The developmentally regulated architectural transcription factor, high mobility group A2 (HMGA2), is involved in growth regulation and plays an important role in embryogenesis and tumorigenesis. Little is known, however, about its downstream targets. We performed a search for genes of which expressi …
Transcription factor high‐mobility group box‐containing protein 1 (HBP1) may function as a tumor suppressor in various types of cancer. In a previous study, we ...
This gene encodes a non-histone chromatin protein involved in many cellular processes, including regulation of inducible gene transcription, DNA replication, heterochromatin organization, integration of retroviruses into chromosomes, and the metastatic progression of cancer cells. HMGA1 proteins are quite small (~10-12 kDa) and basic molecules, and consist of three AT-hooks with the RGRP (Arg-Gly-Arg-Pro) core motif, a novel cross-linking domain located between the second and third AT-hook, and a C-terminal acidic tail characteristic for the HMG family comprising HMGA, HMGB and HMGN proteins. HMGA1-GFP fusion proteins are highly dynamic in vivo (determined using FRAP analysis), but in contrast also show nanomolar affinity to AT-rich DNA in vitro (determined biochemically), which might be explained due to the extensive post-transcriptional modifications in vivo. HMGA1 preferentially binds to the minor groove of AT-rich regions in double-stranded DNA using its AT-hooks. It has little secondary ...
In this article, we show that c-Jun binds to the HMG-I/Y promoter and induces expression of the HMG-I/Y chromatin binding protein. Decreasing HMG-I/Y proteins using an antisense approach inhibits c-Jun/AP-1-induced transformation, while overexpression of HMG-I/Y confers anchorage-independent cell growth. The colonies in Rat1a cells overexpressing HMG-I/Y were smaller and fewer, suggesting that HMG-I/Y expression only partially recapitulates the c-Jun/AP-1 phenotype. HMG-I/Y is a chromatin remodeling protein with DNA binding domains called AT hooks, which bind to the minor groove of stretches of AT-rich DNA (13-21, 26). Several studies suggest an important role for HMG-I/Y in regulating gene transcription (13-26, 42-44). The HMG-I/Y gene is highly conserved among species; the transcribed regions of the human and mouse HMG-I/Y genes are ∼80% identical at the nucleotide sequence level and ,90% identical when only the protein-coding exons are considered (48). Both mouse and human HMG-I/Y promoters ...
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HMGI(Y) is expressed in embryonic tissues and is usually down-regulated in mature adult cells. In contrast, HMGI(Y) is re-expressed in various cancer cells of human and animal tumors (23) and has been proposed to be associated with the more aggressive and metastatic features of many cancers (18 , 24, 25, 26) . Transfections of HMGI(Y) into the nonmalignant fibroblast has been reported to transform it and to increase its metastatic potential (22) . In human prostate cancer, increased expression of HMGI(Y) has been associated with higher Gleason grades (26) that reflect more aggressive pathology. Metastatic lesions in prostate cancer are usually associated with higher chromosomal instability (27) .. Other HMG proteins, not related to HMGI(Y) and expressed from other genes, such as HMG1 and HMG2, have been implicated in recombinations within the same chromosome producing the DNA rearrangements of the genes associated with immunoglobulin diversity at the V(D)J junction (28) . Recombination ...
TY - JOUR. T1 - Expression of the High Mobility Group Proteins HMGI(Y) Correlates with Malignant Progression in Barretts Metaplasia. AU - Chen, Xueyun. AU - Lechago, Juan. AU - Ertan, Atilla. AU - Ergun, Gulchin A.. AU - Verm, Ray. AU - Bridges, Margaret. AU - Johnson, Craig. AU - Woods, Karen. AU - Meriano, Frank V.. AU - Chirala, Minni. AU - Younes, Mamoun. PY - 2004/1. Y1 - 2004/1. N2 - Expression of the high mobility group proteins HMGI(Y) has been shown to be a marker of malignancy in thyroid and pancreatic lesions and to correlate significantly with malignant progression in the colon. The aim of this study was to determine whether HMGI(Y) expression is associated with malignant progression in Barretts metaplasia (BM). Immunoperoxidase staining for HMGI(Y) was performed on sections of formalin-fixed paraffin-embedded endoscopic esophageal biopsies from 42 patients with BM. These consisted of 19 biopsies negative for dysplasia (ND), 16 with low-grade dysplasia (LGD)/indeterminate for ...
TY - JOUR. T1 - Increase in AP-1 activity is a general event in thyroid cell transformation in vitro and in vivo. AU - Battista, Sabrina. AU - De Nigris, Filomena. AU - Fedele, Monica. AU - Chiappetta, Gennaro. AU - Scala, Stefania. AU - Vallone, Daniela. AU - Pierantoni, Giovanna Maria. AU - Megar, Tiziana. AU - Santoro, Massimo. AU - Viglietto, Giuseppe. AU - Verde, Pasquale. AU - Fusco, Alfredo. PY - 1998/7/23. Y1 - 1998/7/23. N2 - We have recently reported that neoplastic transformation of two rat thyroid epithelial cell lines by retroviruses carrying the v-mos and v-ras Ki oncogenes is associated with a drastic increase of AP-1 activity. The most important effects were represented by the dramatic junB and fra-1 gene induction, which was abolished by the block of the transformation-induced HMGI-C protein synthesis. Here, we have further characterized the transformation-dependent AP-1 activity, by analysing the expression of different jun- and fos-related components, in rat thyroid cell lines ...
Background: High mobility group A (HMGA) proteins regulate gene transcription through architectural modulation of chromatin and the formation of multi-protein complexes on promoter/enhancer regions. Differential expression of HMGA variants has been found to be important for distinct differentiation processes and deregulated expression was linked to several disorders. Here we used mouse C2C12 myoblasts and C2C12 cells stably over-expressing HMGA1a-eGFP to study the impact of deregulated HMGA1 expression levels on cellular differentiation. Results: We found that induction of the myogenic or osteogenic program of C2C12 cells caused an immediate down-regulation of HMGA1. In contrast to wild type C2C12 cells, an engineered cell line with stable overexpression of HMGA1a-eGFP failed to differentiate into myotubes. Immunolocalization studies demonstrated that sustained HMGA1a-eGFP expression prevented myotube formation and chromatin reorganization that normally accompanies differentiation. Western Blot analyses
Accumulating studies have demonstrated that high-mobility group A2 (HMGA2), an oncofetal protein, plays a role in tumor development and progression. However, the molecular role of HMGA2 in ovarian carcinoma is yet to be established. MicroRNAs (miRNAs), a group of small noncoding RNAs, negatively regulate gene expression and their dysregulation has been implicated in tumorigenesis. The aim of this study was to investigate the potential involvement of a specific miRNA, miR-219-5p, in HMGA2-induced ovarian cancer. The ovarian cancer cell line, SKOV3, was employed, and miR-219-5p and HMGA2 overexpression vectors constructed. The CCK-8 kit was used to determine cell proliferation and the Transwell® assay used to measure cell invasion and migration. RT-PCR and western blot analyses were applied to analyze the expression of miR-219-5p and HMGA2, and the luciferase reporter assay used to examine the interactions between miR-219-5p and HMGA2. Nude mice were employed to characterize in vivo tumor growth
Les proteïnes HMG (High Mobility Group) són un grup de proteïnes cromosòmiques no histones que van ser anomenades així degut a la seva mobilitat electroforètica. Aquest conjunt de proteïnes està dividit en tres grans subfamílies: les HMGA, les HMGB i les HMGN. Les proteïnes HMGA poden modificar la conformació espacial del DNA, regulant (positivament o negativament) lexpressió de nombrosos gens i influint en molts processos cel·lulars normals com ara el creixement, proliferació, diferenciació i mort cel·lular, i la reparació del DNA. També estan relacionades amb diferents processos patològics, entre ells lobesitat, la diabetis, larteriosclerosi i el càncer. Sha observat com, en molts tipus de càncers, hi ha una sobre-expressió daquestes proteïnes. Se sap que la interacció HMGA-DNA es dóna a través duns motius dunió al DNA anomenats AT-hooks, els quals suneixen a regions riques en adenines (A) i timines (T) del DNA. En les proteïnes HMGA es troben tres motius ...
Role of HMGA1 in basal and cAMP-induced RBP4 expression. Rbp4-Luc reporter vector and HMGA1 expression plasmid (sense or antisense) were cotransfected into Hepa
Anti-HMGA1a / HMGA1b antibody - ChIP Grade (ab4078) has been cited in 13 publications. References for Human, Mouse in ChIP, IHC, IHC-P, WB
Opens the Highlight Feature Bar and highlights feature annotations from the FEATURES table of the record. The Highlight Feature Bar can be used to navigate to and highlight other features and provides links to display the highlighted region separately. Links in the FEATURES table will also highlight the corresponding region of the sequence. More... ...
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英) In a subset of human lipomas, a specific t(3;12) chromosome translocation gives rise to HMGA2-LPP fusion protein, containing the amino (N)-terminal DNA binding domains of HMGA2 fused to the carboxyl (C)-terminal LIM domains of LPP. In addition to its role in adipogenesis, several observations suggest that HMGA2-LPP is linked to chondrogenesis. Here, we analyzed whether HMGA2-LPP promotes chondrogenic differentiation, a marker of which is transactivation of the alpha 2 type XI collagen gene (Col11a2). Real-time PCR analysis showed that HMGA2-LPP and COL11A2 were co-expressed. Luciferase assay demonstrated that either of HMGA2-LPP, wild-type HMGA2 or the N-terminal HMGA2 transactivated the Col11a2 promoter in HeLa cells, while the C-terminal LPP did not. RT-PCR analysis revealed that HMGA2-LPP transcripts in lipomas with the fusion were 591-fold of full-length HMGA2 transcripts in lipomas without the fusion. These results indicate that in vivo overexpression of HMGA2-LPP promotes ...
High Mobility Group AT-hook protein 2 (HMGA2) is a non-histone chromatin binding protein expressed in stem cells, cancer cells but not in normal human somatic cells. The presence of HMGA2 in cancer correlates with advanced neoplastic disease and poor prognosis. HMGA2 plays important roles in Base Excision Repair (BER) and at replication forks. HMGA2 is present at mammalian metaphase telomeres and its loss induces chromosomal aberrations. However, the functional role of HMGA2 at telomeres remains elusive. We hypothesized a protective role of HMGA2 that guards telomeres and modulates DNA damage repair signaling pathways. Employing different HMGA2+ human tumor cell models, we investigated the HMGA2-mediated functions that contribute to chemoresistance in glioblastoma (GB). This study presents a novel interaction of HMGA2 with telomeric protein TRF2 (Telomere Repeat-Binding Factor 2). This interaction retains TRF2 at telomeres, thus capping the telomeres and reducing telomere-dysfunction induced ...
|strong|Mouse anti Human High Mobility Group Protein B2 antibody, clone 3E5|/strong| recognizes human high mobility group protein B2, also known as HMGPB2 or HMG-2. Human high mobility group protein B…
In the study, we used Ba/F3 cells with conditional expression of JAK2V617F or WT JAK2 as a working model to recapitulate the phenotypic comparison between JAK2-mutated and -unmutated MPN cells. We demonstrate that JAK2-mutated cells exhibit upregulation of HMGA2, and the expression of HMGA2 could be affected by the level of let-7a miRNA. HMGA2 overexpression confers JAK2-mutated cells with a survival advantage through inhibited apoptosis, and MPN patients harboring upregulated HMGA2 show an increased propensity for ET phenotype as well as a higher likelihood of developing thrombosis.. The finding, in the study herein, that HMGA2-overex-pressing MPN patients are more likely to belong to the ET subtype and have higher platelet counts is actually supported by several in vivo studies. Oguro et al. disclosed that overexpression of Hmga2 in hematopoietic stem cells induced a myeloproliferative state with enhanced megakaryopoiesis in mice,26 whereas Yang et al. similarly demonstrated that Hmga2 ...
TY - JOUR. T1 - Expression of the HMGI(Y) gene products in human neuroblastic tumours correlates with differentiation status. AU - Giannini, G.. AU - Kim, C. J.. AU - Marcotullio, L. Di. AU - Manfioletti, G.. AU - Cardinali, B.. AU - Cerignoli, F.. AU - Ristori, E.. AU - Zani, M.. AU - Frati, L.. AU - Screpanti, I.. AU - Gulino, A.. PY - 2000. Y1 - 2000. N2 - HMGI and HMGY are splicing variants of the HMGI(Y) gene and together with HMGI-C, belong to a family of DNA binding proteins involved in maintaining active chromatin conformation and in the regulation of gene transcription. The expression of the HMGI(Y) gene is maximal during embryonic development, declines in adult differentiated tissues and is reactivated in most transformed cells in vitro and in many human cancers in vivo. The HMGI(Y) genomic locus is frequently rearranged in mesenchymal tumours, suggesting a biological role for HMGI(Y) gene products in tumour biology. HMGIs are both target and modulators of retinoic acid activity. In ...
The high mobility group (HMG) of nuclear proteins regulates expression of many genes through architectural remodelling of the chromatin structure, and formation of multiprotein complexes on promoter/enhancer regions. This leads to the active transcription of their target genes. Here we show that HMGA2, a member of the HMGA sub-family of HMG proteins, has a critical function in cardiogenesis. Overexpression of HMGA2 enhanced, whereas siRNA-mediated knockdown of HMGA2 blocked, cardiomyocyte differentiation of the embryonal carcinoma cell line P19CL6. Moreover, overexpression of a dominant-negative HMGA2 or morpholino-mediated knockdown of HMGA2 expression blocked normal heart formation in Xenopus laevis embryos, suggesting that HMGA2 has an important role in cardiogenesis both in vitro and in vivo. Mechanistically, HMGA2 associated with Smad1/4 and showed synergistic trans-activation of the gene for a cardiac transcription factor Nkx2.5; a conserved HMGA2 binding site was required for the promoter ...
The story began more than two decades ago with identification of a boy with high glucose levels despite extremely elevated insulin - that is, severe insulin resistance (IR) [2]. His blood cells showed very low insulin binding and insulin receptor expression, and yet, surprisingly, neither of the alleles of the gene encoding the insulin receptor, INSR, had any mutation [3]. Later independent studies found that the protein HMGA1 was bound to key sites in the promoter of the INSR gene, and provided evidence that HMGA1 is involved in the high levels of INSR expression in insulin-responsive tissues [4]. HMG (high mobility group) proteins are the second most abundant nuclear proteins after histones, and proteins in the HMGA subfamily, although without intrinsic transcriptional activating activity, function as permissive architectural transcription factors, binding AT-rich sequence motifs, distorting DNA and nucleating assembly of complexes of other factors with canonical transactivation motifs [5]. ...
Background: High mobility group A (HMGA) proteins regulate gene transcription through architectural modulation of chromatin and the formation of multi-protein complexes on promoter/enhancer regions. Differential expression of HMGA variants has been found to be important for distinct differentiation processes and deregulated expression was linked to several disorders. Here we used mouse C2C12 myoblasts and C2C12 cells stably over-expressing HMGA1a-eGFP to study the impact of deregulated HMGA1 expression levels on cellular differentiation. Results: We found that induction of the myogenic or osteogenic program of C2C12 cells caused an immediate down-regulation of HMGA1. In contrast to wild type C2C12 cells, an engineered cell line with stable overexpression of HMGA1a-eGFP failed to differentiate into myotubes. Immunolocalization studies demonstrated that sustained HMGA1a-eGFP expression prevented myotube formation and chromatin reorganization that normally accompanies differentiation. Western Blot ...
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Genomes and Genes, Publications, Locale, Scientific Experts, Species, Research Topics about Experts and Doctors on high mobility group proteins in France
The dwarf phenotype characterizes the smallest of rabbit breeds and is governed largely by the effects of a single dwarfing allele with an incompletely dominant effect on growth. Dwarf rabbits typically weigh under 1 kg and have altered craniofacial morphology. The dwarf allele is recessive lethal and dwarf homozygotes die within a few days of birth. The dwarf phenotype is expressed in heterozygous individuals and rabbits from dwarf breeds homozygous for the wild-type allele are normal, although smaller when compared to other breeds. Here, we show that the dwarf allele constitutes a ∼12.1 kb deletion overlapping the promoter region and first three exons of the HMGA2 gene leading to inactivation of this gene. HMGA2 has been frequently associated with variation in body size across species. Homozygotes for null alleles are viable in mice but not in rabbits and probably not in humans. RNA-sequencing analysis of rabbit embryos showed that very few genes (4-29 genes) were differentially expressed ...
In vivo IkappaB alpha is a stronger inhibitor of NF-kappaB than is IkappaB beta. This difference is directly correlated with their varying abilities to inhibit NF-kappaB binding to DNA in vitro and in vivo. Moreover, IkappaB alpha, but not IkappaB beta, can remove NF-kappaB from functional preinitiation complexes in in vitro transcription experiments. Both IkappaBs function in vivo not only in the cytoplasm but also in the nucleus, where they inhibit NF-kappaB binding to DNA. The inhibitory activity of IkappaB beta, but not that of IkappaB alpha, is facilitated by phosphorylation of the C-terminal PEST sequence by casein kinase II and/or by the interaction of NF-kappaB with high-mobility group protein I (HMG I) on selected promoters. The unphosphorylated form of IkappaB beta forms stable ternary complexes with NF-kappaB on the DNA either in vitro or in vivo. These experiments suggest that IkappaB alpha works as a postinduction repressor of NF-kappaB independently of HMG I, whereas IkappaB beta ...
High-mobility group A1 (HMGA1) protein are architectural chromatinic protein, abundantly expressed during embryogenesis and in most malignancy cells, but expressed in low amounts or absent in regular adult cells. malignancy cells. We exhibited that HMGA1 silencing in CTSCs raises come cell quiescence and decreases self-renewal and sphere-forming effectiveness (SFE). The second option, collectively with the upregulation and asymmetric Bedaquiline (TMC-207) supplier distribution of NUMB, is usually a sign of the recovery of an asymmetric department design, common of regular come cells. We discovered that HMGA1 transcriptionally manages g53 further, which is known to control the balance between asymmetric and symmetric divisions in CSCs. As a result, our data indicate a important function for HMGA1 in controlling both self-renewal and the symmetric/asymmetric department proportion in CSCs, recommending that preventing HMGA1 function might end up being an effective anti-cancer therapy. gene phrase ...
PREDICTED: similar to High mobility group protein 1 (HMG-1) (High mobility group protein B1) (Amphoterin) (Heparin-binding protein p30) isoform 1 [Canis familiaris ...
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cytoplasm, extracellular space, nuclear chromatin, nucleus, cis-regulatory region sequence-specific DNA binding, DNA binding, DNA binding, bending, double-stranded DNA binding, drug binding, four-way junction DNA binding
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Mouse polyclonal antibody raised against a full-length human TBL1Y protein. TBL1Y (ADR83034.1, 1 a.a. ~ 522 a.a) full-length human protein. (H00090665-B01P) - Products - Abnova
REPORT High Mobility Group Protein B1 (High Mobility Group Protein 1 or High Mobility Group Protein Box 1 or HMGB1) - High mobility group box 1 protein also known as high-mobility group protein 1 (HMG-1) is a protein encoded by ... > ...
J:91358 Brants JR, Ayoubi TA, Chada K, Marchal K, Van de Ven WJ, Petit MM, Differential regulation of the insulin-like growth factor II mRNA-binding protein genes by architectural transcription factor HMGA2. FEBS Lett. 2004 Jul 2;569(1-3):277-83 ...
HMG20B; high mobility group 20B; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related; BRAF25; BRAF35; HMG box domain containing 2; HMGX2; HMGXB2; SMARCE1r; SOXL; SMARCE1-related protein; high-mobility grou; high-mobility group 20B; BRCA2-associated factor 35; HMG box-containing protein 20B; HMG domain-containing protein 2; Sox-like transcriptional factor; HMG domain-containing protein HMGX2; structural DNA-binding protein BRAF35; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E, member 1-related; PP7706; pp8857; FLJ26127; SOXL, HMGX2, BRAF25, BRAF35, HMGXB2, PP7706, pp8857, SMARCE1r; fc85b02; wu:fc85b02; zgc:110001; si:dkey-110c1.6; high mobility group box domain containing ...
While most of the information available concerns the numerous effects of thyroid hormones on the maturation of neurons, it has been noted that glial cells also are affected by thyroid status (1). In...
Conclusion: Variants found in exon 5 of the HMGA2 gene have not been described and have an uncertain significance in the genesis of FML. Further studies, including a more significant number of affected individuals and functional analysis of the novel variants of HGMA2 gene, should be undertaken to better understand its biological role in FML. PMID: 32021365 [PubMed]...
For individuals of white European descent, certain variations of the gene HMGA1 are associated with Type 2 diabetes, according to Antonio Brunetti of the University of Catanzaro in Catanzaro, Italy, and colleagues. They found that among Italian, American and French patients, 7% to 8% of Type 2 diabetes patients in all three populations had the gene mutation. The study authors noted, however, that further studies of the HMGA1 gene and its variants, including studies in other racial types, are needed to understand the role of HMGA1 in insulin resistance and Type 2 diabetes.. The study appeared in the March 2 issue of Journal of the American Medical Association.. ...
Thematrices r 2Y :, i Y :, j L I r 2U :, i Y :, j L I r 2U :, i U :, j L I r 2t 0 Y :, j L I r 2t 0 U :, j L I r 2t 0 t 0 L I r 2t f Y :, j L I r 2t f U :, j L I r 2t f t 0 L I and r 2t f t f L I areobtainedinasparsemanneras r 2Y :, i Y :, j L I = 2664 diag @ 2 L I @ y i @ y j 1N 0 N 1 0 1 N 0 3775 ,( i =1,..., n y j =1,..., i ), r 2U :, i Y :, j L I = diag @ 2 L I @ u i @ y j 1N 0 N 1 # ,( i =1,..., n u j =1,..., n y ), r 2U :, i U :, j L I = diag @ 2 L I @ u i @ u j 1N ,( i =1,..., n u j =1,..., i ), r 2t 0 Y :, j L I = ( @ 2 L I @ t 0 @ y j 1N ) T 0 # ,( j =1,..., n y ), r 2t 0 U :, j L I = ( @ 2 L I @ t 0 @ u j 1N ) T ,( j =1,..., n u ), r 2t 0 t 0 L I = @ 2 L I @ t 2 0 r 2t f Y :, j L I = ( @ 2 L I @ t f @ y j 1N ) T 0 # ,( j =1,..., n y ), r 2t f U :, j L I = ( @ 2 L I @ t f @ u j 1N ) T ,( j =1,..., n u ), r 2t f t 0 L I = @ 2 L I @ t f @ t 0 r 2t f t f L I = @ 2 L I @ t 2 f (3 78) ItisseenthatthederivativesgiveninEq.( 3 78 )arefunctionsofthederivativesof L I ...
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Non-essential INO80 Chromatin Remodeling Complex Subunit; Preferentially Binds DNA Ends, Protecting Them From Exonucleatic Cleavage; Deletion Affects Telomere Maintenance Via Recombination; Related To Mammalian High Mobility Group Proteins
Complete information for TMSB4Y gene (Protein Coding), Thymosin Beta 4, Y-Linked, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Background: MDM2 (12q15), HMGA2 (12q14.3) and CDK4 (12q14.1) are the main target genes of the 12q14-15 amplicon in well-differentiated and dedifferentiated liposarcomas (WDLPS/DDLPS). While MDM2 and HMGA2 are consistently amplified, CDK4 is not amplified in approximately 10% of WDLPS/DDLPS. Our aim was to determine whether the absence of CDK4 amplification was -i) associated with specific clinico-pathological features -ii) compensated by another genomic event involved in the p16/INK4A-CDK4/cyclinD1-pRb pathway. Methods: We compared the clinical characteristics of a series of 143 WDLPS/DDLPS with amplification of both MDM2 and CDK4 (MDM2+/CDK4+) to a series of 45 WDLPS/DDLPS with amplification of MDM2 but no CDK4 amplification (MDM2+/CDK4-). We have used fluorescence in situ hybridization (FISH) and real-time quantitative RT-PCR analysis to determine the status of the CDKN2A (9p21.3) which encodes p16/INK4A and p14/ARF mRNA, RB1 (13q14.2) and CCND1 (CYCLIND1, 11q13.3) genes. Results: In ...
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Protein Related To Mammalian High Mobility Group (HMG) Proteins; Nuclear Protein; Essential For Function Of H/ACA-type SnoRNPs, Which Are Involved In 18S RRNA Processing
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