HMGB Proteins
HMGB3 Protein
High Mobility Group Proteins
Chromatin
DNA
Protein Structure, Tertiary
Protein Binding
Amino Acid Sequence
Molecular Sequence Data
Establishment and maintenance of the border of the neural plate in the chick: involvement of FGF and BMP activity. (1/333)
We have investigated the cell interactions and signalling molecules involved in setting up and maintaining the border between the neural plate and the adjacent non-neural ectoderm in the chick embryo at primitive streak stages. msx-1, a target of BMP signalling, is expressed in this border at a very early stage. It is induced by FGF and by signals from the organizer, Hensen's node. The node also induces a ring of BMP-4, some distance away. By the early neurula stage, the edge of the neural plate is the only major site of BMP-4 and msx-1 expression, and is also the only site that responds to BMP inhibition or overexpression. At this time, the neural plate appears to have a low level of BMP antagonist activity. Using in vivo grafts and in vitro assays, we show that the position of the border is further maintained by interactions between non-neural and neural ectoderm. We conclude that the border develops by integration of signals from the organizer, the developing neural plate, the paraxial mesoderm and the non-neural epiblast, involving FGFs, BMPs and their inhibitors. We suggest that BMPs act in an autocrine way to maintain the border state. (+info)XCtBP is a XTcf-3 co-repressor with roles throughout Xenopus development. (2/333)
XTcf-3 is an HMG box transcription factor that mediates Xenopus dorsal-ventral axis formation. As a Wnt pathway effector, XTcf-3 interacts with beta-catenin and activates the expression of the dorsal organizing gene siamois, while in the absence of beta-catenin, XTcf-3 functions as a transcriptional repressor. We show that XTcf-3 contains amino- and carboxy-terminal repressor domains and have identified a Xenopus member of the C-terminal Binding Protein family of transcriptional co-repressors (XCtBP) as the C-terminal co-repressor. We show that two XCtBP binding sites near the XTcf-3 carboxy-terminus are required for the interaction of XTcf-3 and XCtBP and for the transcriptional repression mediated by the XTcf-3 carboxy-terminal domain. By fusing the GAL4 activation domain to XCtBP we have generated an antimorphic protein, XCtBP/G4A, that activates siamois transcription through an interaction with endogenous XTcf-3. Ectopic expression of XCtBP/G4A demonstrates that XCtBP functions in the regulation of head and notochord development. Our data support a role for XCtBP as a co-repressor throughout Xenopus development and indicate that XCtBP/G4A will be a useful tool in determining how XCtBP functions in various developmental processes. (+info)Beta- and gamma-catenin mutations, but not E-cadherin inactivation, underlie T-cell factor/lymphoid enhancer factor transcriptional deregulation in gastric and pancreatic cancer. (3/333)
Adenomatous polyposis coli (APC) mutations are present in >70% of colon cancers. The APC protein binds to beta-catenin (beta-cat), a protein first identified because of its role in E-cadherin (E-cad) cell adhesion. In some colon cancers lacking APC defects, mutations in presumptive glycogen synthase kinase 3beta phosphorylation sites near the beta-cat NH2 terminus appear to render beta-cat resistant to regulation by APC and glycogen synthase kinase 3beta. In cells with APC or beta-cat defects, beta-cat is stabilized and, in turn, binds to and activates T-cell factor (Tcf)/lymphoid enhancer factor (Lef) transcription factors. To further explore the role of APC, beta-cat, Tcf, and E-cad defects in gastrointestinal cancers, we assessed gastric and pancreatic cancers for constitutive Tcf transcriptional activity (CTTA). Two of four gastric and two of eight pancreatic cancer lines showed CTTA. One gastric and one pancreatic cancer had mutations in the NH2-terminal phosphorylation sites of beta-cat. The other gastric cancer with CTTA had a missense mutation at serine 28 of gamma-cat, a potential phosphorylation site in this beta-cat-related protein. Although E-cad is an important binding partner for beta-cat and gamma-cat, E-cad inactivation did not result in CTTA. The beta-cat and gamma-cat mutant proteins identified in our studies strongly activated Tcf transcription in vitro, whereas beta-cat mutant proteins with large NH2-terminal deletions had only modest effects on Tcf. Our results suggest a role for Tcf deregulation in gastric and pancreatic cancer, resulting from beta-cat and gamma-cat mutations in some cases and, in others, from yet to be defined defects. Furthermore, these data imply that the consequences of APC and beta-cat mutations are distinct from the effects of E-cad inactivation. (+info)The gene for the embryonic stem cell coactivator UTF1 carries a regulatory element which selectively interacts with a complex composed of Oct-3/4 and Sox-2. (4/333)
UTF1 is a transcriptional coactivator which has recently been isolated and found to be expressed mainly in pluripotent embryonic stem (ES) cells (A. Okuda, A. Fukushima, M. Nishimoto, et al., EMBO J. 17:2019-2032, 1998). To gain insight into the regulatory network of gene expression in ES cells, we have characterized the regulatory elements governing UTF1 gene expression. The results indicate that the UTF1 gene is one of the target genes of an embryonic octamer binding transcription factor, Oct-3/4. UTF1 expression is, like the FGF-4 gene, regulated by the synergistic action of Oct-3/4 and another embryonic factor, Sox-2, implying that the requirement for Sox-2 by Oct-3/4 is not limited to the FGF-4 enhancer but is rather a general mechanism of activation for Oct-3/4. Our biochemical analyses, however, also reveal one distinct difference between these two regulatory elements: unlike the FGF-4 enhancer, the UTF1 regulatory element can, by its one-base difference from the canonical octamer-binding sequence, selectively recruit the complex comprising Oct-3/4 and Sox-2 and preclude the binding of the transcriptionally inactive complex containing Oct-1 or Oct-6. Furthermore, our analyses reveal that these properties are dictated by the unique ability of the Oct-3/4 POU-homeodomain that recognizes a variant of the Octamer motif in the UTF1 regulatory element. (+info)Maternal and embryonic expression of zebrafish lef1. (5/333)
Transcription factors of the TCF/LEF family interact with the Wnt signaling pathway to control transcription of downstream genes (Clevers, H., van de Wetering, M., 1997. TCF/LEF factor earn their wings. Trends Genet. 13, 485-489). We were interested in cloning family members which were expressed in zebrafish neural crest, because Wnt signaling modulates specification of neural crest fate (Dorsky, R.I., Moon, R.T., Raible, D.W., 1998. Control of neural crest cell fate by the Wnt signalling pathway. Nature 396, 370-373). We cloned a zebrafish homolog of lef1 and localized its chromosomal position by radiation hybrid mapping. lef1 is expressed in the neural crest as well as the tailbud and developing mesoderm, and is maternally expressed in zebrafish, unlike mouse and Xenopus homologs. In addition, we cloned two tcf3 genes and a homolog of tcf4, neither of which were strongly expressed in premigratory neural crest. (+info)Comparative expression of the mouse Sox1, Sox2 and Sox3 genes from pre-gastrulation to early somite stages. (6/333)
Whole mount in situ hybridisation was used to study the embryonic expression of the mouse HMG box-containing genes Sox1, Sox2 and Sox3 between 6.5 and 9.0 days post coitum (dpc). Sox2 and Sox3 are expressed in the epiblast and extraembryonic ectoderm of the egg cylinder, becoming restricted to the prospective neural plate and chorion at the onset of gastrulation. Sox3 is upregulated in the posterior ectoderm during late streak and neural plate stages and is concomitantly downregulated in the chorion. Sox1 transcripts are first detected in the neural fold ectoderm at the headfold stage. During early somitogenesis, all three genes are expressed in the neuroectoderm, and Sox2 and Sox3 are also expressed in the primitive streak ectoderm, gut endoderm and prospective sensory placodes. (+info)Two distinct subgroups of Group B Sox genes for transcriptional activators and repressors: their expression during embryonic organogenesis of the chicken. (7/333)
Group B Sox genes, Sox1, -2 and -3 are known to activate crystallin genes and to be involved in differentiation of lens and neural tissues. Screening of chicken genomic sequences for more Group B Sox genes identified two additional genes, Sox14 and Sox21. Proteins encoded by Sox14 and Sox21 genes are similar to each other but distinct from those coded by Sox1-3 (subgroup B1) except for the HMG domain and Group B homology immediately C-proximal of the HMG domain. C-terminal domains of SOX21 and SOX14 proteins function as strong and weak repression domains, respectively, when linked to the GAL4 DNA binding domain. These SOX proteins strongly (SOX21) or moderately (SOX14) inhibited activation of delta1-crystallin DC5 enhancer by SOX1 or SOX2, establishing that Sox14 and Sox21 are repressing subgroup (B2) of Group B Sox genes. This provides the first evidence for the occurrence of repressor SOX proteins. Activating (B1) and repressing (B2) subgroups of Group B Sox genes display interesting overlaps of expression domains in developing tissues (e.g. optic tectum, spinal cord, inner ear, alimentary tract, branchial arches). Within each subgroup, most expression domains of Sox1 and -3 are included in those of Sox2 (e.g. CNS, PNS, inner ear), while co-expression of Sox14 and Sox21 occurs in highly restricted sites of the CNS, with the likely temporal order of Sox21 preceding Sox14 (e.g. interneurons of the spinal cord). These expression patterns suggest that target genes of Group B SOX proteins are finely regulated by the counterbalance of activating and repressing SOX proteins. (+info)Direct regulation of the Xenopus engrailed-2 promoter by the Wnt signaling pathway, and a molecular screen for Wnt-responsive genes, confirm a role for Wnt signaling during neural patterning in Xenopus. (8/333)
The co-activation of Wnt signaling and concomitant inhibition of BMP signaling has previously been implicated in vertebrate neural patterning, as evidenced by the combinatorial induction of engrailed-2 and krox-20 in Xenopus. However, screens have not previously been conducted to identify additional potential target genes. Using a PCR-based screening method we determined that XA-1, xCRISP, UVS.2, two UVS.2-related genes, and xONR1 are induced in response to Xwnt-3a and a BMP-antagonist, noggin. Two additional genes, connexin 30 and retinoic acid receptor gamma were induced by Xwnt-3a alone. To determine whether any of the induced genes are direct targets of Wnt signaling, we focussed on engrailed-2. In the present study we show that the Xenopus engrailed-2 promoter contains three consensus binding sites for LEF/TCF, which are HMG box transcription factors which bind to beta-catenin in response to activation of the Wnt- 1 signaling pathway. An engrailed-2 promoter luciferase reporter construct containing these LEF/TCF sites is induced in embryo explant assays by the combination of Xwnt-3a or beta-catenin and noggin. These LEF/TCF sites are required for expression of engrailed-2, as a dominant negative Xtcf-3 blocks expression of endogenous engrailed-2 as well as expression of the reporter construct. Moreover, mutation of these three LEF/TCF sites abrogates expression of the reporter construct in response to noggin and Xwnt-3a or beta-catenin. We conclude that the engrailed-2 gene is a direct target of the Wnt signaling pathway, and that Wnt signaling works with BMP antagonists to regulate gene expression during patterning of the developing nervous system of Xenopus. (+info)High Mobility Group Box (HMGB) proteins are a family of nuclear proteins that are highly conserved and expressed in eukaryotic cells. They play a crucial role in the regulation of gene expression, DNA repair, and maintenance of nucleosome structure. HMGB proteins contain two positively charged DNA-binding domains (HMG boxes) and a negatively charged acidic tail. These proteins can bind to DNA in a variety of ways, bending it and altering its structure, which in turn affects the binding of other proteins and the transcriptional activity of genes. HMGB proteins can also be released from cells under conditions of stress or injury, where they act as damage-associated molecular patterns (DAMPs) and contribute to the inflammatory response.
High Mobility Group Box 2 (HMGB2) protein is a member of the high mobility group box family, which are nuclear proteins that function as architectural chromatin-binding factors. HMGB2 protein has been shown to play roles in DNA replication, repair, recombination, and transcription. It can also be released from cells under conditions of stress or injury, where it acts as a damage-associated molecular pattern (DAMP) molecule, contributing to inflammation and immune responses. HMGB2 is highly expressed during embryonic development and in certain types of adult stem cells, suggesting roles in development and tissue regeneration.
High Mobility Group Box 1 (HMGB1) protein is a non-histone chromosomal protein that is widely expressed in various cell types, including immune cells and nucleated cells. It plays a crucial role in the maintenance of nucleosome structure and stability, regulation of gene transcription, and DNA replication and repair. HMGB1 can be actively secreted by activated immune cells or passively released from necrotic or damaged cells. Once outside the cell, it functions as a damage-associated molecular pattern (DAMP) molecule that binds to various receptors, such as Toll-like receptors and the receptor for advanced glycation end products (RAGE), on immune cells, leading to the activation of inflammatory responses and the induction of innate and adaptive immunity. HMGB1 has been implicated in various physiological and pathological processes, including inflammation, infection, autoimmunity, cancer, and neurological disorders.
High Mobility Group Nucleosome Binding (HMGN) proteins are a group of small, non-histone chromosomal proteins found in the nucleus of eukaryotic cells. They are involved in the regulation of gene transcription, DNA replication, and repair by binding to nucleosomes and altering the structure of chromatin. HMGN proteins have been shown to facilitate the access of transcription factors to their target sites on the DNA, thereby playing a crucial role in the control of gene expression. They are also known to be involved in the maintenance of genome stability and are associated with various chromatin-related processes, including chromosomal organization and dynamics.
High Mobility Group Box 3 (HMGB3) protein, also known as HMG-IY, is a member of the high mobility group box (HMGB) family of proteins. These proteins are characterized by their ability to bind to DNA and function as architectural factors in the regulation of gene transcription, DNA replication, and repair.
HMGB3 protein is widely expressed in various tissues, including the testis, brain, heart, lung, liver, skeletal muscle, and kidney. It has been implicated in several biological processes, such as embryonic development, cell differentiation, and tumorigenesis. HMGB3 can act as a transcriptional regulator by binding to specific DNA sequences and interacting with other proteins involved in gene expression.
In cancer, HMGB3 has been found to be overexpressed in several types of malignancies, including hepatocellular carcinoma, colorectal cancer, gastric cancer, and breast cancer. High levels of HMGB3 have been associated with poor prognosis, increased tumor growth, and metastasis. Therefore, HMGB3 is considered a potential therapeutic target for cancer treatment.
High mobility group proteins (HMG proteins) are a family of nuclear proteins that are characterized by their ability to bind to DNA and influence its structure and function. They are named "high mobility" because of their rapid movement in gel electrophoresis. HMG proteins are involved in various nuclear processes, including chromatin remodeling, transcription regulation, and DNA repair.
There are three main classes of HMG proteins: HMGA, HMGB, and HMGN. Each class has distinct structural features and functions. For example, HMGA proteins have a unique "AT-hook" domain that allows them to bind to the minor groove of AT-rich DNA sequences, while HMGB proteins have two "HMG-box" domains that enable them to bend and unwind DNA.
HMG proteins play important roles in many physiological and pathological processes, such as embryonic development, inflammation, and cancer. Dysregulation of HMG protein function has been implicated in various diseases, including neurodegenerative disorders, diabetes, and cancer. Therefore, understanding the structure, function, and regulation of HMG proteins is crucial for developing new therapeutic strategies for these diseases.
Chromatin is the complex of DNA, RNA, and proteins that make up the chromosomes in the nucleus of a cell. It is responsible for packaging the long DNA molecules into a more compact form that fits within the nucleus. Chromatin is made up of repeating units called nucleosomes, which consist of a histone protein octamer wrapped tightly by DNA. The structure of chromatin can be altered through chemical modifications to the histone proteins and DNA, which can influence gene expression and other cellular processes.
Deoxyribonucleic acid (DNA) is the genetic material present in the cells of organisms where it is responsible for the storage and transmission of hereditary information. DNA is a long molecule that consists of two strands coiled together to form a double helix. Each strand is made up of a series of four nucleotide bases - adenine (A), guanine (G), cytosine (C), and thymine (T) - that are linked together by phosphate and sugar groups. The sequence of these bases along the length of the molecule encodes genetic information, with A always pairing with T and C always pairing with G. This base-pairing allows for the replication and transcription of DNA, which are essential processes in the functioning and reproduction of all living organisms.
Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.
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.
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.
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.
Coronary thrombosis
HMGB2
HMGN
Nucleosome
List of MeSH codes (D12.776.660)
Pyroptosis
High-mobility group
HMGA1
Chondroblast
UBTF
List of MeSH codes (D12.776)
Phagocytosis
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Publication Detail
CIPSM - Research Area D
Wael Jarjour, MD | Ohio State College of Medicine
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HMGB115
- The protein HMGB1 behaves as a redox sensor and its structural changes, which are conditioned by the oxidative environment, are associated with different functions of the protein. (hindawi.com)
- HMGB1 is an abundant protein, 10 6 molecules per cell [ 7 ], which has been postulated as a redox sensor [ 8 ]. (hindawi.com)
- The Jarjour lab has discovered that proinflammatory protein HMGB1 is a substrate of transglutaminase-2 and forms high-molecular-weight complexes with autoantigens. (osu.edu)
- Human High-mobility group box 1 protein (HMGB1), previously known as HMG1 or amphoterin, is a member of the high mobility group box family of non- histone chromosomal proteins. (reliatech.de)
- A recombinant fusion protein containing a sequence corresponding to amino acids 1-215 of human HMGB1. (thermofisher.cn)
- HMGB1 (High-mobility group box-1) protein was originally described as a nuclear non-histone DNA binding chromosomal protein. (thermofisher.cn)
- HMGB1 also act as DNA nuclear binding protein that has recently been shown to be an early trigger of sterile inflammation in animal models of trauma-hemorrhage via the activation of the Toll-like receptor 4 (TLR4) and the receptor for the advanced glycation endproducts (RAGE). (thermofisher.cn)
- In this study, The Cancer Genome Atlas, Gene Expression Omnibus database, Human Protein Atlas, and bioinformatic tools were used to conduct pan-cancer analysis of HMGB1 in various cancers so as to elucidate its role in human tumorigenesis. (accscience.com)
- High-mobility group box 1 (HMGB1) is a nuclear protein that can also act as an extracellular trigger of inflammation, proliferation, and migration in eye diseases. (pkc-inhibitor.com)
- Several studies indicate that ocular diseases have a close relationship with autoimmune reactions and inflammatory responses [2C5], and a key protein in such processes is high-mobility group box 1 (HMGB1) [6C8]. (pkc-inhibitor.com)
- HMGB1 is a DNA-binding nuclear protein discovered over 30 years ago [9C11]. (pkc-inhibitor.com)
- HMGB1 was identified as a nonhistone chromatin-binding protein about 30 years ago [9C11]. (pkc-inhibitor.com)
- HMGB1 is a member of the high-mobility group (HMG) chromosomal protein family [28]. (pkc-inhibitor.com)
- High-mobility group box 1 protein (HMGB1) has been reported to be a potent proangiogenic factor induced by inflammatory stress. (molvis.org)
- The expression of HMGB1, c-Jun N-terminal kinase (JNK), extracellular-signal-regulated kinase (ERK), and p38 mitogen-activated protein kinase (p38 MAPK) was assessed with immunofluorescence and western blot analysis. (molvis.org)
Recombinant2
- This antibody was produced from a hybridoma (mouse myeloma fused with spleen cells from a mouse) immunized with human recombinant protein of HMGB-1. (reliatech.de)
- Recombinant Human High Mobility Group Protein B1 is produced by our Mammalian expression system and the target gene encoding Gly2-Glu215 is expressed with a 6His tag at the C-terminus. (assaygenie.com)
HMG17
- Description: A sandwich quantitative ELISA assay kit for detection of Rat High Mobility Group Protein 1 (HMG1) in samples from serum, plasma, tissue homogenates or other biological fluids. (orbitalbiosciences.com)
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Pig High Mobility Group Protein 1 (HMG1) in serum, plasma and other biological fluids. (orbitalbiosciences.com)
- Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Pig High Mobility Group Protein 1 (HMG1) in samples from Serum, plasma and other biological fluids with no significant corss-reactivity with analogues from other species. (orbitalbiosciences.com)
- The HMG1/2 family is a large group of proteins that share a conserved sequence of ~80 amino acids rich in basic, aromatic and proline side chains, referred to as an HMG box. (nyu.edu)
- To define the basis for DNA recognition by HMG boxes, we characterize the interaction of two model HMG boxes, one a structure-specific box, rHMGb from the rat HMG1 protein, the other a sequence-specific box, Rox1 from yeast, with oligodeoxynucleotide substrates. (nyu.edu)
- We believe that these multimeric complexes are relevant for HMG1/2 proteins in vivo, since Mg 2+ is present in the nucleus and these proteins are expressed at a very high level. (nyu.edu)
- We believe that these multimeric complexes are relevant for HMG1/2 proteins in vivo, since Mg2+ is present in the nucleus and these proteins are expressed at a very high level. (nyu.edu)
Proto-Oncogene1
- A family of inhibitory proteins which bind to the REL PROTO-ONCOGENE PROTEINS and modulate their activity. (bvsalud.org)
Ribosomal Protein1
- In the current study, extensive chromatin immunoprecipitation (ChIP) and ChIP-sequencing analyses revealed that Fpr1 associates specifically with the upstream activating sequences of nearly all RPG (ribosomal protein gene) promoters, presumably in a manner dependent on Rap1 (repressor/activator site binding protein 1). (prolekarniky.cz)
Assembly of nucleoprotein2
Proinflammatory1
- Intracerebral disulfide HMGB-1 mimicked the effect of the stressor, because microglia isolated from HMGB-1-treated rats expressed exaggerated NLRP3 and proinflammatory cytokine expression after LPS treatment, whereas fully reduced HMGB-1 had no effect. (jneurosci.org)
Chromosomal protein3
- The AT-hook is a small DNA-binding protein motif which was first described in the high mobility group non-histone chromosomal protein HMG-I(Y). Since its discovery, this motif has been observed in other DNA-binding proteins from a wide range of organisms. (embl.de)
- With our study we aimed at investigating the levels of high mobility group box chromosomal protein-1 (HMGB-1), tumor necrosis factor-alpha (TNF-α) and interleukin (IL)-1β in periimplant crevicular fluid (PICF) of smokers and never-smokers, with and without periimplantitis, and correlate these levels with the clinical and radiographic periimplant parameters. (europeanreview.org)
- Increased levels of immunological and inflammatory mediators (eg, interleukins 1 and 8, eotaxin, the adhesion molecule E-selectin, the water-channel proteins aquaphorin 1 and aquaphorin 3, the chemotactic factor psoriasin, high-mobility group box chromosomal protein 1, nitric oxide and its isoforms, the antimicrobial peptide LL-37) suggest that erythema toxicum neonatorum may be an immune system reaction. (medscape.com)
Interactions4
- High mobility group (HMG) box domains are involved in binding DNA, and may be involved in protein-protein interactions as well. (embl.de)
- The histone chaperone FACT (facilitates chromatin transcription) enhances transcription in eukaryotic cells, targeting DNA-protein interactions. (elsevierpure.com)
- while the SSRP1 HMGB domain displaces DNA, SPT16 MD/CTD stabilizes DNA-H2A/H2B dimer interactions. (elsevierpure.com)
- We developed a new single-molecule method to probe non-specific DNA interactions for two HMGB homologs: the human HMGB2 box A domain and yeast Nhp6Ap, along with chimeric mutants replacin. (shengsci.com)
Molecules2
- Glycation, the result of a protein or lipid molecule bonding with sugar molecules, is a consequence of the aging process. (molvis.org)
- Deep sequencing of RNA molecules cross-linked to immunoprecipitated protein particles (CLIP-seq) revealed. (shengsci.com)
Chromatin3
- HMG-box domains are found in one or more copies in HMG-box proteins, which form a large, diverse family involved in the regulation of DNA-dependent processes such as transcription, replication, and strand repair, all of which require the bending and unwinding of chromatin. (embl.de)
- Furthermore, AT-hook motifs are frequently associated with known functional domains seen in chromatin proteins and in DNA-binding proteins (e.g. histone folds, homeodomains and zinc fingers). (embl.de)
- Goodwin GH, Sanders C, Johns EW, 1973, A new group of chromatin-associated proteins with a high content of acidic and basic amino acids. (accscience.com)
VIVO2
- Exposure to 100 inescapable tail shocks (ISs) increased HMGB-1 and NLRP3 protein in the hippocampus and led isolated microglia to release HMGB-1 ex vivo . (jneurosci.org)
- All proteins are LPS free, so they are suitable for in vitro and in vivo researches. (hmgbiotech.eu)
Transcriptional1
- Analyzing 5′-upstream non-protein-encoding regions of the human mitochondrial function-associated genes, we speculate that mitochondrial functions could be recovered or improved at a transcriptional level. (intechopen.com)
Complexes3
- Both proteins interact with single-stranded oligonucleotides in this study to form 1:1 complexes. (nyu.edu)
- In the case of the sequence-specific Rox1 protein we find tight 1:1 and 2:1 complexes with its cognate duplex sequence and again a 4:1 complex with four-way branched DNA. (nyu.edu)
- If the DNA branching is reduced to three arms, both proteins form 3:1 complexes. (nyu.edu)
Genes2
- Such bending stabilizes nucleosome formation and regulates the expression of select genes upon recruitment by DNA binding proteins. (reliatech.de)
- Cellular DNA-binding proteins encoded by the rel gene (GENES, REL). (bvsalud.org)
Encodes3
- Encodes a protein belonging to the subgroup of HMGB (high mobility group B) proteins that have a distinctive DNA-binding motif, the HMG-box domain. (or.jp)
- This gene encodes a protein belonging to the DNA mismatch repair mutL/hexB family. (nih.gov)
- Encodes HMGB6, a protein belonging to the subgroup of HMGB (high mobility group B) proteins. (riken.jp)
Nucleus2
- Further we demonstrate that ICK1/KRP1 is an unstable protein and degraded by the 26S proteasome in the nucleus. (uni-bielefeld.de)
- In the CYTOPLASM, I-kappa B proteins bind to the transcription factor NF-KAPPA B. Cell stimulation causes its dissociation and translocation of active NF-kappa B to the nucleus. (bvsalud.org)
Redox1
- Changes in the redox state of cells affect proteins, lipids, and nucleic acids in different ways. (hindawi.com)
Kinase1
- HMGB6 is phosphorylated by protein kinase CK2alpha within its acidic C-terminal domain. (riken.jp)
Human5
- This review describes recent advances in the role of human HMGB proteins and other proteins interacting with them, in cancerous processes related to oxidative stress, with special reference to ovarian and prostate cancer. (hindawi.com)
- To assess the linearity of the assay, samples were spiked with high concentrations of human HMGB-1 in various matrices and diluted with the Sample Diluent to produce samples with values within the dynamic range of the assay. (cusabio.com)
- The recovery of human HMGB-1 spiked to levels throughout the range of the assay in various matrices was evaluated. (cusabio.com)
- Altered expression of mismatch repair proteins associated with acquisition of microsatellite instability in a clonal model of human T lymphocyte aging. (nih.gov)
- Crevicular levels of HMGB-1, TNF-α, and IL-1β were quantified using human enzyme linked immunosorbent assay. (europeanreview.org)
Nuclear protein1
- It was originally discovered as a nuclear protein that could bend DNA. (reliatech.de)
Yeast1
- In a hmo1 Δ (high mobility group family 1-deleted) yeast strain, deletion of FPR1 induced severe growth defects, which could be alleviated by increasing the copy number of RPL25 (ribosome protein of the large subunit 25), suggesting that RPL25 expression was affected in hmo1 Δ fpr1 Δ cells. (prolekarniky.cz)
Saccharomyces1
- Fpr1 (FK506-sensitive proline rotamase 1 ) , a protein of the FKBP12 (FK506-binding protein 12 kDa) family in Saccharomyces cerevisiae , is a primary target for the immunosuppressive agents FK506 and rapamycin. (prolekarniky.cz)
Induces1
- Cyt c then together with ATP or dATP induces a conformational change in the adaptator protein Apaf-1 (a homologue of the C. elegans CED4 protein) (Zou, Henzel et al. (uni-frankfurt.de)
Gene expression1
- Many of these proteins are regulators of gene expression. (embl.de)
Differentiation1
- Roquin proteins preclude spontaneous T cell activation and aberrant differentiation of T follicular helper (Tfh) or T helper 17 (Th17) cells. (cipsm.de)
Sequence5
- Using pattern searches and position-dependent matrices, we have extracted the AT-hook motifs present in a non-redundant protein sequence database. (embl.de)
- We have classified these motifs into three types according to their sequence similarity and have found that they are prevalent in many eukaryotic nuclear proteins in single or multiple copies. (embl.de)
- The HMG family of proteins comprises members with multiple HMG domains that bind DNA with low sequence specificity, and members with single HMG domains that recognize specific nucleotide sequences. (embl.de)
- Kuznetsov 7 studies of sequence-Nonspecific HMGB DNA-Binding Proteins. (progressivetradinggroup.com)
- The miniF plasmid C protein: sequence, purification and DNA binding. (shengsci.com)
MRNA3
- Moreover, expression studies on mRNA and protein level showed upregulation of Fte-1/S3a in colon, lung and kidney carcinoma. (uni-frankfurt.de)
- The VEGF-A protein and mRNA levels in conditioned medium of RGC-5 cells incubated with AGE-modified BSA (AGE-BSA) were examined with real-time PCR and enzyme-linked immunosorbent assay (ELISA), and BSA-treated cells were used as controls. (molvis.org)
- Compared with the BSA controls, the RGC-5 cells incubated with AGE-BSA showed a dose- and time-dependent increase in VEGF-A mRNA and VEGF-A protein secretion in the supernatant, with the highest levels achieved at 24 h. (molvis.org)
Concentrations1
- MAP and ScvO2 significantly increased with CRRT, while CAI and concentrations of lactate, IL-6, and HMGB-1 significantly decreased. (longdom.org)
Stability2
- Ubiquitination is a multifunctional posttranslational modification controlling the activity, subcellular localization and stability of proteins. (cipsm.de)
- This degradation is mediated by at least two domains indicating the presence of at least two different pathways impinging on ICK1/KRP1 protein stability. (uni-bielefeld.de)
Regulators1
- Muscleblind-like proteins (MBNLs) are regulators of RNA metabolism. (shengsci.com)
Replication2
- The encoded protein also functions in mitochondrial DNA replication and repair. (nih.gov)
- Eukaryotic High-Mobility Group B (HMGB) proteins alter DNA elasticity while facilitating transcription, replication and DNA repair. (shengsci.com)
Alarmin1
- High mobility group box-1 protein (HMGB-1) is perhaps the most studied alarmin. (jneurosci.org)
Mammalian cells2
- 1997). The screen resulted in the identification of six proteins displaying cell death-inhibiting activity in S. pombe as well as anti-apoptotic potential in mammalian cells. (uni-frankfurt.de)
- Isolation of a protein target of the FKBP12-rapamycin complex in mammalian cells. (prolekarniky.cz)
Eukaryotic cells1
- This protein is abundantly expressed in nearly all eukaryotic cells [26]. (pkc-inhibitor.com)
Motif3
- In general, it appears that the AT-hook motif is an auxiliary protein motif cooperating with other DNA-binding activities and facilitating changes in the structure of the DNA either as a polypeptide on its own [e.g. (embl.de)
- It is most interesting that this motif seems to be quite specific to known or predicted chromosomal/DNA-binding proteins, suggesting that it may act as a versatile minor groove tether. (embl.de)
- Subunit of the heme-activated, glucose-repressed Hap2/3/4/5 CCAAT-binding complex - there should be a single motif for all four proteins, containing CCAAT. (utoronto.ca)
Receptor2
- CXCR4 is the receptor of CXCL12 chemokine protein: theese proteins create an axis which plays a relevant role in shaping the tumor microenvironment (TME), mainly against dampening immune responses. (hmgbiotech.eu)
- However, TM is a receptor of thrombin and protein C on the endothelial cell surface and regulates the coagulation and complement system [ 15 ]. (biomedcentral.com)
Cells3
- In type 1 diabetes, the lowered expression of adhesion proteins within the intestinal epithelium favours a greater immune response that may result in destruction of pancreatic β cells by CD8+ T-lymphocytes, and increased expression of interleukin-17, related to autoimmunity. (biomedcentral.com)
- The C protein has been purified from cells carrying the Ptrp-C plasmid, and a preliminary study of C protein-DNA binding properties has been carried out. (shengsci.com)
- Cells continuously monitor protein synthesis to prevent accumulation of aberrant polypeptides. (shengsci.com)
Adhesion1
- We have shown in this review that a large body of evidence suggests probiotics reduce the inflammatory response and oxidative stress, as well as increase the expression of adhesion proteins within the intestinal epithelium, reducing intestinal permeability. (biomedcentral.com)
Inflammation1
- HMGB-1 could play a significant role in periimplant inflammatory response and inflammation. (europeanreview.org)
Form heterodimers2
- This protein is thought to be involved in the repair of DNA mismatches, and it can form heterodimers with MLH1, a known DNA mismatch repair protein. (nih.gov)
- Rel frequently combines with other related proteins (NF-KAPPA B, I-kappa B, relA) to form heterodimers that regulate transcription. (bvsalud.org)
Binds1
- C protein binds strongly to pifO, and weakly to sequences in the ori-1 region. (shengsci.com)
Immune3
- The present results suggest that the CNS innate immune system can respond to an acute stressor as if it were cellular damage, thereby releasing the danger signal HMGB-1 in the brain to prime microglia by acting on the NLRP3 inflammasome, in preparation for a later immune challenge. (jneurosci.org)
- This observation lays the ground work for testing if improving membrane resealing could dampen the immune response to muscle proteins in myositis. (osu.edu)
- Inhibition of this protein may be an effective new treatment for patients with immune-inflammatory eye disease. (pkc-inhibitor.com)
Compartment1
- Proteotoxic stress promotes entrapment of ribosomes and misfolded proteins in a shared cytosolic compartment. (shengsci.com)
High mobility2
- Here, high mobility group box-1 (HMGB-1) protein was explored as a potential mediator of stress-induced microglial priming and whether HMGB-1 does so via the nucleotide-binding domain, leucine-rich repeat, pyrin domain containing protein 3 (NLRP3) inflammasome. (jneurosci.org)
- High mobility group box-1 (HMGB-1) proteins as important mediators in thrombus formation. (wikipedia.org)
Arabidopsis1
- Here we address the posttranslational regulation of INHIBITOR/INTERACTOR OF CDK 1 (ICK1)/KIP RELATED PROTEIN 1 ( KRP1), an Arabidopsis ( Arabidopsis thaliana) CDK inhibitor. (uni-bielefeld.de)