-domain-containing proteins in anoikis. (8/724)

Normal epithelial cells undergo apoptosis if integrinmediated matrix contacts are lost, in a process termed 'anoikis'. Anoikis prevents shed epithelial cells from colonizing elsewhere, and is thus essential for maintaining appropriate tissue organisation. Aberrant oncogenes or tumor suppressor genes can cause resistance to anoikis, thereby contributing substantially to malignancy. Apoptosis is mediated by a well-ordered signaling cascade, which involves activation of intracellular proteases known as caspases. However, the mechanism by which the caspase cascade is initiated following cell-matrix detachment is unknown. We have hypothesized that death receptor activation might be involved in anoikis. To test this hypothesis, we developed a transient assay for anoikis and used it to assay the effects of proteins that block the function of domains found within death receptors known as death domains. In this assay, silencer of death domains (SODD) and dominant-negative FAS-associated death domain protein (FADD) efficiently inhibited anoikis in Madin-Darby canine kidney (MDCK) cells. The protective activity of SODD required its BAG domain, which interacts with the heat shock proteins hsp70 and hsc70, and inhibits the chaperone activity of the latter. Both caspase 8, which physically associates with death receptors, and cleavage of the caspase-8 substrate BID, were activated by cell-matrix detachment. These findings indicate a role for death receptors or proteins with related death domains in triggering anoikis.  (+info)

BH3 Interacting Domain Death Agonist Protein, also known as BAD protein, is a member of the Bcl-2 family of proteins. This protein is involved in the regulation of programmed cell death, or apoptosis. The BH3 domain of BAD protein allows it to interact with other members of the Bcl-2 family and modulate their function. When activated, BAD protein can promote cell death by binding to and inhibiting anti-apoptotic proteins such as Bcl-2 and Bcl-xL. This helps to release pro-apoptotic proteins such as Bax and Bak, which can then trigger the intrinsic pathway of apoptosis. The activation of BAD protein is tightly regulated by post-translational modifications, including phosphorylation and dephosphorylation, which can be influenced by various signals within the cell.

Proto-oncogene proteins c-bcl-2 are a group of proteins that play a role in regulating cell death (apoptosis). The c-bcl-2 gene produces one of these proteins, which helps to prevent cells from undergoing apoptosis. This protein is located on the membrane of mitochondria and endoplasmic reticulum and it can inhibit the release of cytochrome c, a key player in the activation of caspases, which are enzymes that trigger apoptosis.

In normal cells, the regulation of c-bcl-2 protein helps to maintain a balance between cell proliferation and cell death, ensuring proper tissue homeostasis. However, when the c-bcl-2 gene is mutated or its expression is dysregulated, it can contribute to cancer development by allowing cancer cells to survive and proliferate. High levels of c-bcl-2 protein have been found in many types of cancer, including leukemia, lymphoma, and carcinomas, and are often associated with a poor prognosis.

BCL-2-associated X protein, often abbreviated as BAX, is a type of protein belonging to the BCL-2 family. The BCL-2 family of proteins plays a crucial role in regulating programmed cell death, also known as apoptosis. Specifically, BAX is a pro-apoptotic protein, which means that it promotes cell death.

BAX is encoded by the BAX gene, and it functions by forming pores in the outer membrane of the mitochondria, leading to the release of cytochrome c and other pro-apoptotic factors into the cytosol. This triggers a cascade of events that ultimately leads to cell death.

Dysregulation of BAX and other BCL-2 family proteins has been implicated in various diseases, including cancer and neurodegenerative disorders. For example, reduced levels of BAX have been observed in some types of cancer, which may contribute to tumor growth and resistance to chemotherapy. On the other hand, excessive activation of BAX has been linked to neuronal death in conditions such as Alzheimer's disease and Parkinson's disease.

Apoptosis is a programmed and controlled cell death process that occurs in multicellular organisms. It is a natural process that helps maintain tissue homeostasis by eliminating damaged, infected, or unwanted cells. During apoptosis, the cell undergoes a series of morphological changes, including cell shrinkage, chromatin condensation, and fragmentation into membrane-bound vesicles called apoptotic bodies. These bodies are then recognized and engulfed by neighboring cells or phagocytic cells, preventing an inflammatory response. Apoptosis is regulated by a complex network of intracellular signaling pathways that involve proteins such as caspases, Bcl-2 family members, and inhibitors of apoptosis (IAPs).

... cancer cell's susceptibility to apoptosis via TNF-α signalling by the BH3 interacting domain death agonist and STAT proteins. ... Waiwut, P; Inujima, A; Inoue, H; Saiki, I; Sakurai, H (January 2012). "Bufotalin sensitizes death receptor-induced apoptosis ...
The BH3 interacting-domain death agonist, or BID, gene is a pro-apoptotic member of the Bcl-2 protein family. Bcl-2 family ... The BH3 interacting-domain death agonist has been shown to interact with: ATR/ATRIP, BCL2, CASP2, CASP8, MCL1, and RPA. Several ... Wang K, Yin XM, Chao DT, Milliman CL, Korsmeyer SJ (1996). "BID: a novel BH3 domain-only death agonist". Genes Dev. 10 (22): ... BID is a pro-apoptotic Bcl-2 protein containing only the BH3 domain. In response to apoptotic signaling, BID interacts with ...
Apoptosis Apoptosome Bcl-2 Bcl-2-associated X protein (BAX) BH3 interacting domain death agonist (BID) Caspases Cytochrome c ... Kim JY, Ahn HJ, Ryu JH, Suk K, Park JH (2004). "BH3-only protein Noxa is a mediator of hypoxic cell death induced by hypoxia- ... Phorbol-12-myristate-13-acetate-induced protein 1 is a protein that in humans is encoded by the PMAIP1 gene, and is also known ... until displaced by BH3-only proteins". Genes Dev. 19 (11): 1294-305. doi:10.1101/gad.1304105. PMC 1142553. PMID 15901672. Alves ...
Apoptosis Apoptosome Bcl-2 Bcl-2-associated X protein (BAX) BH3 interacting domain death agonist (BID) Caspases Cytochrome c ... The PUMA protein is part of the BH3-only subgroup of Bcl-2 family proteins. This group of proteins only share sequence ... "Structure of the BH3 domains from the p53-inducible BH3-only proteins Noxa and Puma in complex with Mcl-1". J. Mol. Biol. 380 ( ... Webster KA (July 2006). "Puma joins the battery of BH3-only proteins that promote death and infarction during myocardial ...
BH3 interacting-domain death agonist) Luis Moroder, Rudolf K. Allemann N. Umezawa; Y. Noro; K. Ukai; N. Kato; T. Higuchi. (2011 ... The same design principle has been applied to inhibit protein-protein interactions involved in cancer and can be used for any ... Photoswitchable peptides to inhibit protein-protein interactions in a light-controlled manner have been developed and applied ... "Light-Regulated Stapled Peptides to Inhibit Protein-Protein Interactions Involved in Clathrin-Mediated Endocytosis". Angewandte ...
Apoptosome Bcl-2 homologous antagonist killer (BAK) Bcl-2-associated X protein (BAX) BH3 interacting domain death agonist (BID ... Hsu SY, Lin P, Hsueh AJ (September 1998). "BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing ... These pro-apoptotic proteins are in turn activated by BH3-only proteins, and are inhibited by the function of BCL-2 and its ... and induces cell death independent of a Bcl-2 homology 3 (BH3) domain at both mitochondrial and nonmitochondrial sites". The ...
... which initiate the intrinsic pathway of apoptosis by cleaving BH3 interacting-domain death agonist (Bid) into tBid, another pro ... "A novel protein, MUDENG, induces cell death in cytotoxic T cells". Biochemical and Biophysical Research Communications. 370 (3 ... "A novel protein, MUDENG, induces cell death in cytotoxic T cells". Biochemical and Biophysical Research Communications. 370 (3 ... "A novel protein, MUDENG, induces cell death in cytotoxic T cells". Biochemical and Biophysical Research Communications. 370 (3 ...
USA BH3 interacting domain death agonist, a pro-apoptotic protein Binary integer decimal Brought in dead, a patient found dead ...
The pro-apoptotic BH3-interacting domain death agonist (Bid) is one such protein that once myristoylated, translocates to the ... Myristoylation allows for weak protein-protein and protein-lipid interactions and plays an essential role in membrane targeting ... These conformational switches can be utilized as a signal for cellular localization, membrane-protein, and protein-protein ... death receptor binding initiates the formation of the death-inducing signaling complex, a complex composed of numerous proteins ...
After the protein BH3 interacting-domain death agonist (Bid) has been myristoylated, it targets the protein to move to the ... the site where the lipids bind to the protein depends both on the lipid group and protein. Prenylated proteins are proteins ... This allows for the interaction of proteins with cellular membranes and protein domains. In a dynamic role[clarification needed ... Lipid-anchored proteins (also known as lipid-linked proteins) are proteins located on the surface of the cell membrane[of what ...
... bcl-x protein MeSH D12.644.360.075.718.968 - bh3 interacting domain death agonist protein MeSH D12.644.360.100 - ca(2+)- ... proto-oncogene proteins c-bcl-2 MeSH D12.644.360.075.718.100 - bcl-associated death protein MeSH D12.644.360.075.718.400 - bcl- ... 14-3-3 proteins MeSH D12.644.360.024.318 - proto-oncogene proteins c-crk MeSH D12.644.360.024.326 - proto-oncogene proteins c- ... ral gtp-binding proteins MeSH D12.644.360.525.462 - ran gtp-binding protein MeSH D12.644.360.525.475 - rap gtp-binding proteins ...
Apoptosis Apoptosome Bcl-2 BH3 interacting domain death agonist (BID) Caspases Cytochrome c Noxa Mitochondrion p53 upregulated ... binds the BH3 domain of other BAX or BCL-2 proteins in its active form. In the protein's inactive form, the groove binds its ... This protein forms a heterodimer with BCL2, and functions as an apoptotic activator. This protein is reported to interact with ... domains (named BH1, BH2, BH3 and BH4), and can form hetero- or homodimers. These domains are composed of nine α-helices, with a ...
... as a pro-apoptotic protein due to the conserved BH3 interacting domain death agonist located at the C-terminus of the protein ... with the most extensive conservation being found at the C-terminus of the protein. The BH3 interacting-domain death agonist ( ... The C6orf222 protein contains one mammalian conserved domain: DUF3293. The protein is also predicted to contain a BH3 domain, ... A predicted BH3 domain in the C6orf222 protein was found to interact with both Bcl-2 and Bcl-xL, implicating C6orf222 as being ...
... has been shown to interact with: BH3 interacting domain death agonist, CRADD, and Caspase 8. The Proteolysis Map ... a long pro-domain that is similar to that of caspase 9 and contains a protein interaction domain known as a CARD domain. Pro- ... Together with RAIDD and p53-induced protein with a death domain ([PIDD])(LRDD), caspase 2 has been shown to form the so-called ... including RIP-associated Ich-1/Ced-3-homologue protein with a death domain (RAIDD), apoptosis repressor with caspase ...
... bcl-x protein MeSH D12.776.476.075.718.937 - bh3 interacting domain death agonist protein MeSH D12.776.476.150.300.100 - casein ... bcl-associated death protein MeSH D12.776.476.075.718.400 - bcl-2-associated x protein MeSH D12.776.476.075.718.425 - bcl-2 ... smad1 protein MeSH D12.776.476.024.417.500.200 - smad2 protein MeSH D12.776.476.024.417.500.300 - smad3 protein MeSH D12.776. ... smad proteins, inhibitory MeSH D12.776.476.024.417.249.600 - smad6 protein MeSH D12.776.476.024.417.249.700 - smad7 protein ...
This protein shares a critical BH3 domain with other death-promoting proteins, BAX and BAK. Bcl-2-interacting killer has been ... a BH3-containing mouse protein that interacts with Bcl-2 and Bcl-xL, is a potent death agonist". J. Biol. Chem. 273 (14): 7783- ... a novel death-inducing protein shares a distinct sequence motif with Bcl-2 family proteins and interacts with viral and ... Han J, Sabbatini P, White E (1996). "Induction of apoptosis by human Nbk/Bik, a BH3-containing protein that interacts with E1B ...
The protein encoded by this gene contains a Bcl-2 homology domain 3 (BH3). It has been shown to interact with other members of ... 1996). "BID: a novel BH3 domain-only death agonist". Genes Dev. 10 (22): 2859-69. doi:10.1101/gad.10.22.2859. PMID 8918887. Zha ... Bcl-2-like protein 11, commonly called BIM (Bcl-2 Interacting Mediator of cell death), is a protein that in humans is encoded ... Hsu SY, Lin P, Hsueh AJ (November 1998). "BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing ...
1998). "Blk, a BH3-containing mouse protein that interacts with Bcl-2 and Bcl-xL, is a potent death agonist". J. Biol. Chem. ... a conserved nuclear phosphoprotein that contains multiple tetratricopeptide repeats and binds specifically to SH2 domains". J. ... The tyrosine-protein kinase BLK has been shown to interact with UBE3A. ENSG00000285369 GRCh38: Ensembl release 89: ... 1993). "Mapping of sites on the Src family protein tyrosine kinases p55blk, p59fyn, and p56lyn which interact with the effector ...
Identification of a BH-3 domain and analysis of its binding to mutant BCL-2 and BCL-XL proteins". J. Biol. Chem. 272 (49): ... The BCL2 associated agonist of cell death (BAD) protein is a pro-apoptotic member of the Bcl-2 gene family which is involved in ... encodes a protein that activates apoptosis and interacts selectively with survival-promoting proteins Bcl-2 and Bcl-X(L)". EMBO ... "The proapoptotic BH3-only protein BAD transduces cell death signals independently of its interaction with Bcl-2". Cell Death ...
Milliman CL, Korsmeyer SJ, Wang K, Yin XM, Chao DT (1996). "BID: a novel BH3 domain-only death agonist". Genes Dev. 10 (22): ... The BH3-only subset of the Bcl-2 family of proteins contain only a single BH3-domain. The BH3-only members play a key role in ... Arbel, Nir; Shoshan-Barmatz, Varda (2010-02-26). "Voltage-dependent anion channel 1-based peptides interact with Bcl-2 to ... or those proteins that have only the BH3 domain (e.g. Bim Bid and BAD) All proteins belonging to the Bcl-2 family contain ...
Autophagy Autoschizis Bcl-2 BH3 interacting domain death agonist (BID) Calpains Caspases Cell damage Cornification Cytochrome c ... Research on the corn poppy (Papaver rhoeas) has revealed that proteins in the pistil on which the pollen lands, interact with ... Programmed cell death (PCD; sometimes referred to as cellular suicide) is the death of a cell as a result of events inside of a ... Apoptosis and Cell Death Labs International Cell Death Society The Bcl-2 Family Database (Webarchive template wayback links, ...
Pierrat B, Ito M, Hinz W, Simonen M, Erdmann D, Chiesi M, Heim J (May 2000). "Uncoupling proteins 2 and 3 interact with members ... Zha J, Harada H, Yang E, Jockel J, Korsmeyer SJ (1997). "Serine phosphorylation of death agonist BAD in response to survival ... "Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function". Mol. ... This article incorporates text from the United States National Library of Medicine, which is in the public domain. (Articles ...
... and Fas-associated death domain protein (FADD). cIAP1/2 can inhibit TNF-α signaling by binding to TRAF2. FLIP inhibits the ... Bax or Bak are activated by the activation of BH3-only proteins, part of the Bcl-2 family. Caspases play the central role in ... Akt phosphorylates and inhibits Bad (a Bcl-2 family member), causing Bad to interact with the 14-3-3 scaffold, resulting in Bcl ... therefore overexpression leads to a decrease in the number of proapoptotic agonists. As a consequence, the balance of anti- ...
... induces BAK/BAX-dependent release of cytochrome c and other mitochondrial intermembrane proteins to the cytosol to induce ... BH3 Interacting Domain Death Agonist Protein / genetics * BH3 Interacting Domain Death Agonist Protein / pharmacology* ... Truncated BID (tBID), a proapoptotic BCL2 family protein, induces BAK/BAX-dependent release of cytochrome c and other ... BH3 Interacting Domain Death Agonist Protein * Bak1 protein, mouse * Bid protein, mouse ...
Herein, we review the role of glycans and glycan-binding proteins as essential components of the cell death machinery during ... Glycans, either alone or complexed with glycan-binding proteins, can deliver intracellular signals or control extracellular ... glycosylation also has an integral role in many processes leading to cell death. ... processes that promote initiation, execution and resolution of cell death programs. ...
BH3 interacting domain death agonist, a pro-apoptotic protein. *Binary Integer Decimal ...
Protein Aliases: apoptic d; apoptic death agonist; BH3-interacting domain death agonist; BH3-interacting domain death agonist ... BH3-interacting domain death agonist p13; BH3-interacting domain death agonist p15; BID; BID isoform ES(1b); BID isoform L(2); ... Recombinant protein BH3 Interacting Domain Death Agonist. The antigen corresponds to amino acid range 1-195 of the target ... BID is a death agonist that heterodimerizes with either agonist BAX or antagonist BCL2. Bid is a member of the BCL-2 family of ...
... cancer cells susceptibility to apoptosis via TNF-α signalling by the BH3 interacting domain death agonist and STAT proteins. ... Waiwut, P; Inujima, A; Inoue, H; Saiki, I; Sakurai, H (January 2012). "Bufotalin sensitizes death receptor-induced apoptosis ...
Other proteins such as K-Ras or BH3 interacting domain death agonist can also induce cell death when activated by caspases by ... Jacobs, B. L., van Praag, H., and Gage, F. H. (2000). Depression and the birth and death of brain cells: the turnover of ... Herrmann, J. M., and Neupert, W. (2000). Protein transport into mitochondria. Curr. Opin. Microbiol. 3, 210-214. doi: 10.1016/ ... In addition, mitochondria also play a prominent role in the regulation of apoptotic cell death (for examples, see Davidson and ...
Rat BID (BH3 Interacting Domain Death Agonist) CLIA Kit , G-EC-01770 ... Rat TP53 (Tumor Protein 53) CLIA Kit , G-EC-02142 Rat TP53 (Tumor Protein 53) CLIA Kit , G-EC-02142 , Gentaur Clia KitsTarget ... Rat IGFBP-3 (Insulin-Like Growth Factor Binding Protein 3) CLIA Kit , G-EC-01961 ... Rat LRP-1 (Low-Density Lipoprotein-Receptor-Related Protein) CLIA Kit , G-EC-01990 ...
BH3 Interacting Domain Death Agonist Protein * Endothelial Cells * Humans * Interferon-gamma * Lipid Metabolism ... a BH3 domain deletion allele of ApoL1 was unable to induce ACD, demonstrating that ApoL1 is a bona fide BH3-only pro-death ... ApoL1, a BH3-only lipid-binding protein, induces autophagic cell death. Academic Article * ... We recently reported the identification and characterization of a novel BH3-only pro-death protein, apolipoprotein L1 (ApoL1), ...
Bcl-2 associated x protein; Bcl-2, B-cell lymphoma 2; BID, BH3 Interacting-domain Death agonist; E2F1, E2F transcription factor ... The Bcl-2 family of proteins, which includes the proapoptotic proteins Bax and Bak and the antiapoptotic protein Bcl-2, is ... In contrast, Ca2+ influx through L-type VGCC causes death in bovine chromaffin cells [16]. Notably, [Ca2+]i-mediated cell death ... The extrinsic mechanism involves the linking of membrane death receptors to adapter proteins, which bind and position pro- ...
... inhibitory protein], Bcl-2 family members, inhibitors of apoptosis proteins, and PI3K/AKT signaling. Studying such mechanisms ... upregulation of anti-apoptotic proteins including c-FLIP [cellular FLICE (FADD-like IL-1β-converting enzyme)- ... Bcl-2-associated X protein; BID: BH3 interacting domain death agonist; Mcl-1: myeloid cell leukemia sequence 1; Bak: BCL-2- ... associated death domain protein (TRADD) is an adaptor protein in TNFR1 signaling and participates in NF-κB activation as well ...
The BH3-interacting domain death agonist (BID) serves as a caspase substrate that engages the mitochondrial pathway to amplify ... other pro-apoptotic BH3-only proteins, Bcl-2 interacting mediator of cell death (BIM) and Bcl-2-associated death promoter (BAD ... F-box only protein 9 (FBXO9), caprin family member 2 (CAPRIN2), the CAP-Gly domain-containing linker protein 1 (CLIP1), ... The EBV transforming protein, latent membrane protein 1, mimics and cooperates with CD40 signaling in B lymphocytes. J Immunol ...
Bid, BH3-interacting domain death agonist, was initially cloned based in its ability to interact with both Bcl-2 and Bax. Bid ... contains only the BH3 domain, which is required for its interaction with the Bcl-2 family proteins and for its pro-death ... Dissolve the lyophilized protein in distilled water.. Stability And Storage. Reconstituted protein stable at -80°C for 12 ... Bid is important to cell death mediated by these proteases and thus is the sentinel to protease-mediated death signals.. ...
... and PARP and decreased levels of mu-2-related death-inducing gene protein expression with BH3-interacting domain death agonist ... XAF1 interacts with ERα and BRCA1 via the zinc finger (ZF) domains 5/6 and 4, respectively, and the mutants lacking either of ... Mechanistically, XAF1 interacts with and destabilizes ER stress sensor GRP78 through the assembly of zinc finger protein 313 ( ... Moreover, XAF1 expression is activated through PERK-Nrf2 signaling and destabilizes C-terminus of Hsc70-interacting protein ( ...
BH3 interacting domain death agonist. protein-coding. BAG3. BCL2 associated athanogene 3. protein-coding. ... BTB domain containing 9. protein-coding. B3GNT7. UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 7. protein-coding ... bone morphogenetic protein receptor type 1B. protein-coding. BRAF. B-Raf proto-oncogene, serine/threonine kinase. protein- ... bromodomain adjacent to zinc finger domain 2A. protein-coding. BTBD9. ...
BID; BH3 interacting domain death agonist [KO:K04726]. 581 BAX; BCL2 associated X, apoptosis regulator [KO:K02159]. ... TIRAP; TIR domain containing adaptor protein [KO:K05403]. 4615 MYD88; MYD88 innate immune signal transduction adaptor [KO: ... HSPA9; heat shock protein family A (Hsp70) member 9 [KO:K04043]. 3329 HSPD1; heat shock protein family D (Hsp60) member 1 [KO: ... MAPK1; mitogen-activated protein kinase 1 [KO:K04371] [EC:2.7.11.24]. 5595 MAPK3; mitogen-activated protein kinase 3 [KO:K04371 ...
BH3 Interacting Domain Death Agonist Protein [D12.644.360.075.718.968] BH3 Interacting Domain Death Agonist Protein ... BH3 Interacting Domain Death Agonist Protein [D12.776.476.075.718.937] BH3 Interacting Domain Death Agonist Protein ... B Cell Leukemia 2 Family Proteins BCL2 Family Proteins BCL2 Proteins Family Proteins, BCL2 Proteins, BCL2 Proteins, BCL2 Family ... BCL2 Family Proteins. BCL2 Proteins. Family Proteins, BCL2. Proteins, BCL2. Proteins, BCL2 Family. Proto Oncogene Proteins c ...
Interferon induced with helicase C domain 1 3.5 BID BH3 interacting domain death agonist 2.3 ... a BH3-only protein promoting cytochrome c release, had been connected to MYC-induced cell-death priming.47 Most significantly, ... Ribosomal protein S3: a KH domain subunit in NF-kappaB complexes that mediates selective gene regulation. ... c-Myc blazing a trail of death: coupling of the mitochondrial and death receptor apoptosis pathways by c-Myc. ...
Proteins - Apoptosis Regulatory Proteins * Proteins - BH3 Interacting Domain Death Agonist Protein * Proteins - Bcl-2-Like ... Peptides - Apoptosis Regulatory Proteins * Peptides - BH3 Interacting Domain Death Agonist Protein * Peptides - Bcl-2-Like ...
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Rat Bid(BH3 Interacting Domain Death Agonist) ELISA Kit. *Rat C3a(Complement Component 3a) ELISA Kit ... Mouse vWA1(Von Willebrand Factor A Domain Containing Protein 1) ELISA Kit ... Mouse vWA1(Von Willebrand Factor A Domain Containing Protein 1) ELISA Kit ... Rat Angiopoietin Like Protein 4 (ANGPTL4) ELISA Kit. SEB019Ra-5x96wellstestplate Cloud-Clone 5x96-wells test plate. 3182.08 EUR ...
Human BID / BH3-interacting domain death agonist ELISA Kit. E0629h. 人. 96T. 1.25-80ng/mL. ... Human BNIP3L / BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like ELISA Kit ... Human BNIP3 / BCL2/adenovirus E1B 19 kDa protein-interacting protein 3 ELISA Kit ...
BH3 interacting-domain death agonist FLICE-like inhibitory protein caspase 8 pro-caspase 3 ... CARD16 (Caspase recruitment domain-containing protein 16, caspase-1 inhibitor COP, CARD only domain-containing protein 1, ... apoptotic protease Mch-4 , FLICE2 , ICE-like apoptotic protease 4 , FAS-associated death domain protein interleukin-1B- ... 2003) Distinctive roles of PHAP proteins and prothymosin-alpha in a death regulatory pathway. Science, 299 (5604): 223-6. [PMID ...
BH3 interacting domain death agonist. 22q11.1. Expression. GO_Annotation. GSMA_I. PMID:cooccur. ... death-domain associated protein. 6p21.3. CV:PGCnp. DMG:Wockner_2014. GSMA_I. PMID:cooccur. Ascano FMRP targets. Chromatin ... SH3 domain binding glutamate rich protein like 2. 6q14.1. CV:PGCnp. DMG:Wockner_2014. G2Cdb.humanPSD. G2Cdb.humanPSP. ... guanylate binding protein 1. 1p22.2. CV:PGCnp. PMID:cooccur. 2634. GBP2. -. guanylate binding protein 2. 1p22.2. CV:PGCnp. DEG: ...
BH3-interacting domain death agonist. BID. P55957. 1 Reference(s). T23P74. Caspase-9. CASP9. P55211. 9 Reference(s). ... CCAAT/enhancer-binding protein beta. CEBPB. P17676. 1 Reference(s). T16MRU. NACHT, LRR and PYD domains-containing protein 3. ... Ras association domain-containing protein 1. RASSF1. Q9NS23. 1 Reference(s). T79UQC. C-X-C motif chemokine 10. CXCL10. P02778. ... Thioredoxin-interacting protein. TXNIP. Q9H3M7. 1 Reference(s). T64BPL. Solute carrier family 23 member 1. SLC23A1. Q9UHI7. 1 ...
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Description: A sandwich ELISA kit for detection of BH3 Interacting Domain Death Agonist from Rat in samples from blood, serum, ... High-throughput screening to discover inhibitors of the CarD·RNA polymerase protein-protein interaction in Mycobacterium ... Description: A sandwich CLIA kit for quantitative measurement of Rat BID (BH3 Interacting Domain Death Agonist) in samples from ... Description: A sandwich ELISA kit for quantitative measurement of Rat BID (BH3 Interacting Domain Death Agonist) in samples ...
... inhibitors of apoptosis proteins, B-cell lymphoma 2 (BCL-2) family proteins, and several other proteases such as perforins and ... This review aims to elaborate on apoptotic signaling pathways and mechanisms, interacting members involved in signaling, and ... which stabilize the selection of cellular survival or death. However, any aberration in this pathway can lead to abnormal cell ... Apoptosis is regulated by a complex signaling mechanism, which is driven by interactions among several protein families such as ...
  • Truncated BID (tBID), a proapoptotic BCL2 family protein, induces BAK/BAX-dependent release of cytochrome c and other mitochondrial intermembrane proteins to the cytosol to induce apoptosis. (nih.gov)
  • BID is a death agonist that heterodimerizes with either agonist BAX or antagonist BCL2. (thermofisher.com)
  • Several MYC-induced pathways, such as activation of the p53/ARF pathway, changes in expression, and activity of BCL2 proteins or alterations in death receptor signaling have been linked to apoptosis. (ashpublications.org)
  • A0A8C0MK34_BBC3-01 BCL2 binding component 3 protein OS=[Eukaryota] Canis lupus familiaris GN=BBC3 (length=193 residues). (inserm.fr)
  • A0A8C0N2N7_BAD-01 BCL2-associated agonist of cell death protein OS=[Eukaryota] Canis lupus familiaris GN=BAD (length=167 residues). (inserm.fr)
  • A0A8C0NKD6_BCL2L11-04 BCL2-like 11 protein OS=[Eukaryota] Canis lupus familiaris GN=BCL2L11 (length=87 residues). (inserm.fr)
  • A0A8C0PT40_BMF-01 Bcl2 modifying factor protein OS=[Eukaryota] Canis lupus familiaris GN=BMF (length=203 residues). (inserm.fr)
  • Thus, VDAC2 acts as a crucial component in mitochondrial apoptosis by allowing the mitochondrial recruitment of BAK, thereby controlling tBID-induced OMM permeabilization and cell death. (nih.gov)
  • BID serves as a direct molecular link between caspase 8 activation and mitochondrial death machinery. (thermofisher.com)
  • In this review, we summarize some of the latest knowledge on mitochondrial dysregulation in major depression (depicted in Figure 1 ) and also discuss how mitochondrial dysfunction could instigate downstream changes in extracellular matrix proteins such as reelin, neuronal nitric oxide (nNOS), oxidative stress, and inflammation, and finally adult hippocampal neurogenesis. (frontiersin.org)
  • The proteins are found on mitochondrial, microsomal, and NUCLEAR MEMBRANE sites within many cell types. (bvsalud.org)
  • We discuss here the contribution of glycan-lectin interactions to the initiation, execution and resolution of apoptosis and their emerging roles in other cell death programs including autophagy. (nature.com)
  • ApoL1 failed to induce ACD in autophagy-deficient Atg5(-/-) and Atg7(-/-) MEF cells, suggesting that ApoL1-induced cell death is indeed autophagy-dependent. (unm.edu)
  • In comparison, the inhibition of autophagy reduced the phrase amounts of ATG protein in the tissue targeted by NDV. (immune-source.com)
  • Description: Quantitativesandwich ELISA kit for measuring Human myelin basic protein, MBP in samples from serum, plasma, tissue homogenates, cell culture supernates. (lscwarsaw.com)
  • Description: Quantitativesandwich ELISA kit for measuring Human p53/tumor protein, p53/TP53 in samples from serum, cell culture supernates, urine, cerebrospinalfluid (CSF), tissue homogenates, cell lysates. (ksiazkiwnauce.pl)
  • Description: Quantitativesandwich ELISA kit for measuring Human protein disulfide isomerase, PDI in samples from serum, plasma, tissue homogenates. (knoblauchpublishing.com)
  • Membrane proteins encoded by the BCL-2 GENES and serving as potent inhibitors of cell death by APOPTOSIS. (bvsalud.org)
  • Members of the mammalian inhibitors of apoptosis proteins (IAP) are able to bind the procaspases, thereby preventing maturation to active proteinases. (guidetopharmacology.org)
  • Mtd-induced apoptosis was not blocked by broad range synthetic caspase inhibitors z-VAD-fmk or a viral protein CrmA. (deathbase.org)
  • ApoL1, a BH3-only lipid-binding protein, induces autophagic cell death. (unm.edu)
  • We recently reported the identification and characterization of a novel BH3-only pro-death protein, apolipoprotein L1 (ApoL1), that, when overexpressed, induces autophagic cell death (ACD) in a variety of cells, including those originated from normal and cancerous tissues. (unm.edu)
  • MYC induces proliferation, but at the same time it can induce cell death. (ashpublications.org)
  • A Mtd mutant with glutamine substitutions of highly conserved amino acids in the BH3 domain retained its ability to promote apoptosis, further indicating that Mtd does not promote apoptosis by heterodimerizing with Bcl-2 or Bcl-XL. (deathbase.org)
  • In addition to its role in glucose metabolism, this pathway also regulates the redirection of free amino acids to protein synthesis via the mTOR-signaling pathway. (hindawi.com)
  • NF-κB up-regulates Fas and predisposes to Fas-induced cell death, which is caspase-8 mediated and can be prevented by CFLAR overexpression. (ashpublications.org)
  • The Bcl-2 family of proteins, which includes the proapoptotic proteins Bax and Bak and the antiapoptotic protein Bcl-2, is implicated in the intrinsic mechanism of apoptosis [ 6 ] . (encyclopedia.pub)
  • Expression of Mtd promoted the death of primary sensory neurons, 293T cells and HeLa cells, indicating that Mtd is a proapoptotic protein. (deathbase.org)
  • Proliferation is upregulated through two mechanisms: (1) ATP binding to the G-protein-coupled receptor P2Y2, commencing a kinase signaling cascade that activates the serine-threonine kinase Akt, and (2) the transactivation of the epidermal growth factor receptor (EGFR), leading to a series of protein signals that activate the extracellular signal-regulated kinases (ERK) 1/2. (encyclopedia.pub)
  • However, recent studies have suggested that BRAFi/MEKi and ERK1/2i resistance can arise through activation of a parallel signalling pathway leading to activation of ERK5, an unusual protein kinase that contains both a kinase domain and a transcriptional transactivation domain. (babraham.ac.uk)
  • Bae KM, Wang H, Jiang G, Chen MG, Lu L, Xiao L. Protein kinase C epsilon is overexpressed in primary human non-small cell lung cancers and functionally required for proliferation of non-small cell lung cancer cells in a p21/Cip1-dependent manner. (famri.org)
  • initiator caspases (caspases 2, 8, 9 and 10), which are able to hydrolyse and activate a second family of effector caspases (caspases 3, 6 and 7), which themselves are able to hydrolyse further cellular proteins to bring about programmed cell death. (guidetopharmacology.org)
  • Caspases are heterotetrameric, being made up of two pairs of subunits, generated by a single gene product, which is proteolysed to form the mature protein. (guidetopharmacology.org)
  • Bak BH3 peptides antagonize Bcl-xL function and induce apoptosis through cytochrome c-independent activation of caspases. (lookformedical.com)
  • The antigen corresponds to amino acid range 1-195 of the target protein. (thermofisher.com)
  • Mouse BID, His Tag immobilized on CM5 Chip can bind Human BCL2L1/Bcl-XL Protein, His Tag with an affinity constant of 33.06 nM as determined in SPR assay (Biacore T200). (kactusbio.com)
  • Unlike all other known death agonists of the Bcl-2 family, Mtd did not bind significantly to the survival-promoting proteins Bcl-2 or Bcl-XL. (deathbase.org)
  • Proteins which bind to DNA. (lookformedical.com)
  • The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases. (lookformedical.com)
  • Description: This is Competitive Enzyme-linked immunosorbent assay for detection of Human Myelin Basic Protein (MBP) in serum, plasma, tissue homogenates, cell lysates, cerebrospinal fluid, cell culture supernates and other biological fluids. (lscwarsaw.com)
  • Description: Enzyme-linked immunosorbent assay based on the Competitive Inhibition method for detection of Human Myelin Basic Protein (MBP) in samples from serum, plasma, tissue homogenates, cell lysates, cerebrospinal fluid, cell culture supernates and other biological fluids with no significant corss-reactivity with analogues from other species. (lscwarsaw.com)
  • Description: A sandwich quantitative ELISA assay kit for detection of Human Myelin Basic Protein (MBP) in samples from serum, plasma, tissue homogenates, cell lysates, cerebrospinal fluid, cell culture supernates or other biological fluids. (lscwarsaw.com)
  • Description: A sandwich quantitative ELISA assay kit for detection of Human Fatty Acid Binding Protein 6, Ileal (FABP6) in samples from serum, plasma, tissue homogenates or other biological fluids. (elisastrip.com)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Fatty Acid Binding Protein 6, Ileal (FABP6) in serum, plasma, tissue homogenates and other biological fluids. (elisastrip.com)
  • Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Fatty Acid Binding Protein 6, Ileal (FABP6) in samples from serum, plasma, tissue homogenates and other biological fluids with no significant corss-reactivity with analogues from other species. (elisastrip.com)
  • Description: A sandwich quantitative ELISA assay kit for detection of Human Protein Disulfide Isomerase (PDI) in samples from serum, plasma, tissue homogenates or other biological fluids. (knoblauchpublishing.com)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Protein Disulfide Isomerase (PDI) in serum, plasma, tissue homogenates and other biological fluids. (knoblauchpublishing.com)
  • Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Protein Disulfide Isomerase (PDI) in samples from serum, plasma, tissue homogenates and other biological fluids with no significant corss-reactivity with analogues from other species. (knoblauchpublishing.com)
  • Description: A sandwich quantitative ELISA assay kit for detection of Rat Angiopoietin Like Protein 4 (ANGPTL4) in samples from serum, plasma, tissue homogenates, cell lysates or other biological fluids. (ksiazkiwnauce.pl)
  • The Camp Assay For Dual Glp-1R And Gcrr Agonists reagent is RUO (Research Use Only) to test human serum or cell culture lab samples. (mytaq.net)
  • No antibody was detected against rat IgM or against non-immunoglobulin serum proteins. (srgroupchemical.com)
  • Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process. (lookformedical.com)
  • Proliferation is involved in structural development and renewal, while programmed cell death is necessary to eliminate defective cells and prevent uncontrolled growth. (encyclopedia.pub)
  • 3 Increased amounts of MYC protein are found in many types of human cancer because control mechanisms keeping MYC in check are inactivated during malignant transformation of cells. (ashpublications.org)
  • Targeted therapies exploit molecular vulnerabilities unique to cancer cells and typically alter cellular signaling pathways to inhibit tumorigenic growth and promote cell death. (biomedcentral.com)
  • Genes up-regulated in comparison of dendritic cells (DC) stimulated with LPS (TLR4 agonist) at 16 h versus DC cells stimulated with Pam3Csk4 (TLR1/2 agonist) at 16 h. (gsea-msigdb.org)
  • Three and 9) was noticed after URB597 administration within the coronary heart of each teams of hypertensive rats, whereas expression of the antiapoptotic protein (Bcl-2) elevated in SHR rats. (caspase-14.com)
  • The Bcl-2 homology 3 (BH3) domain is crucial for the death-inducing and dimerization properties of pro-apoptotic members of the Bcl-2 protein family, including Bak, Bax, and Bad. (lookformedical.com)
  • Glycosylation of classical death receptors fine-tunes cell death programs. (nature.com)
  • Description: G protein coupled receptors (GPCR) are one of the largest receptor classes targeted by drug discovery programs. (mytaq.net)
  • Glycans, either alone or complexed with glycan-binding proteins, can deliver intracellular signals or control extracellular processes that promote initiation, execution and resolution of cell death programs. (nature.com)
  • What is the precise role of intracellular and extracellular galectins in the control of cell death programs? (nature.com)
  • Overexpression of bcl-2 proteins, due to a translocation of the gene, is associated with follicular lymphoma. (bvsalud.org)
  • 1 MYC is a basic helix-loop-helix-leucine zipper transcription factor that dimerizes with the related protein MAX. (ashpublications.org)
  • The RUNX1: type pyrophosphate directly is change of the dendritic receptor, quantifying DNA transcription protein 1( CD35)( Kim et al. (erik-mill.de)
  • Antennapedia homeodomain protein is a homeobox protein involved in limb patterning in ARTHROPODS. (lookformedical.com)
  • Proteins encoded by homeobox genes (GENES, HOMEOBOX) that exhibit structural similarity to certain prokaryotic and eukaryotic DNA-binding proteins. (lookformedical.com)
  • The proteins encoded by homeobox genes are called HOMEODOMAIN PROTEINS. (lookformedical.com)
  • Endogenous lectins and glycans are critical signals in the resolution of cell death. (nature.com)
  • Pull-down assays using beads conjugated with a Cdc42/Rac interactive binding domain lead to see more an enrichment of endogenous alpha-synuclein oligomers. (proteasomesignaling.com)
  • The TP53 role anything, which is as heterodimerization of the RUNX1: loop repeat, was identified to directly eventually heat Phosphorylation of several proteins that are diseases of intellectual stages. (erik-mill.de)
  • Is there a hallmark 'glycosylation signature' that characterizes the initiation, execution and resolution of cell death programs in physiologic and pathologic settings? (nature.com)
  • Bid is important to cell death mediated by these proteases and thus is the sentinel to protease-mediated death signals. (kactusbio.com)
  • This triggers potent inside out signals inducing ADP release from dense bodies ( Shape change & agonist release ) as well as activating platelet major integrin α IIb β 3 . (biomedcentral.com)
  • Bid is a member of the BCL-2 family of cell death regulators. (thermofisher.com)
  • Bid contains only the BH3 domain, which is required for its interaction with the Bcl-2 family proteins and for its pro-death activity. (kactusbio.com)
  • We showed here that human Bok is the only member of the Bcl-2 family to have a leucine-rich sequence indicative of a nuclear export signal within its BH3 domain. (deathbase.org)
  • Sequence analysis revealed that Mtd is a member of the Bcl-2 family of proteins containing conserved BH1, BH2, BH3, and BH4 regions and a carboxyl-terminal hydrophobic domain. (deathbase.org)
  • DnaJ heat shock protein family (Hsp. (gsea-msigdb.org)
  • By two-dimensional gel electrophoretic analysis of synaptosomal fractions from transgenic mouse brains we detected additional isoforms of septin 6, a downstream target of Cdc42 effector proteins. (proteasomesignaling.com)
  • At that time, glycobiology, which is the study of carbohydrates and their recognition by motif-specific carbohydrate-binding proteins or lectins, lagged far behind the studies that defined the structural and cellular biology of cell death. (nature.com)
  • The structural diversity of sPLA 2 -BPs reveals sPLA 2 s as very promiscuous proteins, and we offer some structural explanations for this nature that makes these proteins evolutionarily highly advantageous. (ijbs.com)
  • Phosphorylation of eIF2α on Ser51 inhibits 5' cap-dependent mRNA translation, resulting in the global suppression of protein synthesis to facilitate adaptation to a variety of stresses linked to protein synthesis, including proteotoxic stress, viral replication, heme depletion and amino acid withdrawal [ 2 ]. (biomedcentral.com)
  • Molecular mechanisms that mediate cell death and proliferation exist in balance in functional physiological systems. (encyclopedia.pub)
  • Several other genetic backgrounds result in enlargement of the haltere significantly beyond the normal range of haploinsufficient phenotypes, suggesting genetic variation in cofactors that mediate homeotic protein function. (lookformedical.com)
  • sequence of domain gangliosides is identified by vertebrate TAR and removal remaining to the chemiosmotic transporters of the elongation( thought in Percipalle and Farrants 2006, McStay and Grummt 2008, Goodfellow and Zomerdijk 2012, Grummt and Langst 2013). (erik-mill.de)
  • Boosani CS, Mannam AP, Cosgrove D, Silva R, Hodivala-Dilke KM, Keshamouni VG, Sudhakar A. Regulation of COX-2 mediated signaling by alpha3 type IV noncollagenous domain in tumor angiogenesis. (famri.org)
  • Homeodomain proteins are involved in the control of gene expression during morphogenesis and development (GENE EXPRESSION REGULATION, DEVELOPMENTAL). (lookformedical.com)
  • Proteins found in the nucleus of a cell. (lookformedical.com)
  • Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus. (lookformedical.com)
  • Two decades later, pioneering studies suggested that lectin-like molecules constitutively expressed on the surface of macrophages can selectively recognize changes on glycans decorating the surface of apoptotic thymocytes, 4 , 5 although these studies likewise did not provide substantial insight into the mechanisms by which lectin-glycan interactions regulate cell death. (nature.com)
  • We reveal the potential to exploit interactions of sPLA 2 s with other proteins in medical terms, for the development of original diagnostic and therapeutic procedures. (ijbs.com)
  • CASP8 cleaves this encoded protein, and the COOH-terminal part translocates to mitochondria where it triggers cytochrome c release. (thermofisher.com)
  • The eIF2α kinases phosphorylate Ser51 of eIF2α which leads to suppression of global protein synthesis but selective enhancement of translation of some mRNAs, such as that encoding ATF4. (biomedcentral.com)
  • Herein, we review the role of glycans and glycan-binding proteins as essential components of the cell death machinery during physiologic and pathologic settings. (nature.com)
  • Two major mechanisms of apoptosis are an extrinsic, death-receptor mediated mechanism, and an intrinsic, mitochondria-mediated mechanism [ 4 ] . (encyclopedia.pub)
  • The ISR (Fig. 1 ) is a complex signaling pathway that regulates cellular responses to stress stimuli and enables either adaptation or the instigation of cell death mechanisms [ 2 ]. (biomedcentral.com)
  • We also found that Crm1 interacted with wild-type Bok but not with the mutated form. (deathbase.org)
  • Finally, the further GIX sPLA 2 s are found in venom of marine snails, and GXIA and GXIB sPLA 2 s are plant proteins. (ijbs.com)