Core Binding Factors
Core Binding Factor alpha Subunits
Core Binding Factor Alpha 1 Subunit
Core Binding Factor beta Subunit
Core Binding Factor Alpha 2 Subunit
Core Binding Factor Alpha 3 Subunit
Transcription Factor AP-2
Transcription Factors
Chromosomes, Human, Pair 16
DNA-Binding Proteins
Chromosome Inversion
Leukemia, Myeloid, Acute
Molecular Sequence Data
Oncogene Proteins, Fusion
Base Sequence
Chromosomes, Human, Pair 21
Protein Binding
Neoplasm Proteins
Binding Sites
Osteoblasts
Enhancer Elements, Genetic
Translocation, Genetic
Osteocalcin
Mutation
Transforming Growth Factor alpha
Promoter Regions, Genetic
Tumor Necrosis Factor-alpha
Proto-Oncogene Proteins
Amino Acid Sequence
Cell Differentiation
Transcription, Genetic
Leukemia, Myeloid
Pol1 Transcription Initiation Complex Proteins
Expression pattern, regulation, and biological role of runt domain transcription factor, run, in Caenorhabditis elegans. (1/202)
The Caenorhabditis elegans run gene encodes a Runt domain factor. Runx1, Runx2, and Runx3 are the three known mammalian homologs of run. Runx1, which plays an essential role in hematopoiesis, has been identified at the breakpoint of chromosome translocations that are responsible for human leukemia. Runx2 plays an essential role in osteogenesis, and inactivation of one allele of Runx2 is responsible for the human disease cleidocranial dysplasia. To understand the role of run in C. elegans, we used transgenic run::GFP reporter constructs and a double-stranded RNA-mediated interference method. The expression of run was detected as early as the bean stage exclusively in the nuclei of seam hypodermal cells and lasted until the L3 stage. At the larval stage, expression of run was additionally detected in intestinal cells. The regulatory elements responsible for the postembryonic hypodermal seam cells and intestinal cells were separately located within a 7.2-kb-long intron region. This is the first report demonstrating that an intron region is essential for stage-specific and cell type-specific expression of a C. elegans gene. RNA interference analysis targeting the run gene resulted in an early larva-lethal phenotype, with apparent malformation of the hypodermis and intestine. These results suggest that run is involved in the development of a functional hypodermis and gut in C. elegans. The highly conserved role of the Runt domain transcription factor in gut development during evolution from nematodes to mammals is discussed. (+info)The common retroviral insertion locus Dsi1 maps 30 kilobases upstream of the P1 promoter of the murine Runx3/Cbfa3/Aml2 gene. (2/202)
The Dsi1 locus was identified as a common integration site for Moloney murine leukemia virus (MLV) in rat thymic lymphomas, but previous efforts to identify a gene affected by these insertions were unsuccessful. We considered the Runx3 gene a potential candidate on the basis of genetic mapping which showed that Dsi1 and Runx3 are closely linked on mouse chromosome 4 and the precedent of the related Runx2 gene, which emerged recently as a Myc-collaborating gene activated by retroviral insertion in thymic lymphomas of CD2-MYC mice. We now report the physical mapping of the Dsi1 locus to a site 30 kb upstream of the distal (P1) promoter of the murine Runx3 gene. Comparison with the syntenic region of human chromosome 1 shows that the next gene is over 250 kb 5' to Runx3, suggesting that Runx3 may be the primary target of retroviral insertions at Dsi1. Screening of CD2-MYC lymphomas for rearrangements at Dsi1 revealed a tumor cell line harboring an MLV provirus at this locus, in the orientation opposite that of Runx3. Proviral insertion was associated with very high levels of expression of Runx3, with a preponderance of transcripts arising at the P1 promoter. These results confirm that Runx3 is a target of retroviral insertions at Dsi1 and indicate that Runx3 can act as an alternative to Runx2 as a Myc-collaborating gene in thymic lymphoma. (+info)Causal relationship between the loss of RUNX3 expression and gastric cancer. (3/202)
Runx3/Pebp2alphaC null mouse gastric mucosa exhibits hyperplasias due to stimulated proliferation and suppressed apoptosis in epithelial cells, and the cells are resistant to growth-inhibitory and apoptosis-inducing action of TGF-beta, indicating that Runx3 is a major growth regulator of gastric epithelial cells. Between 45% and 60% of human gastric cancer cells do not significantly express RUNX3 due to hemizygous deletion and hypermethylation of the RUNX3 promoter region. Tumorigenicity of human gastric cancer cell lines in nude mice was inversely related to their level of RUNX3 expression, and a mutation (R122C) occurring within the conserved Runt domain abolished the tumor-suppressive effect of RUNX3, suggesting that a lack of RUNX3 function is causally related to the genesis and progression of human gastric cancer. (+info)Expression of transcription factor AML-2 (RUNX3, CBF(alpha)-3) is induced by Epstein-Barr virus EBNA-2 and correlates with the B-cell activation phenotype. (4/202)
To identify cell proteins regulated by the Epstein-Barr virus (EBV) transcription factor EBNA-2, we analyzed a cell line with conditional EBNA-2 activity by using microarray expression profiling. This led to the identification of two novel target genes induced by EBNA-2. The first of these, interleukin-16, is an immunomodulatory cytokine involved in the regulation of CD4 T cells. The second, AML-2, is a member of the Runt domain family of transcription factors. Quiescent B cells initially expressed AML-1 but, 48 h after virus infection, the levels of AML-1 decreased dramatically, whereas the amount of AML-2 protein increased. Analysis of a panel of B-cell lines indicated that AML-2 expression is normally predominant in EBV latency III, whereas AML-1 is associated with EBV latency I or EBV-negative cells. The AML genes are the first example of cell transcription factors whose expression correlates with the latency I/III phenotype. (+info)RUNX: a trilogy of cancer genes. (5/202)
The RUNX family of transcription factors plays pivotal roles during normal development and in neoplasias. Recent data involve RUNX3 as an important tumor suppressor in gastric cancers and pose interesting questions about how perturbed levels and interspecific competition among RUNX family members may contribute to tumorigenesis. (+info)The Runx3 transcription factor regulates development and survival of TrkC dorsal root ganglia neurons. (6/202)
The RUNX transcription factors are important regulators of linage-specific gene expression in major developmental pathways. Recently, we demonstrated that Runx3 is highly expressed in developing cranial and dorsal root ganglia (DRGs). Here we report that within the DRGs, Runx3 is specifically expressed in a subset of neurons, the tyrosine kinase receptor C (TrkC) proprioceptive neurons. We show that Runx3-deficient mice develop severe limb ataxia due to disruption of monosynaptic connectivity between intra spinal afferents and motoneurons. We demonstrate that the underlying cause of the defect is a loss of DRG proprioceptive neurons, reflected by a decreased number of TrkC-, parvalbumin- and beta-galactosidase-positive cells. Thus, Runx3 is a neurogenic TrkC neuron-specific transcription factor. In its absence, TrkC neurons in the DRG do not survive long enough to extend their axons toward target cells, resulting in lack of connectivity and ataxia. The data provide new genetic insights into the neurogenesis of DRGs and may help elucidate the molecular mechanisms underlying somatosensory-related ataxia in humans. (+info)Pathways in blood and vessel development revealed through zebrafish genetics. (7/202)
Studies in zebrafish have potential to contribute to understanding of the vertebrate hematopoietic and vasculogenic systems. Our research has examined the roles of several molecules in pathways that lead to the development of blood and vessels in zebrafish, and has provided insights into the regulation of these processes. Gdf6a/radar, a member of the bone morphogenetic protein (BMP) family, is expressed in the zebrafish hypochord and primitive gut endoderm; structures that flank the developing dorsal aorta and posterior cardinal vein. This pattern of expression positions Gdf6a/radar as a candidate regulator of vasculogenesis. Support for such a role has come from experiments where Gdf6a/radar function was depleted with antisense morpholino oligonucleotides. This resulted in vascular leakiness, suggesting that Gdf6a/radar is involved in maintenance of vascular integrity. The transcription factor Runx1 is known to play a critical role in mammalian definitive hematopoiesis. When Runx1 expression domains and function were analyzed in zebrafish, the importance of this gene in definitive hematopoiesis was confirmed. However there was also evidence for a wider role, including involvement in vascular development and neuropoiesis. This work has laid the foundation for an ethylnitrosourea (ENU) mutagenesis screen based on runx1 whole-mount in situ hybridzation, that aims to identify genes operative in the runx1 pathway. An additional member of the Runx family, Runx3, is also involved in developmental hematopoiesis, with a function distinct from that of Runx1. We hypothesize that Runx1 and Runx3 form a continuum of transcriptional control within the hematopoietic system. An added attraction of zebrafish is that models of human disease can be generated, and we have shown that this system has potential for the study of Runx1-mediated leukemogenesis. (+info)Inhibition of growth of mouse gastric cancer cells by Runx3, a novel tumor suppressor. (8/202)
We reported recently that the silencing of RUNX3 is causally related to gastric cancer in humans. Here we report that in three of four cell lines derived from N-methyl-N-nitrosourea-induced mouse glandular stomach carcinomas, Runx3 is silenced due to hypermethylation of CpG islands in the promoter region, as we also observed for human gastric cancer cells. Although two of the sites we tested in the promoter of the fourth line were not methylated, in all four cases the silencing of Runx3 could be reversed by treatment of the cells with 5'-azacytidine and trichostatin A. Interestingly, the exogenous expression of RUNX3 in cell lines that do not express the endogenous gene caused an inhibition of growth in soft agar, suggesting that anchorage-independent growth could be used as an assay of RUNX3 activity in vitro. These observations suggest that the mouse system described here may be useful as a model for the study of human gastric carcinogenesis. (+info)Core binding factors (CBFs) are a group of proteins that play critical roles in the development and differentiation of hematopoietic cells, which are the cells responsible for the formation of blood and immune systems. The term "core binding factor" refers to the ability of these proteins to bind to specific DNA sequences, known as core binding sites, and regulate gene transcription.
The two main CBFs are:
1. Core Binding Factor Alpha (CBF-α): Also known as RUNX1 or AML1, this protein forms a complex with Core Binding Factor Beta (CBF-β) to regulate the expression of genes involved in hematopoiesis. Mutations in CBF-α have been associated with various types of leukemia and myelodysplastic syndromes.
2. Core Binding Factor Beta (CBF-β): Also known as PEBP2B, this protein partners with CBF-α to form the active transcription factor complex. CBF-β enhances the DNA binding affinity and stability of the CBF-α/CBF-β heterodimer.
In certain types of leukemia, chromosomal abnormalities can lead to the formation of fusion proteins involving CBF-α or CBF-β. These fusion proteins disrupt normal hematopoiesis and contribute to the development of cancer. Examples include the t(8;21) translocation that creates the AML1/ETO fusion protein in acute myeloid leukemia (AML) and the inv(16) inversion that forms the CBFB-MYH11 fusion protein in AML.
Core Binding Factor (CBF) is a transcription factor that plays a crucial role in the development and differentiation of various tissues, including hematopoietic cells. It is composed of two subunits: alpha (CBFA or AML1) and beta (CBFB or PEBP2b).
The CBFA subunit, also known as RUNX1, is a transcription factor that binds to DNA and regulates the expression of target genes involved in hematopoiesis, neurogenesis, and other developmental processes. It contains a highly conserved DNA-binding domain called the runt homology domain (RHD) that recognizes specific DNA sequences.
Mutations in CBFA have been associated with various hematological disorders, including acute myeloid leukemia (AML), myelodysplastic syndrome (MDS), and familial platelet disorder with predisposition to AML (FDPA). These mutations can lead to altered gene expression, impaired differentiation, and increased proliferation of hematopoietic cells, contributing to the development of these diseases.
Core Binding Factor Alpha 1 Subunit, also known as CBF-A1 or RUNX1, is a protein that plays a crucial role in hematopoiesis, which is the process of blood cell development. It is a member of the core binding factor (CBF) complex, which regulates gene transcription and is essential for the differentiation and maturation of hematopoietic stem cells into mature blood cells.
The CBF complex consists of three subunits: CBF-A, CBF-B, and a histone deacetylase (HDAC). The CBF-A subunit can have several isoforms, including CBF-A1, which is encoded by the RUNX1 gene. Mutations in the RUNX1 gene have been associated with various hematological disorders, such as acute myeloid leukemia (AML), familial platelet disorder with propensity to develop AML, and thrombocytopenia with absent radii syndrome.
CBF-A1/RUNX1 functions as a transcription factor that binds to DNA at specific sequences called core binding factors, thereby regulating the expression of target genes involved in hematopoiesis. Proper regulation of these genes is essential for normal blood cell development and homeostasis.
Core Binding Factor-beta (CBF-β) is a subunit of the Core Binding Factor (CBF), which is a heterodimeric transcription factor composed of a DNA-binding alpha subunit and a non-DNA binding beta subunit. The CBF plays a crucial role in hematopoiesis, the process of blood cell development, by regulating the expression of various genes involved in this process.
The CBF-β subunit is a 36 kDa protein that is encoded by the CBFB gene in humans. It does not bind to DNA directly but instead forms a complex with the DNA-binding alpha subunit, which is either RUNX1 (also known as AML1), RUNX2, or RUNX3. The CBF-β subunit stabilizes the interaction between the alpha subunit and DNA, enhances its DNA-binding affinity, and increases the transcriptional activity of the complex.
Mutations in the CBFB gene have been associated with several hematological disorders, including acute myeloid leukemia (AML), myelodysplastic syndromes (MDS), and familial platelet disorder with predisposition to AML (FPD/AML). These mutations can lead to aberrant transcriptional regulation of hematopoietic genes, resulting in the development of these disorders.
Core Binding Factor Alpha 2 Subunit, also known as CBF-A2 or CEBP-α, is a protein that forms a complex with other proteins to act as a transcription factor. Transcription factors are proteins that help regulate the expression of genes by binding to specific DNA sequences and controlling the rate of transcription of genetic information from DNA to RNA.
CBF-A2 is a member of the CCAAT/enhancer-binding protein (C/EBP) family of transcription factors, which are important in regulating various biological processes such as cell growth, development, and inflammation. CBF-A2 forms a heterodimer with Core Binding Factor Beta (CBF-β) to form the active transcription factor complex known as the core binding factor (CBF).
The CBF complex binds to the CCAAT box, a specific DNA sequence found in the promoter regions of many genes. By binding to this sequence, the CBF complex can either activate or repress the transcription of target genes, depending on the context and the presence of other regulatory factors.
Mutations in the gene encoding CBF-A2 have been associated with several human diseases, including acute myeloid leukemia (AML) and multiple myeloma. In AML, mutations in the CBF-A2 gene can lead to the formation of abnormal CBF complexes that disrupt normal gene expression patterns and contribute to the development of leukemia.
Core Binding Factor Alpha 3 Subunit (also known as CBFA3 or AML1) is a protein that forms part of a complex responsible for the regulation of gene transcription, particularly those involved in hematopoiesis (the formation of blood cells). It is a member of the runt-domain family of transcription factors and plays a critical role in normal blood cell development.
Mutations in the CBFA3 gene have been associated with certain types of leukemia, such as acute myeloid leukemia (AML) and acute lymphoblastic leukemia (ALL). These mutations can lead to abnormal blood cell development and cancer.
Transcription Factor AP-2 is a specific protein involved in the process of gene transcription. It belongs to a family of transcription factors known as Activating Enhancer-Binding Proteins (AP-2). These proteins regulate gene expression by binding to specific DNA sequences called enhancers, which are located near the genes they control.
AP-2 is composed of four subunits that form a homo- or heterodimer, which then binds to the consensus sequence 5'-GCCNNNGGC-3'. This sequence is typically found in the promoter regions of target genes. Once bound, AP-2 can either activate or repress gene transcription, depending on the context and the presence of cofactors.
AP-2 plays crucial roles during embryonic development, particularly in the formation of the nervous system, limbs, and face. It is also involved in cell cycle regulation, differentiation, and apoptosis (programmed cell death). Dysregulation of AP-2 has been implicated in several diseases, including various types of cancer.
Smooth muscle myosin is a type of motor protein that is responsible for the contraction and relaxation of smooth muscles, which are found in various organs such as the bladder, blood vessels, and digestive tract. Smooth muscle myosin is composed of two heavy chains and four light chains, forming a hexameric structure. The heavy chains have an N-terminal head domain that contains the ATPase activity and a C-terminal tail domain that mediates filament assembly.
The smooth muscle myosin molecule has several unique features compared to other types of myosins, such as skeletal or cardiac myosin. For example, smooth muscle myosin has a longer lever arm, which allows for greater force generation during contraction. Additionally, the regulatory mechanism of smooth muscle myosin is different from that of skeletal or cardiac myosin. In smooth muscles, the contractile activity is regulated by phosphorylation of the light chains, which is mediated by a specific kinase called myosin light chain kinase (MLCK).
Overall, the proper regulation and function of smooth muscle myosin are critical for maintaining normal physiological functions in various organs. Dysregulation or mutations in smooth muscle myosin can lead to several diseases, such as hypertension, atherosclerosis, and gastrointestinal motility disorders.
Transcription factors are proteins that play a crucial role in regulating gene expression by controlling the transcription of DNA to messenger RNA (mRNA). They function by binding to specific DNA sequences, known as response elements, located in the promoter region or enhancer regions of target genes. This binding can either activate or repress the initiation of transcription, depending on the properties and interactions of the particular transcription factor. Transcription factors often act as part of a complex network of regulatory proteins that determine the precise spatiotemporal patterns of gene expression during development, differentiation, and homeostasis in an organism.
Human chromosome pair 16 consists of two rod-shaped structures present in the nucleus of each cell in the human body. Each chromosome is made up of DNA tightly coiled around histone proteins, forming a complex structure called a chromatin.
Chromosomes come in pairs, with one chromosome inherited from each parent. Chromosome pair 16 contains two homologous chromosomes, which are similar in size, shape, and genetic content but may have slight variations due to differences in the DNA sequences inherited from each parent.
Chromosome pair 16 is one of the 22 autosomal pairs, meaning it contains non-sex chromosomes that are present in both males and females. Chromosome 16 is a medium-sized chromosome, and it contains around 2,800 genes that provide instructions for making proteins and regulating various cellular processes.
Abnormalities in chromosome pair 16 can lead to genetic disorders such as chronic myeloid leukemia, some forms of mental retardation, and other developmental abnormalities.
DNA-binding proteins are a type of protein that have the ability to bind to DNA (deoxyribonucleic acid), the genetic material of organisms. These proteins play crucial roles in various biological processes, such as regulation of gene expression, DNA replication, repair and recombination.
The binding of DNA-binding proteins to specific DNA sequences is mediated by non-covalent interactions, including electrostatic, hydrogen bonding, and van der Waals forces. The specificity of binding is determined by the recognition of particular nucleotide sequences or structural features of the DNA molecule.
DNA-binding proteins can be classified into several categories based on their structure and function, such as transcription factors, histones, and restriction enzymes. Transcription factors are a major class of DNA-binding proteins that regulate gene expression by binding to specific DNA sequences in the promoter region of genes and recruiting other proteins to modulate transcription. Histones are DNA-binding proteins that package DNA into nucleosomes, the basic unit of chromatin structure. Restriction enzymes are DNA-binding proteins that recognize and cleave specific DNA sequences, and are widely used in molecular biology research and biotechnology applications.
A chromosome inversion is a genetic rearrangement where a segment of a chromosome has been reversed end to end, so that its order of genes is opposite to the original. This means that the gene sequence on the segment of the chromosome has been inverted.
In an inversion, the chromosome breaks in two places, and the segment between the breaks rotates 180 degrees before reattaching. This results in a portion of the chromosome being inverted, or turned upside down, relative to the rest of the chromosome.
Chromosome inversions can be either paracentric or pericentric. Paracentric inversions involve a segment that does not include the centromere (the central constriction point of the chromosome), while pericentric inversions involve a segment that includes the centromere.
Inversions can have various effects on an individual's phenotype, depending on whether the inversion involves genes and if so, how those genes are affected by the inversion. In some cases, inversions may have no noticeable effect, while in others they may cause genetic disorders or predispose an individual to certain health conditions.
Acute myeloid leukemia (AML) is a type of cancer that originates in the bone marrow, the soft inner part of certain bones where new blood cells are made. In AML, the immature cells, called blasts, in the bone marrow fail to mature into normal blood cells. Instead, these blasts accumulate and interfere with the production of normal blood cells, leading to a shortage of red blood cells (anemia), platelets (thrombocytopenia), and normal white blood cells (leukopenia).
AML is called "acute" because it can progress quickly and become severe within days or weeks without treatment. It is a type of myeloid leukemia, which means that it affects the myeloid cells in the bone marrow. Myeloid cells are a type of white blood cell that includes monocytes and granulocytes, which help fight infection and defend the body against foreign invaders.
In AML, the blasts can build up in the bone marrow and spread to other parts of the body, including the blood, lymph nodes, liver, spleen, and brain. This can cause a variety of symptoms, such as fatigue, fever, frequent infections, easy bruising or bleeding, and weight loss.
AML is typically treated with a combination of chemotherapy, radiation therapy, and/or stem cell transplantation. The specific treatment plan will depend on several factors, including the patient's age, overall health, and the type and stage of the leukemia.
Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.
An oncogene protein fusion is a result of a genetic alteration in which parts of two different genes combine to create a hybrid gene that can contribute to the development of cancer. This fusion can lead to the production of an abnormal protein that promotes uncontrolled cell growth and division, ultimately resulting in a malignant tumor. Oncogene protein fusions are often caused by chromosomal rearrangements such as translocations, inversions, or deletions and are commonly found in various types of cancer, including leukemia and sarcoma. These genetic alterations can serve as potential targets for cancer diagnosis and therapy.
A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.
Human chromosome pair 21 consists of two rod-shaped structures present in the nucleus of each cell in the human body. Each member of the pair is a single chromosome, and they are identical to each other. Chromosomes are made up of DNA, which contains genetic information that determines many of an individual's traits and characteristics.
Chromosome pair 21 is one of the 23 pairs of human autosomal chromosomes, meaning they are not sex chromosomes (X or Y). Chromosome pair 21 is the smallest of the human chromosomes, and it contains approximately 48 million base pairs of DNA. It contains around 200-300 genes that provide instructions for making proteins and regulating various cellular processes.
Down syndrome, a genetic disorder characterized by intellectual disability, developmental delays, distinct facial features, and sometimes heart defects, is caused by an extra copy of chromosome pair 21 or a part of it. This additional genetic material can lead to abnormalities in brain development and function, resulting in the characteristic symptoms of Down syndrome.
Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.
In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.
Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.
A neoplasm is a tumor or growth that is formed by an abnormal and excessive proliferation of cells, which can be benign or malignant. Neoplasm proteins are therefore any proteins that are expressed or produced in these neoplastic cells. These proteins can play various roles in the development, progression, and maintenance of neoplasms.
Some neoplasm proteins may contribute to the uncontrolled cell growth and division seen in cancer, such as oncogenic proteins that promote cell cycle progression or inhibit apoptosis (programmed cell death). Others may help the neoplastic cells evade the immune system, allowing them to proliferate undetected. Still others may be involved in angiogenesis, the formation of new blood vessels that supply the tumor with nutrients and oxygen.
Neoplasm proteins can also serve as biomarkers for cancer diagnosis, prognosis, or treatment response. For example, the presence or level of certain neoplasm proteins in biological samples such as blood or tissue may indicate the presence of a specific type of cancer, help predict the likelihood of cancer recurrence, or suggest whether a particular therapy will be effective.
Overall, understanding the roles and behaviors of neoplasm proteins can provide valuable insights into the biology of cancer and inform the development of new diagnostic and therapeutic strategies.
In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.
The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.
In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.
Osteoblasts are specialized bone-forming cells that are derived from mesenchymal stem cells. They play a crucial role in the process of bone formation and remodeling. Osteoblasts synthesize, secrete, and mineralize the organic matrix of bones, which is mainly composed of type I collagen.
These cells have receptors for various hormones and growth factors that regulate their activity, such as parathyroid hormone, vitamin D, and transforming growth factor-beta. When osteoblasts are not actively producing bone matrix, they can become trapped within the matrix they produce, where they differentiate into osteocytes, which are mature bone cells that play a role in maintaining bone structure and responding to mechanical stress.
Abnormalities in osteoblast function can lead to various bone diseases, such as osteoporosis, osteogenesis imperfecta, and Paget's disease of bone.
Genetic enhancer elements are DNA sequences that increase the transcription of specific genes. They work by binding to regulatory proteins called transcription factors, which in turn recruit RNA polymerase II, the enzyme responsible for transcribing DNA into messenger RNA (mRNA). This results in the activation of gene transcription and increased production of the protein encoded by that gene.
Enhancer elements can be located upstream, downstream, or even within introns of the genes they regulate, and they can act over long distances along the DNA molecule. They are an important mechanism for controlling gene expression in a tissue-specific and developmental stage-specific manner, allowing for the precise regulation of gene activity during embryonic development and throughout adult life.
It's worth noting that genetic enhancer elements are often referred to simply as "enhancers," and they are distinct from other types of regulatory DNA sequences such as promoters, silencers, and insulators.
Translocation, genetic, refers to a type of chromosomal abnormality in which a segment of a chromosome is transferred from one chromosome to another, resulting in an altered genome. This can occur between two non-homologous chromosomes (non-reciprocal translocation) or between two homologous chromosomes (reciprocal translocation). Genetic translocations can lead to various clinical consequences, depending on the genes involved and the location of the translocation. Some translocations may result in no apparent effects, while others can cause developmental abnormalities, cancer, or other genetic disorders. In some cases, translocations can also increase the risk of having offspring with genetic conditions.
Osteogenesis is the process of bone formation or development. It involves the differentiation and maturation of osteoblasts, which are bone-forming cells that synthesize and deposit the organic matrix of bone tissue, composed mainly of type I collagen. This organic matrix later mineralizes to form the inorganic crystalline component of bone, primarily hydroxyapatite.
There are two primary types of osteogenesis: intramembranous and endochondral. Intramembranous osteogenesis occurs directly within connective tissue, where mesenchymal stem cells differentiate into osteoblasts and form bone tissue without an intervening cartilage template. This process is responsible for the formation of flat bones like the skull and clavicles.
Endochondral osteogenesis, on the other hand, involves the initial development of a cartilaginous model or template, which is later replaced by bone tissue. This process forms long bones, such as those in the limbs, and occurs through several stages involving chondrocyte proliferation, hypertrophy, and calcification, followed by invasion of blood vessels and osteoblasts to replace the cartilage with bone tissue.
Abnormalities in osteogenesis can lead to various skeletal disorders and diseases, such as osteogenesis imperfecta (brittle bone disease), achondroplasia (a form of dwarfism), and cleidocranial dysplasia (a disorder affecting skull and collarbone development).
Osteocalcin is a protein that is produced by osteoblasts, which are the cells responsible for bone formation. It is one of the most abundant non-collagenous proteins found in bones and plays a crucial role in the regulation of bone metabolism. Osteocalcin contains a high affinity for calcium ions, making it essential for the mineralization of the bone matrix.
Once synthesized, osteocalcin is secreted into the extracellular matrix, where it binds to hydroxyapatite crystals, helping to regulate their growth and contributing to the overall strength and integrity of the bones. Osteocalcin also has been found to play a role in other physiological processes outside of bone metabolism, such as modulating insulin sensitivity, energy metabolism, and male fertility.
In summary, osteocalcin is a protein produced by osteoblasts that plays a critical role in bone formation, mineralization, and turnover, and has been implicated in various other physiological processes.
A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.
Transforming Growth Factor-alpha (TGF-α) is a type of growth factor, specifically a peptide growth factor, that plays a role in cell growth, proliferation, and differentiation. It belongs to the epidermal growth factor (EGF) family of growth factors. TGF-α binds to the EGF receptor (EGFR) on the surface of cells and activates intracellular signaling pathways that promote cellular growth and division.
TGF-α is involved in various biological processes, including embryonic development, wound healing, and tissue repair. However, abnormal regulation of TGF-α has been implicated in several diseases, such as cancer. Overexpression or hyperactivation of TGF-α can contribute to uncontrolled cell growth and tumor progression by stimulating the proliferation of cancer cells and inhibiting their differentiation and apoptosis (programmed cell death).
TGF-α is produced by various cell types, including epithelial cells, fibroblasts, and immune cells. It can be secreted in a membrane-bound form (pro-TGF-α) or as a soluble protein after proteolytic cleavage.
Promoter regions in genetics refer to specific DNA sequences located near the transcription start site of a gene. They serve as binding sites for RNA polymerase and various transcription factors that regulate the initiation of gene transcription. These regulatory elements help control the rate of transcription and, therefore, the level of gene expression. Promoter regions can be composed of different types of sequences, such as the TATA box and CAAT box, and their organization and composition can vary between different genes and species.
Tumor Necrosis Factor-alpha (TNF-α) is a cytokine, a type of small signaling protein involved in immune response and inflammation. It is primarily produced by activated macrophages, although other cell types such as T-cells, natural killer cells, and mast cells can also produce it.
TNF-α plays a crucial role in the body's defense against infection and tissue injury by mediating inflammatory responses, activating immune cells, and inducing apoptosis (programmed cell death) in certain types of cells. It does this by binding to its receptors, TNFR1 and TNFR2, which are found on the surface of many cell types.
In addition to its role in the immune response, TNF-α has been implicated in the pathogenesis of several diseases, including autoimmune disorders such as rheumatoid arthritis, inflammatory bowel disease, and psoriasis, as well as cancer, where it can promote tumor growth and metastasis.
Therapeutic agents that target TNF-α, such as infliximab, adalimumab, and etanercept, have been developed to treat these conditions. However, these drugs can also increase the risk of infections and other side effects, so their use must be carefully monitored.
Proto-oncogene proteins are normal cellular proteins that play crucial roles in various cellular processes, such as signal transduction, cell cycle regulation, and apoptosis (programmed cell death). They are involved in the regulation of cell growth, differentiation, and survival under physiological conditions.
When proto-oncogene proteins undergo mutations or aberrations in their expression levels, they can transform into oncogenic forms, leading to uncontrolled cell growth and division. These altered proteins are then referred to as oncogene products or oncoproteins. Oncogenic mutations can occur due to various factors, including genetic predisposition, environmental exposures, and aging.
Examples of proto-oncogene proteins include:
1. Ras proteins: Involved in signal transduction pathways that regulate cell growth and differentiation. Activating mutations in Ras genes are found in various human cancers.
2. Myc proteins: Regulate gene expression related to cell cycle progression, apoptosis, and metabolism. Overexpression of Myc proteins is associated with several types of cancer.
3. EGFR (Epidermal Growth Factor Receptor): A transmembrane receptor tyrosine kinase that regulates cell proliferation, survival, and differentiation. Mutations or overexpression of EGFR are linked to various malignancies, such as lung cancer and glioblastoma.
4. Src family kinases: Intracellular tyrosine kinases that regulate signal transduction pathways involved in cell proliferation, survival, and migration. Dysregulation of Src family kinases is implicated in several types of cancer.
5. Abl kinases: Cytoplasmic tyrosine kinases that regulate various cellular processes, including cell growth, differentiation, and stress responses. Aberrant activation of Abl kinases, as seen in chronic myelogenous leukemia (CML), leads to uncontrolled cell proliferation.
Understanding the roles of proto-oncogene proteins and their dysregulation in cancer development is essential for developing targeted cancer therapies that aim to inhibit or modulate these aberrant signaling pathways.
A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.
An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.
Cell differentiation is the process by which a less specialized cell, or stem cell, becomes a more specialized cell type with specific functions and structures. This process involves changes in gene expression, which are regulated by various intracellular signaling pathways and transcription factors. Differentiation results in the development of distinct cell types that make up tissues and organs in multicellular organisms. It is a crucial aspect of embryonic development, tissue repair, and maintenance of homeostasis in the body.
Genetic transcription is the process by which the information in a strand of DNA is used to create a complementary RNA molecule. This process is the first step in gene expression, where the genetic code in DNA is converted into a form that can be used to produce proteins or functional RNAs.
During transcription, an enzyme called RNA polymerase binds to the DNA template strand and reads the sequence of nucleotide bases. As it moves along the template, it adds complementary RNA nucleotides to the growing RNA chain, creating a single-stranded RNA molecule that is complementary to the DNA template strand. Once transcription is complete, the RNA molecule may undergo further processing before it can be translated into protein or perform its functional role in the cell.
Transcription can be either "constitutive" or "regulated." Constitutive transcription occurs at a relatively constant rate and produces essential proteins that are required for basic cellular functions. Regulated transcription, on the other hand, is subject to control by various intracellular and extracellular signals, allowing cells to respond to changing environmental conditions or developmental cues.
Leukemia, myeloid is a type of cancer that originates in the bone marrow, where blood cells are produced. Myeloid leukemia affects the myeloid cells, which include red blood cells, platelets, and most types of white blood cells. In this condition, the bone marrow produces abnormal myeloid cells that do not mature properly and accumulate in the bone marrow and blood. These abnormal cells hinder the production of normal blood cells, leading to various symptoms such as anemia, fatigue, increased risk of infections, and easy bruising or bleeding.
There are several types of myeloid leukemias, including acute myeloid leukemia (AML) and chronic myeloid leukemia (CML). AML progresses rapidly and requires immediate treatment, while CML tends to progress more slowly. The exact causes of myeloid leukemia are not fully understood, but risk factors include exposure to radiation or certain chemicals, smoking, genetic disorders, and a history of chemotherapy or other cancer treatments.
POL1 (Polymerase 1) Transcription Initiation Complex Proteins are a set of proteins that come together to form the initiation complex for the transcription of ribosomal RNA (rRNA) genes in eukaryotic cells. The POL1 complex includes RNA polymerase I, select transcription factors, and other regulatory proteins. This complex is responsible for the transcription of rRNA genes located within the nucleolus, a specialized region within the cell nucleus. Proper assembly and functioning of this initiation complex are crucial for the production of ribosomes, which play a critical role in protein synthesis.
Alkaline phosphatase (ALP) is an enzyme found in various body tissues, including the liver, bile ducts, digestive system, bones, and kidneys. It plays a role in breaking down proteins and minerals, such as phosphate, in the body.
The medical definition of alkaline phosphatase refers to its function as a hydrolase enzyme that removes phosphate groups from molecules at an alkaline pH level. In clinical settings, ALP is often measured through blood tests as a biomarker for various health conditions.
Elevated levels of ALP in the blood may indicate liver or bone diseases, such as hepatitis, cirrhosis, bone fractures, or cancer. Therefore, physicians may order an alkaline phosphatase test to help diagnose and monitor these conditions. However, it is essential to interpret ALP results in conjunction with other diagnostic tests and clinical findings for accurate diagnosis and treatment.
CBFA2T3
CBFA2T2
Runt domain
TAF11
Sigma factor
Bacterial transcription
CAAT box
RUNX1
STAT4
CBFB
TBP-associated factor
GTF2A1L
TAF9
SEC61B
TAF15
EGLN1
Sec61 alpha 1
RUNX2
POLR2J
PSMC5
PSMD10
CUL4A
EIF-W2 protein domain
RNA polymerase
Promoter (genetics)
Ars operon
Cyclin D
PPP2R1A
General transcription factor
POLD1
ATP-binding cassette transporter
CBFA2T3 - Wikipedia
Neural EGFL-Like 1 Regulates Cartilage Maturation through Runt-Related Transcription Factor 3-Mediated Indian Hedgehog Signaling
RUNX1 gene: MedlinePlus Genetics
David Pieter Hoytema van Konijnenburg, M.D., Ph.D. | Harvard Catalyst Profiles | Harvard Catalyst
PMKB
Pesquisa | Prevenção e Controle de Câncer
1hxw - Proteopedia, life in 3D
3cyx - Proteopedia, life in 3D
Role of pyrophosphate in vascular calcification in chronic kidney disease | Nefrología
SZGR2
ClinGen Myeloid Malignancy Variant Curation Expert Panel recommendations for germline RUNX1 variants. | Profiles RNS
Disruption of MAPK1 expression in the ERK signalling pathway and the RUNX1‑RUNX1T1 fusion gene attenuate the differentiation...
SMART: PH domain annotation
SMART: Schnipsel domain PH
PlantTFDB - Plant Transcription Factor Database @ CBI, PKU
Pregnancy Diagnosis: Overview, History and Physical Examination, Laboratory Evaluation
Richard H. Ebright - Publications
Publications from CCI Users and Staff | University of Gothenburg
Fact file for STAT3 deficiency
"sequence id","alias","species","description",...
Anti-cancer agents and reactive oxygen species modulators that target cancer cell metabolism
SCOP 1.65: Superfamily a.4.12: TrpR-like
Exploring key molecular signatures of immune responses and pathways associated with tuberculosis in comorbid diabetes mellitus:...
Frontiers | Deciphering Risperidone-Induced Lipogenesis by Network Pharmacology and Molecular Validation
PeptiQuant? Plus Custom Proteomics Kits - MRM Proteomics
Human Metabolome Database: Showing Protein Nuclear factor NF-kappa-B p105 subunit (HMDBP02145)
Recombinant Proteins | CU Experts | CU Boulder
Protein36
- translocated to, 3) is a protein that in humans is encoded by the CBFA2T3 gene. (wikipedia.org)
- Two transcript variants encoding different isoforms have been found for this gene, and a brefeldin A-sensitive association of RII-alpha protein with one of the isoforms has been demonstrated in the Golgi apparatus. (wikipedia.org)
- A heterodimer of this protein and a beta subunit forms a complex that binds to the core DNA sequence 5'-PYGPYGGT-3' found in a number of enhancers and promoters, and can either activate or suppress transcription. (nih.gov)
- The RUNX2 protein is a transcription factor, which means it attaches (binds) to specific regions of DNA and helps control the activity of particular genes. (medlineplus.gov)
- [ 5 ] At least two isoforms of the alpha subunit protein, AML1a and AML1b, are produced by alternative splicing of the wild-type AML1 gene. (medscape.com)
- CBF complexes binding to the transcriptional silencer is essential for recruitment of nuclear protein complexes that catalyze epigenetic modifications to establish epigenetic ZBTB7B silencing. (idrblab.net)
- HN - 2006(1981) BX - Cofilins MH - Actin-Related Protein 2 UI - D051377 MN - D5.750.78.730.246.500 MN - D12.776.220.525.246.500 MS - A PROFILIN binding domain protein that is part of the Arp2-3 complex. (nih.gov)
- HN - 2006(1998) MH - Actin-Related Protein 2-3 Complex UI - D051376 MN - D5.750.78.730.246 MN - D12.776.220.525.246 MS - A complex of seven proteins including ARP2 PROTEIN and ARP3 PROTEIN that plays an essential role in maintenance and assembly of the CYTOSKELETON. (nih.gov)
- Arp2-3 complex binds WASP PROTEIN and existing ACTIN FILAMENTS, and it nucleates the formation of new branch point filaments. (nih.gov)
- HN - 2006 BX - Arp2-3 Complex MH - Actin-Related Protein 3 UI - D051378 MN - D5.750.78.730.246.750 MN - D12.776.220.525.246.750 MS - A component of the Arp2-3 complex that is related in sequence and structure to ACTIN and that binds ATP. (nih.gov)
- It is expressed at higher levels than ARP2 PROTEIN and does not contain a PROFILIN binding domain. (nih.gov)
- protein_coding" "AAC73572","dnaX","Escherichia coli","DNA polymerase III/DNA elongation factor III, tau and gamma subunits [Ensembl]. (ntu.edu.sg)
- protein_coding" "AAC73733","dacA","Escherichia coli","D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5) [Ensembl]. (ntu.edu.sg)
- Penicillin-binding protein 5, D-alanyl-D-alanine carboxypeptidase [Interproscan]. (ntu.edu.sg)
- RNA-binding protein;RNA degradosome binding protein [Ensembl]. (ntu.edu.sg)
- protein_coding" "AAC74207","potD","Escherichia coli","spermidine/putrescine ABC transporter periplasmic binding protein [Ensembl]. (ntu.edu.sg)
- The effect of metformin on NAFLD mainly related to cytoplasm and protein binding, NAFLD, hepatitis B, pathway in cancer, toll like receptor signaling pathway and type 2 diabetes mellitus (T2DM). (bvsalud.org)
- The powdery mildew resistance gene Pm21, encoding a nucleotide-binding leucine-rich repeat receptor (NLR) protein, confers broad-spectrum resistance to powdery mildew and has great potential for controlling this disease. (bvsalud.org)
- Regulators of small G-proteins like guanine nucleotide releasing factor GNRP (Ras-GRF) (which contains 2 PH domains), guanine nucleotide exchange proteins like vav, dbl, SoS and Saccharomyces cerevisiae CDC24, GTPase activating proteins like rasGAP and BEM2/IPL2, and the human break point cluster protein bcr. (embl.de)
- Mouse protein citron, a putative rho/rac effector that binds to the GTP-bound forms of rho and rac. (embl.de)
- During the initiation of protein synthesis, what binds to the P-site? (flashcardmachine.com)
- What assists in protein folding by binding to hydrophobic regions exposed in an unfolded or partially folded protein? (flashcardmachine.com)
- AraC protein bound to arabinose and two two separate sites in the araBAD promoter region. (flashcardmachine.com)
- Protein Serine-threonine kinases that phosphorylate the 63-kDa subunit of AMP-ACTIVATED PROTEIN KINASES. (nih.gov)
- Binds DNA in conjunction with GTF2A2 and TBP (the TATA-binding protein) and together with GTF2A2, allows mRNA transcription. (nih.gov)
- The assembly and stability of the RNA polymerase II transcription pre-initiation complex on a eukaryotic core promoter involve the effects of transcription factor IIA (TFIIA) on the interaction between TATA-binding protein (TBP) and DNA. (nih.gov)
- protein_coding" "Cz08g16110.t1","No alias","Chromochloris zofingiensis","tRNA (1-methyladenosine) methyltransferase catalytic subunit Gcd14 [Interproscan]. (ntu.edu.sg)
- These studies demonstrate that a Cys430-Phe mutation does not prevent the de novo synthesis of the b subunit, but alters the conformation of the mutant protein sufficiently to impair its intracellular transport, resulting in its deficiency in this patient. (embl.de)
- Mediator, a large modular protein complex with varying subunit composition, bridges TFs with Pol II and coordinates DNA-loop formation, transcriptional initiation, and post-initiation events ( 3 , 4 ). (frontiersin.org)
- Tissue factor (TF) is an integral membrane protein that is essential to life. (hindawi.com)
- TF is an integral transmembrane protein expressed by various cells, is a component of the factor VIIa-TF complex enzyme and is essential for normal hemostasis [ 1 , 2 ]. (hindawi.com)
- The product of the protein Case reaction, activated protein C (APC), inactivates the cofactors factors Va and VIIIa. (hindawi.com)
- In eukaryotic organisms, there exist at least three distinct multi-protein assemblies that are jointly referred to as 'PCI complexes' [ 1 ] and have a similar subunit architecture despite their fundamentally different function: i) the proteasome lid, a subcomplex of the 19S proteasome regulator and the 26S proteasome, ii) the COP9 signalosome or CSN complex, and iii) the eukaryotic translation initiation factor eIF3. (biomedcentral.com)
- Binding-protein-dependent transport system inner membrane component [Interproscan]. (ntu.edu.sg)
- protein_coding" "AAC74155","flgM","Escherichia coli","anti-sigma factor for FliA (sigma 28) [Ensembl]. (ntu.edu.sg)
- Rod binding protein, Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase [Interproscan]. (ntu.edu.sg)
Polymerase5
- DNA polymerase III subunits gamma and tau domain III, DNA polymerase III subunits tau domain IV DnaB-binding, DNA polymerase III tau subunit V interacting with alpha [Interproscan]. (ntu.edu.sg)
- What general transcription factor for RNA polymerase II acts immediately after TFIID in the formation of the pre-initiation complex? (flashcardmachine.com)
- For those circumstances in which the holoenzyme is built onto the euchromatin, it is necessary to consider the holoenzyme components and the likely sequence of binding, RNA polymerase II entrance upon the scene and subsequent action. (wikiversity.org)
- The diagram describes the eukaryotic preinitiation complex which includes the general transcription factors and RNA Polymerase II. (wikiversity.org)
- Inducible transcriptional control relies on signal-activated transcription factors (TFs) that bind to DNA regulatory elements distant from the transcriptional start site (TSS) and facilitate the recruitment of transcriptional co-regulators and the general transcriptional machinery, including RNA polymerase II (Pol II). (frontiersin.org)
Catalytic2
- The proteins of hypoxia inducible factor-1 (HIF1A), nuclear factor erythroid 2-related factor (NFE2L2), nitric oxide synthase 3 (NOS3), nuclear receptor subfamily 3 group C member 1 (NR3C1), PI3K catalytic subunit alpha (PIK3CA), and silencing information regulator 2 related enzyme 1 (SIRT1) may the core targets of metformin for the treatment of NAFLD. (bvsalud.org)
- The E3 subunit is a flavoprotein- containing dihydrolipoamide dehydrogenase which is reduced and oxidized during the catalytic cycle to reset the E2 subunit for additional reactions. (aacc.org)
Cofactor4
- A transcription factor that dimerizes with the cofactor CORE BINDING FACTOR BETA SUBUNIT to form core binding factor. (nih.gov)
- Factor de transcripción que dimeriza con el cofactor SUBUNIDAD BETA DEL FACTOR DE UNIÓN AL SITIO PRINCIPAL para formar el factor de unión al sitio principal. (bvsalud.org)
- The E2 subunit is a dihydrolipoamide acyltransferase with a lipoic acid cofactor. (aacc.org)
- Upon an injury to the vessel wall, TF, a membrane-bound cofactor, is exposed to circulating factor VIIa, forming the extrinsic factor Xase, a complex enzyme. (hindawi.com)
Regulatory6
- RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-binding regulatory subunit that allosterically enhances the sequence-specific DNA-binding capacity of RUNX. (idrblab.net)
- METHODS: We performed conditional analysis of genetic association data and used ENCODE data on chromatin remodelling and transcription factor (TF) binding sites to identify the primary AS-associated regulatory SNP in the RUNX3 region. (ox.ac.uk)
- pRB functions as a negative regulatory transcription factor during the G1 to S phase cell cycle transition. (medscape.com)
- Transcription factors, proteins that bind to the regulatory sequences of target genes, compose the largest class of oncogenes identified in pediatric tumors. (medscape.com)
- Moreover, we show for the first time that the STAT1 C-terminal TAD is required for an efficient recruitment of components of the core Mediator complex to the IFN regulatory factor ( Irf ) 1 and Irf8 promoters, which both harbor an open chromatin state under basal conditions. (frontiersin.org)
- Binding to co-regulatory proteins, such as chromatin remodeling and histone modifying enzymes, occurs through one or more transactivation domains (TADs, also called activation domains) present in TFs ( 1 , 2 ). (frontiersin.org)
Kinase3
- S5 phosphorylation is triggered by cyclin dependent kinase (CDK) 7, the kinase subunit of the general TF (GTF) complex TFIIH, and allows Pol II to initiate transcription. (frontiersin.org)
- S2 phosphorylation of the Pol II CTD is executed by CDK9, the kinase subunit of the positive transcription elongation factor b (p-TEFb), which also phosphorylates negative elongation factors and enables the release of paused Pol II from the promoter ( 9 ). (frontiersin.org)
- The neutrophil B of IFN elongation and residue were bound in all characterized CNS symbols upon state with genes: C). distinctively, regulated kinase synergistically mediated detail I and III IFN organization in neural proteins and inhibitors( Lafaille FG et al. (erik-mill.de)
Runt domain3
- RUNX3 is a member of the runt domain-containing family of transcription factors. (nih.gov)
- It contains a highly conserved DNA-binding domain known as the runt domain. (nih.gov)
- It contains a highly conserved DNA-binding domain known as the runt domain and is involved in genetic regulation of skeletal development and CELL DIFFERENTIATION. (rush.edu)
Genes8
- [ 2 ] Recurrent chromosome translocations, inversions, and deletions result in structural genomic rearrangements often involving genes that encode transcription factors. (medscape.com)
- [ 3 , 4 ] CBF is an alpha/beta heterodimeric transcription factor involved in the transcriptional regulation of several genes important in hematopoiesis. (medscape.com)
- Disruption of the CBF subunit alpha and beta genes is involved in t(8;21)(q22;q22) and inv(16)(p13q22), respectively. (medscape.com)
- Three homologous genes can encode for the CBFalpha subunit. (medscape.com)
- [ 9 ] The CBFalpha subunit binds directly to the enhancer core DNA sequence on target genes, whereas the beta subunit does not bind the DNA directly but increases the affinity and stabilizes the binding of the alpha subunit to the DNA. (medscape.com)
- HN - 2006(1998) MH - Activating Transcription Factor 1 UI - D051697 MN - D12.776.260.108.61.500 MN - D12.776.930.127.61.500 MS - An activating transcription factor that regulates expression of a variety of genes including C-JUN GENES and TRANSFORMING GROWTH FACTOR BETA2. (nih.gov)
- A few dozen genes in the actin and tubulin cytoskeletal systems have been characterized thoroughly, including gene families encoding actins, profilins, actin depolymerizing factors, α-tubulins, and β-tubulins. (bioone.org)
- Prediction of Core Cancer Genes Using Multitask Classification Framework. (nih.gov)
RUNX32
- In this study, changes in the methylation of runt-related transcription factor-3 (RUNX3) were investigated in CCD18Co normal colon cells and DLD-1 colorectal adenocarcinoma cells. (nih.gov)
- The risk allele decreases TF binding (including IRF4) and reduces reporter activity and RUNX3 expression. (ox.ac.uk)
AML14
- The translocation produces a chimeric gene made up of the 5'-region of the AML1 gene fused to the 3'-region of this gene. (wikipedia.org)
- 3. Transcriptional activity of core binding factor-alpha (AML1) and beta subunits on murine leukemia virus enhancer cores. (nih.gov)
- The AML1 N-terminus contains the DNA binding motif. (medscape.com)
- [ 14 , 15 ] Structural analysis of the AML1/ETO mRNA reveals that most of the ETO coding region fuses to the DNA and beta binding domains of AML1 , creating a fusion transcript that lacks the AML1 transcription activation domain, just as is seen in the AML1a subunit. (medscape.com)
Beta10
- [ 8 ] The CBFbeta subunit is encoded by CBF _ beta on chromosome 16q22 and is disrupted by inv(16)(p13q22) and t(16;16)(p13;q22). (medscape.com)
- The most commonly used assays are for the beta subunit of hCG. (medscape.com)
- hCG is composed of alpha and beta subunits. (medscape.com)
- The free beta subunit of hCG differs from the others in that it has a 30-amino acid tailpiece at the COOH terminus. (medscape.com)
- Free beta subunits are degraded by macrophage enzymes in the kidney to make a beta subunit core fragment, which is primarily detected in urine samples. (medscape.com)
- The beta-hCG subunit is present in the syncytial layer of the blastomere. (medscape.com)
- Sheehan KCF , Lai KS, Dunn GP, Bruce AT, Diamond MS, Heutel JD, Dungo-Arthur C, Carrero JA, White JM, Hertzog PJ and Schreiber RD. Blocking Monoclonal Antibodies Specific for Mouse IFNalpha/beta Receptor Subunit 1 (IFNAR1) from Mice Immunized by In Vivo Hydrodynamic Transfection. (wustl.edu)
- This gene encodes a germ cell-specific counterpart of the large (alpha/beta) subunit of general transcription factor TFIIA that is able to stabilize the binding of TBP to DNA and may be uniquely important to testis biology. (nih.gov)
- It is composed of two subunits: E1 alpha and E1 beta. (aacc.org)
- The sushi domain folds into a small and compact hydrophobic core enveloped by six beta-strands and stabilised by two disulfide bridges. (embl.de)
TRNA3
- Leucyl-tRNA synthetase, tRNA synthetases class I (I, Anticodon-binding domain of tRNA [Interproscan]. (ntu.edu.sg)
- The E.coli ribosome has how many binding sites for tRNA? (flashcardmachine.com)
- Understanding the sequence specificity of tRNA binding to elongation factor Tu using tRNA mutagenesis. (colorado.edu)
Interproscan5
- Ftsk gamma domain, FtsK alpha domain, FtsK/SpoIIIE family, 4TM region of DNA translocase FtsK/SpoIIIE [Interproscan]. (ntu.edu.sg)
- S1 RNA binding domain, Ribonuclease E/G family, Polyribonucleotide phosphorylase C terminal [Interproscan]. (ntu.edu.sg)
- Thiamin pyrophosphokinase, thiamin-binding domain [Interproscan]. (ntu.edu.sg)
- Periplasmic binding proteins and sugar binding domain of LacI family [Interproscan]. (ntu.edu.sg)
- Anti-sigma-28 factor [Interproscan]. (ntu.edu.sg)
Recombinant2
Enhancer factor1
- 12. SL3-3 enhancer factor 1 transcriptional activators are required for tumor formation by SL3-3 murine leukemia virus. (nih.gov)
Sequence2
- They bind to RUNX-binding sequence within the ZBTB7B locus acting as transcriptional silencer and allowing for cytotoxic T cell differentiation. (idrblab.net)
- It is related in sequence and structure to ACTIN and binds ATP. (nih.gov)
Polymerases1
- only, small download Dis integrating proteins( preinitiation) involved from defective inactive main products Was reviewed into sites of downstream transduction tissues( NSC), polymerases, bonds and binds( Lafaille FG et al. (erik-mill.de)
Actin-binding1
- HN - 2006(1981) BX - Actin-Capping Proteins MH - Actin Depolymerizing Factors UI - D051339 MN - D5.750.78.730.212 MN - D12.776.220.525.212 MS - A family of low MOLECULAR WEIGHT actin-binding proteins found throughout eukaryotes. (nih.gov)
Proteins that bind2
- AN - coordinate IM with ADENOMA (IM) HN - 2006 BX - Corticotroph Adenoma BX - Pituitary Adenoma, ACTH-Secreting BX - Pituitary Corticotropin-Secreting Adenoma MH - Actin Capping Proteins UI - D051344 MN - D5.750.78.730.32 MN - D12.776.220.525.32 MS - Actin capping proteins are cytoskeletal proteins that bind to the ends of ACTIN FILAMENTS to regulate actin polymerization. (nih.gov)
- For proteins that bind to DNA via helix-turn-helix motif, what is in the turn to provide flexibility? (flashcardmachine.com)
Chromatin2
- Its effects on TF binding were investigated by electrophoretic mobility gel shift assays and chromatin immunoprecipitation. (ox.ac.uk)
- Transcriptome and chromatin immunoprecipitation sequencing (ChIP-seq) analyses demonstrated similar alterations of genome-wide binding of AFF4, cohesin and RNAP2 in CdLS and CHOPS syndrome. (nih.gov)
Ligand2
- cotranslationally, no subsequent CD62L brain on cytosines reported found after gradient of cellular cell neurons reduced from UNC93B-deficients Proteins with R-848( separation of TLR7 and TLR8)( von Bernuth H. specifically, no available ligand binds thought not not reviewed with SRC-mediated TLR7, TLR8, TLR9 active to lysosomal transcription so this sulfate is still been not. (erik-mill.de)
- ligand-independent binding activates a not recaptured range. (erik-mill.de)
Proteasome2
- The 'lid' subcomplex of the 26S proteasome and the COP9 signalosome (CSN complex) share a common architecture consisting of six subunits harbouring a so-called PCI domain ( p roteasome, C SN, e I F3) at their C-terminus, plus two subunits containing MPN domains ( M pr1/ P ad1 N -terminal). (biomedcentral.com)
- Unlike the proteasome lid and the CSN, the eIF3 complex contains a number of non-PCI/non-MPN subunits, which are required for its function in translation. (biomedcentral.com)
Nuclear6
- The binding of Jurkat or CD8+ T-cell nuclear extracts to the risk allele was decreased and IRF4 recruitment was reduced. (ox.ac.uk)
- The carboxy terminus of Spc110p, which binds calmodulin, resides at the central plaque, and the amino terminus resides at the inner plaque from which nuclear microtubules originate. (sdbonline.org)
- Microtubule organization requires the Tub4p complex, which binds to the nuclear side of the SPB at the N-terminal domain of Spc110p. (sdbonline.org)
- The solution structure of the 16th CCP module from human complement factor H has been determined by a combination of 2-dimensional nuclear magnetic resonance spectroscopy and restrained simulated annealing. (embl.de)
- Hepatocyte Nuclear Factor 4 Alpha and Farnesoid X Receptor Co-regulates Gene Transcription in Mouse Livers on a Genome-Wide Scale. (nih.gov)
- NURBS: A Database of Experimental and Predicted Nuclear Receptor Binding Sites. (nih.gov)
Transcriptional4
- On transcriptional level interferon and TNF signaling were deregulated in primary RUNX1 mut CML cells and stem cell and B-lymphoid factors upregulated giving a rise to distinct phenotype. (nature.com)
- The SCP is the strongest core promoter observed in vitro and in cultured cells and yields high levels of transcription in conjunction with transcriptional enhancers. (wikiversity.org)
- These data support a common molecular pathogenesis for CHOPS syndrome and CdLS caused by disturbance of transcriptional elongation due to alterations in genome-wide binding of AFF4 and cohesin. (nih.gov)
- UNC93B pore transactivates induced involved in the increased subunit to glycan infected course 5-phosphate 1( HSV1) activation( HSE), a transcriptional dyslexia during single superfamily of the characteristic consequent ha34( CNS)( Casrouge A et al. (erik-mill.de)
Interacts1
- It also interacts with other transcription factors. (nih.gov)
Domain8
- Genetic and biochemical data indicate that Spc98p and Spc97p from the Tub4p complex bind to the N-terminal domain of the SPB component Spc110p. (sdbonline.org)
- This Tub4p complex-binding domain of Spc72p is essential: temperature-sensitive alleles of SPC72 or overexpression of a binding domain-deleted variant of SPC72 (DeltaN-SPC72) impair cytoplasmic microtubule formation. (sdbonline.org)
- Exchange of the Tub4p complex-binding domains of Spc110p and Spc72p establishes that the Spc110p domain, when attached to DeltaN-Spc72p, is functional at the cytoplasmic site of the SPB, while the corresponding domain of Spc72p, when fused to DeltaN-Spc110p, leads to a dominant-negative effect. (sdbonline.org)
- The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. (embl.de)
- A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII. (embl.de)
- Molecular and cellular basis of deficiency of the b subunit for factor XIII secondary to a Cys430-Phe mutation in the seventh Sushi domain. (embl.de)
- As a common feature, these complexes are composed of multiple subunits harbouring the PCI domain, named after the three participating complexes [ 2 ], sometimes also referred to as the PINT domain [ 3 ]. (biomedcentral.com)
- Other subunits of these complexes are characterized by a second shared homology domain called MPN ( M pr1- P ad1 N -terminal) [ 2 , 3 ]. (biomedcentral.com)
Complex10
- RUNX1 , also known as core binding factor subunit alpha ( CBFA2 ), is a transcription factor (TF) and an essential component of the core binding factor complex that plays a key role in hematopoiesis [ 1 ]. (nature.com)
- Forms the heterodimeric complex core-binding factor (CBF) with CBFB. (idrblab.net)
- Studies have been carried out to determine how the Tub4p complex binds to the yeast microtubule organizing center, the spindle pole body (SPB). (sdbonline.org)
- The E1 subunit of the complex is responsible for the oxidative decarboxylation of 2-oxoacids and requires thiamin pyrophosphate as a co-factor. (aacc.org)
- E2 forms the core of the enzyme complex and is responsible for the formation of the acyl-CoA products. (aacc.org)
- It is a component of the factor VIIa-TF complex enzyme and plays a primary role in both normal hemostasis and thrombosis. (hindawi.com)
- With a vascular injury, TF becomes exposed to blood and binds plasma factor VIIa, and the resulting complex initiates a series of enzymatic reactions leading to clot formation and vascular sealing. (hindawi.com)
- The factor VIIa-TF complex initiates blood coagulation by activating the zymogens factor IX and factor X to their respective serine proteases, factor IXa and factor Xa. (hindawi.com)
- Factor IXa and factor Xa form complex enzymes with their nonenzymatic co-factors (factor VIIIa and factor Va, resp. (hindawi.com)
- By contrast, the eIF3 complex has a smaller number of PCI subunits (table 1 ) and its two MPN subunits are absent in several unicellular eukaryotes. (biomedcentral.com)
Polyomavirus1
- The heterodimers bind to the core site of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters. (idrblab.net)
Gene Expression1
- These findings indicate that gene expression levels can be modulated via the core promoter. (wikiversity.org)
XIII3
- We studied the defect responsible for deficiency of the b subunit for factor XIII in the first known case of this condition. (embl.de)
- Thrombin accelerates its own generation via several feed-back reactions, cleaves fibrinogen, and activates factor XIII, which leads to the formation of a crosslinked insoluble fibrin clot [ 6 , 7 ] (Figure 1 ). (hindawi.com)
- and activates factor XIII to form a cross-linked fibrin clot. (hindawi.com)
Eukaryotes1
- What is ORC bound by in the DNA replication process of Eukaryotes? (flashcardmachine.com)
Cells5
- The mutant as well as wild-type b subunit was synthesized by the cells. (embl.de)
- The mutant b subunit was secreted from the cells much less effectively than the wild type and remained susceptible to endoglycosidase H, indicating that it was not transported from the endoplasmic reticulum to the Golgi apparatus where the processing of oligosaccharides occurs. (embl.de)
- These toxins bind to specific receptors of the intestinal epithelial cells and cause secretion of water and electrolytes into the intestinal lumen. (cdc.gov)
- Under normal circumstances cells in contact with blood do not express physiologically active TF [ 3 ]. (hindawi.com)
- The hypoxia-inducible factors (HIF) act as hypoxia sensors that orchestrate a coordinated response increasing the pro-survival and pro-invasive phenotype of cancer cells, and determine a broad metabolic rewiring. (mdpi.com)
20201
- As of 24:00 on 3 March 2020 (Beijing time), the SARS-CoV-2 has resulted in 80,270 laboratory and clinical confirmed cases in the mainland of China, and 2981 patient deaths [ 10 ]. (springer.com)
RUNX1
- Heredity factors are important for BMD, and Runx-2 is accepted as a regulator of osteoblasts and bone formation. (univr.it)
Ribosomal1
- complement Complexes may navigate to the eye via a third nucleoside of ribosomal Fc awnings that may, in 3-phosphate, family oxygen evidence further. (familie-vos.de)
Primarily1
- The vitro of the form primarily atomic to subunit of Ca2+ active AMPA acts, which is Na+ activity, affecting to the SSA of NMDA proteinases. (erik-mill.de)
Regulation1
- Several S. cerevisiae proteins involved in cell cycle regulation and bud formation like BEM2, BEM3, BUD4 and the BEM1-binding proteins BOI2 (BEB1) and BOI1 (BOB1). (embl.de)
Nucleotide1
- Crk proteins activate the Rap1 guanine nucleotide exchange factor C3G by segregated adaptor-dependent and -independent mechanisms. (nih.gov)
Elongation Factors1
- Typically, after 20-60 nucleotides from the TSS, Pol II is driven into a paused condition by negative elongation factors. (frontiersin.org)
Differentiation1
- Transcription factor involved in osteoblastic differentiation and skeletal morphogenesis. (abcam.com)
Yeast1
- Directed mutagenesis identifies amino acid residues involved in elongation factor Tu binding to yeast Phe-tRNAPhe. (colorado.edu)
Enzyme6
- 9/3/2005) TOTAL DESCRIPTORS = 935 MH - 1-Acylglycerol-3-Phosphate O-Acyltransferase UI - D051103 MN - D8.811.913.50.173 MS - An enzyme that catalyzes the acyl group transfer of ACYL COA to 1-acyl-sn-glycerol 3-phosphate to generate 1,2-diacyl-sn-glycerol 3-phosphate. (nih.gov)
- HN - 2006(1983) MH - 2-Oxoisovalerate Dehydrogenase (Acylating) UI - D050645 MN - D8.811.682.657.350.825 MS - An NAD+ dependent enzyme that catalyzes the oxidation 3-methyl-2-oxobutanoate to 2-methylpropanoyl-CoA. (nih.gov)
- use AMINO ACIDS, BRANCHED-CHAIN 1979, & KETO ACIDS & VALERATES 1973-1979 MH - 3-Hydroxyanthranilate 3,4-Dioxygenase UI - D050561 MN - D8.811.682.690.416.328 MS - An enzyme that catalyzes the conversion of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde. (nih.gov)
- use ANTHRANILIC ACID 1974-1979 MH - 3-Isopropylmalate Dehydrogenase UI - D050539 MN - D8.811.682.47.500 MS - An NAD+ dependent enzyme that catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate to 3-carboxy-4-methyl-2-oxopentanoate. (nih.gov)
- use DICARBOXYLIC ACIDS 1970-1979 MH - 3-Phosphoshikimate 1-Carboxyvinyltransferase UI - D051229 MN - D8.811.913.225.735 MS - An enzyme of the shikimate pathway of AROMATIC AMINO ACID biosynthesis, it generates 5-enolpyruvylshikimate 3-phosphate and ORTHOPHOSPHATE from PHOSPHOENOLPYRUVATE and SHIKIMATE-3-PHOSPHATE. (nih.gov)
- When mechanical or chemical damage of the vascular wall occurs, subendothelial TF is expressed/exposed to blood flow and binds plasma factor VIIa, which circulates as an enzyme at a concentration of approximately 0.1 nM (1% of plasma factor VII) [ 4 ] and escapes the inhibition by serine proteases inhibitors because of its poor enzymatic qualities [ 1 , 5 ]. (hindawi.com)
Abundant1
- Although the L-VDCC subunits are most abundant in fast skeletal transverse tubules, Ca 2+ influx is not required for contraction in skeletal muscle, unlike cardiac muscle, which requires Ca 2+ entry with each beat and triggers Ca 2+ release from the sarcoplasmic reticulum (SR) via Ca 2+ -release channels, e.g., ryanodine receptor 2 (RyR2). (jci.org)
Membrane bound1
- BCAAs in circulation are taken up by a membrane bound transporter system and are reversibly deaminated by pyridoxine-dependent branched-chain aminotransferases (BCATs), producing branched chain-2-oxoacids. (aacc.org)
Specific transcription1
- May function as a testis specific transcription factor. (nih.gov)