An AT-hook-containing (AT-HOOK MOTIFS) nuclear protein that is expressed predominantly in proliferating and undifferentiated mesenchymal cells.
An 11-kDa AT-hook motif-containing (AT-HOOK MOTIFS) protein that binds to the minor grove of AT-rich regions of DNA. It is the full-length product of the alternatively-spliced HMGA1 gene and may function as an architectural chromatin binding protein that is involved in transcriptional regulation.
An AT-hook motif-containing protein (AT-HOOK MOTIFS) that binds to the minor grove of AT-rich regions of DNA. It is a truncated form of HMGA1a protein that is produced by alternative-splicing of the HMGA1 gene. It may function as an architectural chromatin binding protein that is involved in transcriptional regulation.
DNA-binding motifs, first described in one of the HMGA PROTEINS: HMG-I(Y) PROTEIN. They consist of positively charged sequences of nine amino acids centered on the invariant tripeptide glycine-arginine-proline. They act to fasten the protein to an AT RICH SEQUENCE in the DNA.
An AT-hook-containing (AT-HOOK MOTIFS) nuclear protein that may be involved in retinoid-dependent transcriptional activity.
A benign tumor composed of fat cells (ADIPOCYTES). It can be surrounded by a thin layer of connective tissue (encapsulated), or diffuse without the capsule.
A mononuclear Fe(II)-dependent oxygenase, this enzyme catalyzes the conversion of homogentisate to 4-maleylacetoacetate, the third step in the pathway for the catabolism of TYROSINE. Deficiency in the enzyme causes ALKAPTONURIA, an autosomal recessive disorder, characterized by homogentisic aciduria, OCHRONOSIS and ARTHRITIS. This enzyme was formerly characterized as EC 1.13.1.5 and EC 1.99.2.5.
An HMG-box domain (HMG-BOX DOMAINS) found highly expressed in embryonic tissue and in placenta.

Specific binding of high-mobility-group I (HMGI) protein and histone H1 to the upstream AT-rich region of the murine beta interferon promoter: HMGI protein acts as a potential antirepressor of the promoter. (1/192)

The high-mobility-group I (HMGI) protein is a nonhistone component of active chromatin. In this work, we demonstrate that HMGI protein specifically binds to the AT-rich region of the murine beta interferon (IFN-beta) promoter localized upstream of the murine virus-responsive element (VRE). Contrary to what has been described for the human promoter, HMGI protein did not specifically bind to the VRE of the murine IFN-beta promoter. Stably transfected promoters carrying mutations on this HMGI binding site displayed delayed virus-induced kinetics of transcription. When integrated into chromatin, the mutated promoter remained repressed and never reached normal transcriptional activity. Such a phenomenon was not observed with transiently transfected promoters upon which chromatin was only partially reconstituted. Using UV footprinting, we show that the upstream AT-rich sequences of the murine IFN-beta promoter constitute a preferential binding region for histone H1. Transfection with a plasmid carrying scaffold attachment regions as well as incubation with distamycin led to the derepression of the IFN-beta promoter stably integrated into chromatin. In vitro, HMGI protein was able to displace histone H1 from the upstream AT-rich region of the wild-type promoter but not from the promoter carrying mutations on the upstream high-affinity HMGI binding site. Our results suggest that the binding of histone H1 to the upstream AT-rich region of the promoter might be partly responsible for the constitutive repression of the promoter. The displacement by HMGI protein of histone H1 could help to convert the IFN-beta promoter from a repressed to an active state.  (+info)

High mobility group-I(Y) protein facilitates nuclear factor-kappaB binding and transactivation of the inducible nitric-oxide synthase promoter/enhancer. (2/192)

Nitric oxide (NO), a free radical gas whose production is catalyzed by the enzyme NO synthase, participates in the regulation of multiple organ systems. The inducible isoform of NO synthase (iNOS) is transcriptionally up-regulated by inflammatory stimuli; a critical mediator of this process is nuclear factor (NF)-kappaB. Our objective was to determine which regulatory elements other than NF-kappaB binding sites are important for activation of the iNOS promoter/enhancer. We also wanted to identify transcription factors that may be functioning in conjunction with NF-kappaB (subunits p50 and p65) to drive iNOS transcription. Deletion analysis of the iNOS promoter/enhancer revealed that an AT-rich sequence (-61 to -54) downstream of the NF-kappaB site (-85 to -76) in the 5'-flanking sequence was important for iNOS induction by interleukin-1beta and endotoxin in vascular smooth muscle cells. This AT-rich sequence, corresponding to an octamer (Oct) binding site, bound the architectural transcription factor high mobility group (HMG)-I(Y) protein. Electrophoretic mobility shift assays showed that HMG-I(Y) and NF-kappaB subunit p50 bound to the iNOS promoter/enhancer to form a ternary complex. The formation of this complex required HMG-I(Y) binding at the Oct site. The location of an HMG-I(Y) binding site typically overlaps that of a recruited transcription factor. In the iNOS promoter/enhancer, however, HMG-I(Y) formed a complex with p50 while binding downstream of the NF-kappaB site. Furthermore, overexpression of HMG-I(Y) potentiated iNOS promoter/enhancer activity by p50 and p65 in transfection experiments, suggesting that HMG-I(Y) contributes to the transactivation of iNOS by NF-kappaB.  (+info)

The host-cell architectural protein HMG I(Y) modulates binding of herpes simplex virus type 1 ICP4 to its cognate promoter. (3/192)

The productive infection cycle of herpes simplex virus is controlled in part by the action of ICP4, an immediate-early gene product that acts as both an activator and repressor of transcription. ICP4 is autoregulatory, and IE-3, the gene that encodes it, contains a high-affinity binding site for the protein at its cap site. Previously, we had demonstrated that this site could be occupied by proteins found in nuclear extracts from uninfected cells. A HeLa cell cDNA expression library was screened with a DNA probe containing the IE-3 gene cap site, and clones expressing the architectural chromatin proteins HMG I and HMG Y were identified by this technique. HMG I is shown to augment binding of ICP4 to its cognate site in in vitro assays and to enhance the activity of this protein in short-term transient expression assays.  (+info)

Determination of high mobility group I(Y) expression level in colorectal neoplasias: a potential diagnostic marker. (4/192)

High mobility group I(Y) [HMGI(Y)] proteins are architectural factors abundantly expressed during embryogenesis, and their overexpression is known to be closely associated with neoplastic transformation of cells. This study was performed to investigate whether determination of HMGI(Y) expression level could assist in (a) differential diagnosis between colorectal carcinoma, adenoma, and normal tissue and (b) determination of the prognosis of patients with colorectal cancer. To this end, HMGI(Y) expression was determined at both the protein and mRNA levels in 30 colorectal carcinomas, 26 adenomas, and 23 normal mucosa samples, and further correlations between the protein expression levels and various clinicopathological parameters, such as depth of tumor invasion, lymphatic and/or venous involvement, regional lymph node metastasis, and Dukes' stage, were determined in 30 carcinoma cases. The expression of HMGI(Y) proteins was significantly increased in carcinoma and adenoma with severe atypia compared with that in adenoma with less atypia and normal colorectal mucosa. This increase in HMGI(Y) protein expression was found to be because of an increase in its mRNA expression by RNA in situ hybridization analysis. Clinicopathological analysis revealed that the level of HMGI(Y) protein expression was significantly correlated with parameters known to be indicative of a poor prognosis in colorectal cancer patients. These findings indicate that the determination of the HMGI(Y) protein expression level could be a potential marker for the diagnosis of colorectal neoplasias and can be of great value in predicting the prognosis of patients with colorectal cancer.  (+info)

Directional binding of HMG-I(Y) on four-way junction DNA and the molecular basis for competitive binding with HMG-1 and histone H1. (5/192)

Histone H1, HMG-1 and HMG-I(Y) are mammalian nuclear proteins possessing distinctive DNA-binding domain structures that share the common property of preferentially binding to four-way junction (4H) DNA, an in vitro mimic of the in vivo genetic recombination intermediate known as the Holliday junction. Nevertheless, these three proteins bind to 4H DNA in vitro with very different affinities and in a mutually exclusive manner. To investigate the molecular basis for these distinctive binding characteristics, we employed base pair resolution hydroxyl radical footprinting to determine the precise sites of nucleotide interactions of both HMG-1 and histone H1 on 4H DNA and compared these contacts with those previously described for HMG-I(Y) on the same substrate. Each of these proteins had a unique binding pattern on 4H DNA and yet shared certain common nucleotide contacts on the arms of the 4H DNA molecule near the branch point. Both the HMG-I(Y) and HMG-1 proteins made specific contacts across the 4H DNA branch point, as well as interacting at discrete sites on the arms, whereas the globular domain of histone H1 bound exclusively to the arms of the 4H DNA substrate without contacting nucleotides at the crossover region. Experiments employing the chemical cleavage reagent 1, 10-orthophenanthroline copper(II) attached to the C-terminal end of a site-specifically mutagenized HMG-I(Y) protein molecule demonstrated that this protein binds to 4H DNA in a distinctly polar, direction-specific manner. Together these results provide an attractive molecular explanation for the observed mutually exclusive 4H DNA-binding characteristics of these proteins and also allow for critical assessment of proposed models for their interaction with 4H DNA substrates. The results also have important implications concerning the possible in vivo roles of HMG-I(Y), histone H1 and HMG-1 in biological processes such as genetic recombination and retroviral integration.  (+info)

HMGI(Y) and HMGI-C genes are expressed in neuroblastoma cell lines and tumors and affect retinoic acid responsiveness. (6/192)

HMGI-C and HMGI(Y) are architectural DNA-binding proteins that participate in the conformational regulation of active chromatin. Their pattern of expression in embryonal and adult tissues, the analysis of the "pygmy" phenotype induced by the inactivation of the HMGI-C gene, and their frequent qualitative or quantitative alteration in experimental and human tumors indicate their pivotal role in the control of cell growth, differentiation, and tumorigenesis in several tissues representative of the epithelial, mesenchymal, and hematopoietic lineages. In contrast, very little information is available on their expression and function in neural cells. Here, we investigated the expression of the HMGI(Y) and HMGI-C genes in neuroblastoma (NB), a tumor arising from an alteration of the normal differentiation of neural crest-derived cells and in embryonal and adult adrenal tissue. Although HMGI(Y) is constitutively expressed in the embryonal and adult adrenal gland and in all of the NB cell lines and ex vivo tumors examined, its regulation appears to be associated to growth inhibition and differentiation because we observed that HMGI(Y) expression is reduced by retinoic acid (RA) in several NB cell lines that are induced to differentiate into postmitotic neurons, whereas it is up-regulated by RA in cells that fail to differentiate. Furthermore, the decrease of HMGI(Y) expression observed in RA-induced growth arrest and differentiation is abrogated in cells that have been made insensitive to this drug by NMYC overexpression. In contrast, HMGI-C expression is down-regulated during the development of the adrenal gland, completely absent in the adult individual, and only detectable in a subset of ex vivo NB tumors and in RA-resistant NB cell lines. We provide evidence of a causal link between HMGI-C expression and resistance to the growth arrest induced by RA in NB cell lines because exogenous HMGI-C expression in HMGI-C-negative and RA-sensitive cells is sufficient to convert them into RA-resistant cells. Therefore, we suggest that HMGI-C and HMGI(Y) may participate in growth- and differentiation-related tumor progression events of neuroectodermal derivatives.  (+info)

The HMG-I(Y) A.T-hook peptide motif confers DNA-binding specificity to a structured chimeric protein. (7/192)

Chromosomal translocations involving genes coding for members of the HMG-I(Y) family of "high mobility group" non-histone chromatin proteins (HMG-I, HMG-Y, and HMG-IC) have been observed in numerous types of human tumors. Many of these gene rearrangements result in the creation of chimeric proteins in which the DNA-binding domains of the HMG-I(Y) proteins, the so-called A.T-hook motifs, have been fused to heterologous peptide sequences. Although little is known about either the structure or biophysical properties of these naturally occurring fusion proteins, the suggestion has been made that such chimeras have probably assumed an altered in vivo DNA-binding specificity due to the presence of the A.T-hook motifs. To investigate this possibility, we performed in vitro "domain-swap" experiments using a model protein fusion system in which a single A. T-hook peptide was exchanged for a corresponding length peptide in the well characterized "B-box" DNA-binding domain of the HMG-1 non-histone chromatin protein. Here we report that chimeric A. T-hook/B-box hybrids exhibit in vitro DNA-binding characteristics resembling those of wild type HMG-I(Y) protein, rather than the HMG-1 protein. These results strongly suggest that the chimeric fusion proteins produced in human tumors as a result of HMG-I(Y) gene chromosomal translocations also retain A.T-hook-imparted DNA-binding properties in vivo.  (+info)

The role of HMG I(Y) in the assembly and function of the IFN-beta enhanceosome. (8/192)

Transcriptional activation of the virus inducible enhancer of the human interferon-beta (IFN-beta) gene in response to virus infection requires the assembly of an enhanceosome, consisting of the transcriptional activators NF-kappaB, ATF-2/c-Jun, IRFs and the architectural protein of the mammalian high mobility group I(Y) [HMG I(Y)]. Here, we demonstrate that the first step in enhanceosome assembly, i.e. HMG I(Y)-dependent recruitment of NF-kappaB and ATF-2/c-Jun to the enhancer, is facilitated by discrete regions of HMG I and is mediated by allosteric changes induced in the DNA by HMG I(Y) and not by protein-protein interactions between HMG I(Y) and these proteins. However, we show that completion of the enhanceosome assembly process requires protein-protein interactions between HMG I(Y) and the activators. Finally, we demonstrate that once assembled, the IFN-beta enhanceosome is an unusually stable nucleoprotein structure that can activate transcription at high levels by promoting multiple rounds of reinitiation of transcription.  (+info)

High Mobility Group AT-Hook 2 (HMGA2) protein is a non-histone chromatin protein that belongs to the HMGA family. This protein contains structural DNA-binding domains called AT-hooks, which allow it to bind to the minor groove of AT-rich sequences in the promoter or enhancer regions of genes.

HMGA2 protein plays a crucial role in regulating gene transcription, chromatin architecture, and nuclear organization during development and differentiation. It is involved in various cellular processes such as proliferation, apoptosis, and senescence. Moreover, HMGA2 has been implicated in several human diseases, including cancer, where its overexpression is often associated with poor prognosis and aggressive tumor behavior.

In summary, HMGA2 protein is a DNA-binding protein that regulates gene expression and is involved in development, differentiation, and disease, particularly cancer.

High Mobility Group AT-Hook 1 (HMGA1) is a non-histone chromosomal protein that belongs to the HMGA family. The HMGA proteins are characterized by their ability to bind to AT-rich regions in the minor groove of DNA and modulate the chromatin structure, thereby regulating gene transcription.

The HMGA1 protein exists in two isoforms, HMGA1a and HMGA1b, which differ in their amino acid sequences due to alternative splicing of the HMGA1 pre-mRNA. The HMGA1a isoform has 108 amino acids, while HMGA1b has 109 amino acids.

HMGA1 proteins play crucial roles in various cellular processes, including proliferation, differentiation, and apoptosis. Dysregulation of HMGA1 expression has been implicated in several human diseases, such as cancer, where it functions as a transcriptional regulator of genes involved in tumorigenesis.

High Mobility Group AT-Hook 1b (HMGA1b) protein is a subtype of the HMGA1 protein, which belongs to the High Mobility Group AT-hook (HMGA) family of non-histone chromatin proteins. These proteins are characterized by their ability to bind to the minor groove of AT-rich DNA sequences and modulate chromatin structure and gene expression.

The HMGA1 protein exists in two isoforms, HMGA1a and HMGA1b, which are generated through alternative splicing of the same gene. Both isoforms share a similar structure, consisting of three AT-hook DNA binding domains and a C-terminal acidic tail. However, they differ in their N-terminal regions, with HMGA1b having a unique 29-amino acid sequence that is not present in HMGA1a.

HMGA1 proteins play important roles in various cellular processes, including transcription regulation, DNA replication, and repair. Dysregulation of HMGA1 expression has been implicated in several human diseases, such as cancer, where it can act as a potent oncogene by promoting tumor cell proliferation, migration, and invasion.

AT-hook motifs are short DNA-binding domains that are found in many eukaryotic transcription factors and other proteins that interact with chromatin. These motifs are typically composed of 6-8 amino acid residues, characterized by the presence of a highly conserved tripeptide sequence (PWK, PWV, or PWY), which is responsible for their ability to bind to the minor groove of AT-rich DNA sequences.

The AT-hook motifs can bend and kink the DNA helix, leading to changes in chromatin structure and modulation of gene expression. They play important roles in various nuclear processes, including transcriptional regulation, DNA replication, and repair. The presence of multiple AT-hook motifs in a single protein can enhance its DNA-binding affinity and specificity, allowing it to interact with specific regulatory elements in the genome.

High Mobility Group AT-Hook 1 (HMGA1) is a protein that belongs to the non-histone chromosomal high mobility group (HMG) family. HMGA1 has been shown to play a role in the regulation of gene transcription by binding to DNA and modifying its structure, thereby influencing the interaction between DNA and other proteins involved in transcription.

The HMGA1 protein exists in several isoforms due to alternative splicing, one of which is HMGA1c. HMGA1c is a splicing variant of HMGA1 that contains an additional 39 amino acids at its C-terminus compared to other isoforms.

It's important to note that there seems to be some confusion in the literature regarding the definition and naming of HMGA1 isoforms, including HMGA1c. Therefore, it's crucial to consider the context and specific nomenclature used in each study when interpreting results related to this protein.

In summary, HMGA1c is a splicing variant of the HMGA1 protein that has an additional 39 amino acids at its C-terminus and plays a role in gene transcription regulation by binding to DNA and modifying its structure.

A lipoma is a common, benign (non-cancerous) soft tissue growth. It is composed of adipose or fatty tissue and typically found just beneath the skin, but they can also occur deeper within the body. Lipomas are usually round, moveable, and painless, although they may cause discomfort if they grow large enough to put pressure on nearby nerves or if they're located in a sensitive area. They generally grow slowly over time. Surgical removal is an option if the lipoma becomes bothersome or grows significantly in size. It's important to note that while lipomas are typically harmless, any new lumps or bumps should be evaluated by a healthcare professional to confirm the diagnosis and rule out other more serious conditions.

Homogentisate 1,2-dioxygenase (HGD) is an enzyme that plays a crucial role in the catabolism of tyrosine, an aromatic amino acid. This enzyme is involved in the third step of the tyrosine degradation pathway, also known as the tyrosine breakdown or catabolic pathway.

The homogentisate 1,2-dioxygenase enzyme catalyzes the conversion of homogentisic acid (HGA) into maleylacetoacetic acid. This reaction involves the cleavage of the aromatic ring of HGA and the introduction of oxygen, hence the name 'dioxygenase.' The reaction can be summarized as follows:

Homogentisate + O2 → Maleylacetoacetate

Deficiency or dysfunction in homogentisate 1,2-dioxygenase leads to a rare genetic disorder called alkaptonuria. In this condition, the body cannot break down tyrosine properly, resulting in an accumulation of HGA and its oxidation product, alkapton, which can cause damage to connective tissues and joints over time.

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.

HMGA proteins (HMGA1a, HMGA1b and HMGA2) are implicated in cancer, and expression of these proteins is regulated by microRNAs. ... binding protein], PACT (protein activator of the interferon-induced protein kinase), the SMN complex, fragile X mental ... HMGA2 protein specifically targets the promoter of ERCC1, thus reducing expression of this DNA repair gene. ERCC1 protein ... HMGA proteins are polypeptides of ~100 amino acid residues characterized by a modular sequence organization. These proteins ...
... show a strong increase of HMGA1a and HMGA1b proteins. Transgenic mice with HMGA1 targeted to lymphoid cells develop aggressive ... HMGA2 protein specifically targets the promoter of ERCC1, thus reducing expression of this DNA repair gene. ERCC1 protein ... HGMA proteins are polypeptides of ~100 amino acid residues characterized by a modular sequence organization. These proteins ... April 2003). "Negative regulation of BRCA1 gene expression by HMGA1 proteins accounts for the reduced BRCA1 protein levels in ...
Recently it has been shown that HMGA1 proteins, HMGA1a and HMGA1b, can cross-link DNA fibers in vitro and can induce chromatin ... High-mobility group protein HMG-I/HMG-Y is a protein that in humans is encoded by the HMGA1 gene. This gene encodes a non- ... HMGB and HMGN proteins. HMGA1-GFP fusion proteins are highly dynamic in vivo (determined using FRAP analysis), but in contrast ... "Functional interaction between the POU domain protein Tst-1/Oct-6 and the high-mobility-group protein HMG-I/Y". Molecular and ...
The protein appears to have important roles in neuronal development and mRNA transport. NFX1 is also a probable E3 ubiquitin- ... They mapped the interaction of HMGA1a and the paired homeodomain motif within Crx and showed that these interactions help ... "Eyelid protein is key to allergy". BBC News. January 16, 2005. Archived from the original on July 14, 2022. Retrieved April 1, ... This factor can bind DNA, RNA and protein via a reiterated RING finger motifs in the central domain of the polypeptide. ...
... hmga proteins MeSH D12.776.660.235.400.500.100 - hmga1a protein MeSH D12.776.660.235.400.500.200 - hmga1b protein MeSH D12.776. ... hmgb2 protein MeSH D12.776.660.235.400.600.800 - hmgb3 protein MeSH D12.776.660.235.400.700 - sex-determining region y protein ... hmga2 protein MeSH D12.776.660.235.400.600 - hmgb proteins MeSH D12.776.660.235.400.600.300 - hmgb1 protein MeSH D12.776. ... MeSH D12.776.660.235.400.400 - hmgn proteins MeSH D12.776.660.235.400.400.200 - hmgn1 protein MeSH D12.776.660.235.400.400.300 ...
Bell SD (2012). "Archaeal Orc1/Cdc6 Proteins". The Eukaryotic Replisome: A Guide to Protein Structure and Function. Subcellular ... February 2008). "Interaction between HMGA1a and the origin recognition complex creates site-specific replication origins". ... Additionally, the WhiP protein, an initiator unrelated to Orc1/Cdc6, has been shown to bind all origins as well and to drive ... A variety of proteins have been described as being involved in viral replication. For instance, Polyoma viruses utilize host ...
... hmga proteins MeSH D12.776.664.235.400.500.100 - hmga1a protein MeSH D12.776.664.235.400.500.200 - hmga1b protein MeSH D12.776. ... groel protein MeSH D12.776.602.500.500.100 - fusion proteins, bcr-abl MeSH D12.776.602.500.500.320 - fusion proteins, gag-onc ... oncogene protein v-maf MeSH D12.776.964.700.750.875 - oncogene proteins v-abl MeSH D12.776.964.700.750.882 - oncogene proteins ... fusion proteins, gag-pol MeSH D12.776.964.775.350.400 - hiv core protein p24 MeSH D12.776.964.775.375.325 - fusion proteins, ...
HMGA1a Protein * Receptor, Insulin Grants and funding * 064890/WT_/Wellcome Trust/United Kingdom ...
HMGA proteins (HMGA1a, HMGA1b and HMGA2) are implicated in cancer, and expression of these proteins is regulated by microRNAs. ... binding protein], PACT (protein activator of the interferon-induced protein kinase), the SMN complex, fragile X mental ... HMGA2 protein specifically targets the promoter of ERCC1, thus reducing expression of this DNA repair gene. ERCC1 protein ... HMGA proteins are polypeptides of ~100 amino acid residues characterized by a modular sequence organization. These proteins ...
Proteins [D12.776] * DNA-Binding Proteins [D12.776.260] * HMGA Proteins [D12.776.260.312] * HMGA1a Protein [D12.776.260.312.500 ... HMGA Proteins [D12.776.660.235.400.500] * HMGA1a Protein [D12.776.660.235.400.500.100] * HMGA1b Protein [D12.776.660.235. ... HMGA Proteins [D12.776.664.235.400.500] * HMGA1a Protein [D12.776.664.235.400.500.100] * HMGA1b Protein [D12.776.664.235. ... HMG I-Type Protein HMG I-Y Phosphoprotein HMG-I(Y) Protein HMGI Protein HMGI(Y) Gene Product High Mobility Group I(Y) Protein ...
The Chromatin Regulator HMGA1a Undergoes Phase Separation in the Nucleus**. Zhu, H., Narita, M., Joseph, J. A., Krainer, G., ... Aromatic and arginine content drives multiphasic condensation of protein-RNA mixtures. Chew, P. Y., Joseph, J. A., Collepardo- ... Thermodynamic origins of two-component multiphase condensates of proteins. Chew, P. Y., Joseph, J. A., Collepardo-Guevara, R. ... Physical determinants of multiphase organisation in multi-component protein/RNA condensates. Chew, P. Y., Joseph, J. A., ...
Protein arginine methyltransferase 5 (PRMT5) targets nuclear and cytoplasmic proteins. Here, we identified a nuclear protein, ... and to provide evidences for a modulatory role of HMGA1a on the methyltransferase activity of PRMT6. ... The mechanism underlying the protein-protein interaction of hnRNP K and PRMT family proteins is unclear. We examined and ... These results suggest that protein arginine methylation can selectively modulate certain protein-protein interactions and that ...
HMGA1a Protein. *Humans. *Immune Tolerance. *Immunocompromised Host. *Immunoglobulin G. *Immunoglobulin M. *Immunologic Factors ...
HMGA Proteins N0000169231 HMGA1a Protein N0000169233 HMGA1b Protein N0000169232 HMGA1c Protein N0000169234 HMGA2 Protein .... ... ADAMTS Proteins ADAMTS1 Protein ADAMTS13 Protein ADAMTS4 Protein ADAMTS5 Protein ADAMTS7 Protein ADAMTS9 Protein Adansonia ... ... ELAV Proteins ELAV-Like Protein 1 ELAV-Like Protein 2 ELAV-Like Protein 3 ELAV-Like Protein 4 Elbow Elbow Joint Elbow ... ... Adaptor Protein Complex 1 Adaptor Protein Complex 2 Adaptor Protein Complex 3 Adaptor Protein Complex 4 Adaptor Protein Complex ...
Though there exists no protein with homology to PrPc in yeast, numerous yeast proteins have now been shown to exist both in a ... This supports that HMGA1a down regulation is important to activate the whole myo genic system which include chromatin ... These different states from the same protein induce distinct phenotypes. On top of that, every prion protein can usually type ... selleck chemicals Discussion HMGA1 proteins are architectural chromatin proteins regarded to be preferentially expressed in ...
These information illustrate that a sustained large HMGA1a protein level after induction of myogenesis alters the expression of ... Igf binding proteins 1, 2, and 3 even more fine tune the bioavailability of Igf1 and Igf2. RT PCR analyses unveiled that Igf1, ... HMGA1a in excess of expression deregulates myogenic gene expression To examine no matter whether the impaired myogenesis of ... Therefore, HMGA1a above expression elevates the expression of MeCP2 but additionally counteracts its cap ability to bring about ...
The HMGA2 gene encodes for the HMGA2 protein, member of the HMGA family. This family of four proteins (HMGA1a, HMGA1b, HMGA1c ... HMGA2 gene encodes for the HMGA2 protein, member of the "high-mobility group AT-hook" (HMGA) family. These proteins act as ... The expression of HMGA proteins is high in early developmental stages in embryos and mesenchymal stem cells, whilst it is ... The HMGA proteins: a myriad of functions (review). Int J Oncol. 2008;32(2):289-305. ...
... we demonstrate that phase separation of HMGA1a is promoted by protein-DNA interactions, and has the potential to be modulated ... We find that for a constant nucleotide/protein ratio, the protein fused in sarcoma (FUS), which can phase separate on its own-i ... We compare the behavior of three different protein condensates, i.e., those formed by either hnRNPA1, FUS, or TDP-43 proteins, ... Protein structural transitions critically transform the network connectivity and viscoelasticity of RNA-binding protein ...
proteins and mRNA had been elevated in the cells transduced using the HMGA1a lentivirus as proven by quantitative, change ... encodes the HMGA1a and HMGA1b proteins isoforms that derive from additionally spliced RNA and differ by an interior 11 proteins ... HMGA protein are AT-hook protein that bind towards the minimal groove of DNA at AT wealthy locations (11C13, 33C35), recruit ... E. HMGA1 proteins amounts in HPNE-K-RASCHMGA1 (HMGA1) cells set alongside the Pexacerfont HPNE-K-RAS-GFP (control) cells and ...
Other site-specific PTMs of HMGA proteins, such as acetylation of K60 of HMGA1b [50] and methylation of R25 of HMGA1a [146-148 ... of the total population of cellular HMGA proteins [41]. Since phosphorylation of HMGA proteins significantly reduces their ... Hypo-phosphorylated HMGA proteins, on the other hand, have an increased overall positive change that facilitates tighter DNA ... Once apoptosis has been initiated the HMGA proteins themselves undergo marked changes in both the types and extent of their ...
Proteins containing AT-HOOK MOTIFS that are rich in arginine and glycine residues. They bind to the minor grove of AT-rich ... "HMGA Proteins" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical Subject ... This graph shows the total number of publications written about "HMGA Proteins" by people in this website by year, and whether ... Below are the most recent publications written about "HMGA Proteins" by people in Profiles. ...
Protein Diagram. Primary Papers. * Levy-Lahad E, Wasco W, Poorkaj P, Romano DM, Oshima J, Pettingell WH, Yu CE, Jondro PD, ... The position is not within an established binding site for HMGA1A, which can promote exon 6 skipping. ... Expected Protein Consequence: Deletion; Missense Codon Change: AAC to ATC Reference Isoform: PSEN2 Isoform 1 (448 aa) Genomic ...
PPFIA binding protein 1. 12p12.1. CV:GWASdb. CV:PGCnp. PROTEIN CLUSTERING. 2120. ETV6. TEL , TEL/ABL , THC5. ETS variant 6. ... HMG-R , HMGA1A , HMGIY. high mobility group AT-hook 1. 6p21. CV:GWASdb. CV:PGCnp. DMG:Jaffe_2016. GSMA_I. GSMA_IIE. ... thioredoxin related transmembrane protein 1. 14q22.1. CV:PGCnp. 5583. PRKCH. PKC-L , PKCL , PRKCL , nPKC-eta. protein kinase C ... ribosomal protein S6 kinase B2. 11q13.2. DMG:Jaffe_2016. 8500. PPFIA1. LIP.1 , LIP1 , LIPRIN. PTPRF interacting protein alpha 1 ...
PPI (protein-protein interaction) results are shown above.. *Green is ENSDARG00000078075 (ilrun), yellow represents other genes ... hmga1a. 23: 3751451 ~ 3759692 (-). ENSDARG00000062293. qpctlb. 21: 21325500 ~ 21336437 (+). ENSDARG00000074111. bcdin3d. 22: ...
Inhibition of protein kinase C, p34-kinase or histone deacetylases increases HMGA1a mobility in heterochromatin. HMGA1 proteins ... HMGA1a-GFP proteins are enriched in heterochromatin in vivo. During interphase, HMGA1-GFP proteins were distributed throughout ... A) Distribution of HMGA1a-GFP fusion proteins in transfected cells. (a) Distribution of HMGA1a-GFP in living cells as revealed ... A) Distribution of HMGA1a-GFP fusion proteins in transfected cells. (a) Distribution of HMGA1a-GFP in living cells as revealed ...
HMGA1a Protein / genetics* Actions. * Search in PubMed * Search in MeSH * Add to Search ...
Homeodomain-interacting protein kinase-2 (HIPK2) phosphorylates HMGA1a at Ser-35, Thr-52, and Thr-77 and modulates its DNA ... Dynamic and differential in vivo modifications of the isoform HMGA1a and HMGA1b chromatin proteins.. Edberg DD; Adkins JN; ... 6. HMGA1/HMGA2 protein expression and prognostic implications in gastric cancer.. Jun KH; Jung JH; Choi HJ; Shin EY; Chin HM. ... HMGA1 and HMGA2 protein expression in mouse spermatogenesis.. Chieffi P; Battista S; Barchi M; Di Agostino S; Pierantoni GM; ...
Dynamic interaction of HMGA1a proteins with chromatin. J. Cell Sci.. 117. :. 3459 ... The dynamic exchange of chromatin proteins makes the prediction that a soluble unbound pool of the exchanging protein must ... other DNA-binding proteins, including GFP-fusion of topoisomerase II, HMGA1, HMGB1, B2, and RCC1 proteins, also show exchanges ... Condensed mitotic chromatin is accessible to transcription factors and chromatin structural proteins Danyang Chen, Danyang Chen ...
title = "The Chromatin Regulator HMGA1a Undergoes Phase Separation in the Nucleus**",. abstract = "The protein high mobility ... we demonstrate that phase separation of HMGA1a is promoted by protein-DNA interactions, and has the potential to be modulated ... we demonstrate that phase separation of HMGA1a is promoted by protein-DNA interactions, and has the potential to be modulated ... we demonstrate that phase separation of HMGA1a is promoted by protein-DNA interactions, and has the potential to be modulated ...
HMGA1a Protein Entry term(s). AT Hook 1a Protein, High Mobility Group AT-Hook 1a Protein, High Mobility Group HMG I Type ... HMG I-Type Protein HMG I-Y Phosphoprotein HMG-I(Y) Protein HMGI Protein HMGI(Y) Gene Product High Mobility Group I(Y) Protein ... HMG I Type Protein. HMG I Y Phosphoprotein. HMG I-Type Protein. HMG I-Y Phosphoprotein. HMG-I(Y) Protein. HMGI Protein. HMGI(Y ... HMGA1a Protein - Preferred Concept UI. M0375723. Scope note. An 11-kDa AT-hook motif-containing (AT-HOOK MOTIFS) protein that ...
These include TATA-box-binding protein, integration host factor (IHF), high mobility group I(Y)[HMG I(Y)], and the HMG-box- ... containing proteins SRY and LEF-1. Each of th … ... have been solved for five different architectural proteins ... HMGA1a Protein Actions. * Search in PubMed * Search in MeSH * Add to Search ... Minor groove-binding architectural proteins: structure, function, and DNA recognition C A Bewley 1 , A M Gronenborn, G M Clore ...
Proteins [D12.776] * DNA-Binding Proteins [D12.776.260] * HMGA Proteins [D12.776.260.312] * HMGA1a Protein [D12.776.260.312.500 ... HMGA Proteins [D12.776.660.235.400.500] * HMGA1a Protein [D12.776.660.235.400.500.100] * HMGA1b Protein [D12.776.660.235. ... HMGA Proteins [D12.776.664.235.400.500] * HMGA1a Protein [D12.776.664.235.400.500.100] * HMGA1b Protein [D12.776.664.235. ... HMG I-Type Protein HMG I-Y Phosphoprotein HMG-I(Y) Protein HMGI Protein HMGI(Y) Gene Product High Mobility Group I(Y) Protein ...
HMGA1a Protein, 124544-67-8; Neoplasm Proteins; Nuclear Proteins; Nupr1 protein, mouse; P8 protein, human; PAX2 protein, human ... DNA binding protein; glucagon; Pax2 transactivation domain interacting protein; protein p300; protein p8; recombinant protein; ... DNA-Binding Proteins; E1A-Associated p300 Protein; Glucagon; Growth Substances; Hela Cells; Histidine; HMGA1a Protein; Humans; ... Basic Helix-Loop-Helix Transcription Factors; Carrier Proteins; DNA-Binding Proteins; E1A-Associated p300 Protein, EC 2.3.1.48 ...
Using a stratagem chemical cross-linker, we covalently bonded the HMGA receptor to the HMGA1a-GFP fusion protein, thus ... Cell viability assays also suggested that extracellular HMGA1a protein directly influences the survival ability of Hela cells ... Indeed, dyes or nanoparticles labeled with HMGA1a protein readily enter Hela cells. ... in which the internalized HMGA1a-decorated species are transported by motor proteins on microtubules and eventually arrive at ...
... is a critical downstream target of HMGA1a. STAT3 mRNA and protein are up-regulated in fibroblasts overexpressing HMGA1a and ... HMGA1 encodes the HMGA1a and HMGA1b protein isoforms, which function in regulating gene expression. To determine how HMGA1 ... HMGA1a also binds directly to a conserved region of the STAT3 promoter in vivo in human leukemia cells by chromatin ... Our results show that the HMGA1a-STAT3 axis is a potential Achilles heel that could be exploited therapeutically in ...
... the shorter isoform of HMGA1 proteins), and HMGA2. HMGA1a isoform turned out not to be efficiently produced as a GST-fusion ... the shorter isoform of HMGA1 proteins), and HMGA2. HMGA1a isoform turned out not to be efficiently produced as a GST-fusion ... and 1 protein (RNA binding protein NOB1) resulted to specifically interact only with HMGA2. To further validate our screening, ... and 1 protein (RNA binding protein NOB1) resulted to specifically interact only with HMGA2. To further validate our screening, ...
High mobility group protein A1, High mobility group protein R , HMGA1, HMGIY, HMG-R, HMGA1A. ... Home Page > RECOMBINANT PROTEIN > Recombinant Proteins > High Mobility Group AT-Hook 1 Human Recombinant High Mobility Group AT ... High mobility group protein HMG-I/HMG-Y, HMG-I(Y), High mobility group AT-hook protein 1, ... HMGA1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50% glycerol and 0.2M NaCl. Greater than ...
The encoded protein preferentially binds to the minor groove of AT-rich regions in double-stranded DNA. Multiple transcript ... This gene encodes a chromatin-associated protein involved in the regulation of gene transcription, integration of retroviruses ... It is suggested that these proteins could function in nucleosome phasing and in the 3-end processing of mRNA transcripts. They ... High Mobility Group Protein Hmg-i/hmg-y. DTO Classes. Protein. / Nucleic Acid Binding. / Dna Binding Protein. / High Mobility ...
By real-time quantitative RT-PCR; we measured HMGA1a mRNA in cultured pancreatic ductal adenocarcinoma cell lines and found ... The high-mobility group A1 (HMGA1) protein is an architectural transcription factor that has been implicated in the ...
Protein arginine methyltransferase 6 specifically methylates the nonhistone chromatin protein HMGA1a. Biochem Biophys Res ... Identification of methylated proteins in the yeast small ribosomal subunit: a role for SPOUT methyltransferases in protein ... Human Protein-l-isoaspartate O-Methyltransferase Domain-Containing Protein 1 (PCMTD1) Associates with Cullin-RING Ligase ... Integrated proteomic analysis of major isoaspartyl-containing proteins in the urine of wild type and protein L-isoaspartate O- ...
ribosomal protein L26. 17p13. CV:PGCnp. DMG:Nishioka_2013. 7157. TP53. BCC7 , LFS1 , P53 , TRP53. tumor protein p53. 17p13.1. ... HMG-R , HMGA1A , HMGIY. high mobility group AT-hook 1. 6p21. CV:GWASdb. CV:PGCnp. DMG:Jaffe_2016. GSMA_I. GSMA_IIE. ... BCL2-associated X protein. 19q13.3-q13.4. GO_Annotation. PMID:cooccur. 6193. RPS5. S5. ribosomal protein S5. 19q13.4. CV:PGCnp ... ELAV like RNA binding protein 1. 19p13.2. CV:PGCnp. 6217. RPS16. S16. ribosomal protein S16. 19q13.1. CV:PGCnp. DMG:Jaffe_2016 ...
HMGA Proteins N0000169231 HMGA1a Protein N0000169233 HMGA1b Protein N0000169232 HMGA1c Protein N0000169234 HMGA2 Protein ... N0000169241 HMGB3 Protein N0000169206 HMGN Proteins N0000169207 HMGN1 Protein N0000169208 HMGN2 Protein N0000171143 HN Protein ... N0000170951 Wnt Proteins N0000170952 Wnt1 Protein N0000170953 Wnt2 Protein N0000183504 Wnt3 Protein N0000183484 Wnt3A Protein ... Protein Precursors N0000170932 Protein S N0000170621 Protein Sorting Signals N0000169154 Protein Subunits N0000178699 Protein ...
... for HMG I-C PROTEIN use HMGA1A PROTEIN (NM) 1993-2001; for HMGI-C PROTEIN use HMGA2 PROTEIN (NM) 1992-2001 BX - HMG I-C Protein ... HN - 2002; for HMG I-TYPE PROTEIN use HMGA1A PROTEIN (NM) 1993-2001 BX - HMG I-Type Protein MH - HMGA1b Protein UI - D025742 MN ... HN - 2002; for ONCOGENE PROTEIN MIL use ONCOGENE PROTEINS V-RAF (NM) 1986-2001 BX - Oncogene Proteins v-mil BX - v-mil Protein ... HN - 2002; for HMG 14 PROTEIN use HIGH MOBILITY GROUP PROTEINS 1985-2001 BX - HMG 14 Protein MH - HMGN2 Protein UI - D024242 MN ...
  • It is the full-length product of the alternatively-spliced HMGA1 gene and may function as an architectural chromatin binding protein that is involved in transcriptional regulation. (nih.gov)
  • Five friends of methylated chromatin target of protein-arginine-methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation to desumoylation. (embl.de)
  • Chromatin target of Prmt1 (Chtop) is a vertebrate-specific chromatin-bound protein that plays an important role in transcriptional regulation. (embl.de)
  • HMGA chromatin binding proteins get excited about diverse biological procedures by virtue of their capability to regulate gene appearance (11C33). (eyesoftheelephants.com)
  • Since phosphorylation of HMGA proteins significantly reduces their binding affinity for A/T-rich DNA [109,136], hyper-phosphorylation likely results in partial displacement of HMGA proteins from DNA and the formation of a less condensed chromatin structure that is more easily digested by nucleases. (mg132.com)
  • Hypo-phosphorylated HMGA proteins, on the other hand, have an increased overall positive change that facilitates tighter DNA binding, chromatin condensation and placement of HMGA:DNA complexes into apoptotic bodies [41]. (mg132.com)
  • The expression of HMGA proteins is high in early developmental stages in embryos and mesenchymal stem cells, whilst it is almost absent or very low in adult tissues. (biomedcentral.com)
  • For example, the early stages of apoptosis are first accompanied by a global hyper-phosphorylation, which is quickly followed by a massive de-phosphorylation, of the total population of cellular HMGA proteins [41]. (mg132.com)
  • Other site-specific PTMs of HMGA proteins, such as acetylation of K60 of HMGA1b [50] and methylation of R25 of HMGA1a [146-148], have also been reported to occur during apoptosis but the function(s) of such modifications in the death process is unknown. (mg132.com)
  • In contrast to induction of apoptosis in normal cells, overexpression of HMGA proteins in some "pre-disposed" normal cells, as well as in immortalized cell lines that have already breached the senescence barrier, often has anti-apoptotic affects [85-87] and frequently induces overt cancerous transformation [34,72,168,169]. (mg132.com)
  • HMGA proteins have recently been directly implicated in the process of senescence, or aging, of normal cells. (mg132.com)
  • HMGA Proteins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (uchicago.edu)
  • This graph shows the total number of publications written about "HMGA Proteins" by people in this website by year, and whether "HMGA Proteins" was a major or minor topic of these publications. (uchicago.edu)
  • Below are the most recent publications written about "HMGA Proteins" by people in Profiles. (uchicago.edu)
  • HMGA2 gene encodes for the HMGA2 protein, member of the "high-mobility group AT-hook" (HMGA) family. (biomedcentral.com)
  • We lately reported high degrees of (gene encodes the HMGA1a and HMGA1b proteins isoforms that derive from additionally spliced RNA and differ by an interior 11 proteins, present just in the HMGA1a isoform (11C13), while HMGA2 is certainly encoded by another gene (13, 16, 24, 27, 32C33). (eyesoftheelephants.com)
  • And, importantly for the present discussion, SAHFs are depleted in linker histone H1 and enriched for HMGA1 and HMGA2, proteins which have been demonstrated to be essential components of these heterochromatin structures [56,107,176]. (mg132.com)
  • These proteins act as architectural transcription factors that regulate the trascriptional activity of several genes. (biomedcentral.com)
  • Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus. (lookformedical.com)
  • An 11-kDa AT-hook motif-containing ( AT-HOOK MOTIFS ) protein that binds to the minor grove of AT-rich regions of DNA . (nih.gov)
  • Proteins containing AT-HOOK MOTIFS that are rich in arginine and glycine residues. (uchicago.edu)
  • Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process. (lookformedical.com)
  • miRNAs base-pair to complementary sequences in mRNA molecules, then gene silence said mRNA molecules by one or more of the following processes: Cleavage of mRNA strand into two pieces, Destabilization of mRNA by shortening its poly(A) tail, or Translation of mRNA into proteins. (wikipedia.org)
  • Transcriptional regulation of the human ferritin gene by coordinated regulation of Nrf2 and protein arginine methyltransferases PRMT1 and PRMT4. (embl.de)
  • Mutations in the gene for the antennapedia homeodomain protein are associated with the conversion of antenna to leg or leg to antenna DROSOPHILA. (lookformedical.com)
  • Homeodomain proteins are involved in the control of gene expression during morphogenesis and development (GENE EXPRESSION REGULATION, DEVELOPMENTAL). (lookformedical.com)
  • HMGA protein are AT-hook protein that bind towards the minimal groove of DNA at AT wealthy locations (11C13, 33C35), recruit extra transcription elements, and in collaboration with these elements, alter gene appearance (11). (eyesoftheelephants.com)
  • isolated the lin-4 miRNA, they found that instead of producing an mRNA encoding a protein, it produced short non-coding RNAs, one of which was a ~22-nucleotide RNA that contained sequences partially complementary to multiple sequences in the 3' UTR of the lin-14 mRNA. (wikipedia.org)
  • This complementarity was proposed to inhibit the translation of the lin-14 mRNA into the LIN-14 protein. (wikipedia.org)
  • proteins and mRNA had been elevated in the cells transduced using the HMGA1a lentivirus as proven by quantitative, change transcriptase real-time PCR (qRT-PCR) and Traditional western evaluation (Fig. 1A). (eyesoftheelephants.com)
  • The assembly of PRMT6 protein network allowed us to formulate functional hypotheses which led to the discovery of new molecular partners for the architectural transcription factor HMGA1a, a known substrate for PRMT6, and to provide evidences for a modulatory role of HMGA1a on the methyltransferase activity of PRMT6. (embl.de)
  • To test our hypothesis that histone H4R3 and H3R17 methylation regulates ferritin transcription, H4R3 and H3R17 protein arginine (R) methyltransferases 1 and 4 (PRMT1 and PRMT4) were investigated. (embl.de)
  • We describe the residue-specific methylation of E2F-1 by the asymmetric dimethylating protein arginine methyltransferase 1 (PRMT1) and symmetric dimethylating PRMT5 and relate the marks to different functional consequences of E2F-1 activity. (embl.de)
  • The Tudor domain protein p100-TSN reads the symmetric methylation mark, and binding of p100-TSN downregulates E2F-1 apoptotic activity. (embl.de)
  • In this study, we demonstrate that formation and regulation of PRC1 condensates are consistent with the scaffold-client model, where the Chromobox 2 (CBX2) protein behaves as the scaffold while the other PRC1 proteins are clients. (bvsalud.org)
  • Identification and characterization of new molecular partners for the protein arginine methyltransferase 6 (PRMT6). (embl.de)
  • PRMT6 is a protein arginine methyltransferase that has been implicated in transcriptional regulation, DNA repair, and human immunodeficiency virus pathogenesis. (embl.de)
  • Proteins encoded by homeobox genes (GENES, HOMEOBOX) that exhibit structural similarity to certain prokaryotic and eukaryotic DNA-binding proteins. (lookformedical.com)
  • The proteins encoded by homeobox genes are called HOMEODOMAIN PROTEINS. (lookformedical.com)
  • Proteins which bind to DNA. (lookformedical.com)
  • The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases. (lookformedical.com)
  • We propose that sorbitol is a mechanosensitive metabolite enabling protein condensation to control mechano-regulated cellular functions. (bvsalud.org)
  • Proteins that originate from insect species belonging to the genus DROSOPHILA. (lookformedical.com)
  • The proteins from the most intensely studied species of Drosophila, DROSOPHILA MELANOGASTER, are the subject of much interest in the area of MORPHOGENESIS and development. (lookformedical.com)
  • The Bcl-2 homology 3 (BH3) domain is crucial for the death-inducing and dimerization properties of pro-apoptotic members of the Bcl-2 protein family, including Bak, Bax, and Bad. (lookformedical.com)
  • SAHFs also contain heterochromatin protein 1 (HP1) and the transcriptionally repressive histone variant macroH2A [56,106,176]. (mg132.com)
  • This network included the abundant pattern recognition proteins, signal transduction compo nents involved with Toll, Imd and JAK/STAT pathways, modulation molecules in proPO activating cascade and immune responsive effectors. (cox2-inhibitors.com)
  • The Traditional western blot displays Pexacerfont the elevated HMGA1 proteins in the HPNE-K-RAS-HMGA1 cells (denoted HMGA1) set alongside the control HPNE-K-RAS cells (denoted control). (eyesoftheelephants.com)
  • Phase separation plays an important role in the formation of membraneless compartments within the cell and intrinsically disordered proteins with low-complexity sequences can drive this compartmentalisation. (bvsalud.org)
  • PPI (protein-protein interaction) results are shown above. (ihb.ac.cn)
  • Several other genetic backgrounds result in enlargement of the haltere significantly beyond the normal range of haploinsufficient phenotypes, suggesting genetic variation in cofactors that mediate homeotic protein function. (lookformedical.com)