CORTICAL LARGE BONE SCREWS
- Known as:
- CORTICAL LARGE BONE SCREWS
- Catalog number:
- 35-571-74
- Product Quantity:
- 74 mm x 50
- Category:
- -
- Supplier:
- AJMAL
- Gene target:
- CORTICAL LARGE BONE SCREWS
Ask about this productRelated genes to: CORTICAL LARGE BONE SCREWS
- Gene:
- LARGE1 NIH gene
- Name:
- LARGE xylosyl- and glucuronyltransferase 1
- Previous symbol:
- LARGE
- Synonyms:
- KIAA0609
- Chromosome:
- 22q12.3
- Locus Type:
- gene with protein product
- Date approved:
- 1999-06-02
- Date modifiied:
- 2019-04-23
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- Matriglycan, a recently characterized linear polysaccharide, is composed of alternating xylose and glucuronic acid subunits bound to the ubiquitously expressed protein α-dystroglycan (α-DG). Pathogenic arenaviruses, like the Lassa virus (LASV), hijack this long linear polysaccharide to gain cellular entry. Until recently, it was unclear through what mechanisms LASV engages its matriglycan receptor to initiate infection. Additionally, how matriglycan is synthesized onto α-DG by the Golgi-resident glycosyltransferase LARGE1 remained enigmatic. Recent structural data for LARGE1 and for the LASV spike complex informs us about the synthesis of matriglycan as well as its usage as an entry receptor by arenaviruses. In this review, we discuss structural insights into the system of matriglycan generation and eventual recognition by pathogenic viruses. We also highlight the unique usage of matriglycan as a high-affinity host receptor compared with other polysaccharides that decorate cells. - Source: PubMed
Publication date: 2024/03/07
Katz MichaelDiskin Ron - Spinal muscular atrophy (SMA) is a neuromuscular disorder caused by recessive pathogenic variants affecting the survival of motor neuron (SMN1) gene (localized on 5q). In consequence, cells lack expression of the corresponding protein. This pathophysiological condition is clinically associated with motor neuron (MN) degeneration leading to severe muscular atrophy. Additionally, vulnerability of other cellular populations and tissues including skeletal muscle has been demonstrated. Although the therapeutic options for SMA have considerably changed, treatment responses may differ thus underlining the persistent need for validated biomarkers. To address this need and to identify novel marker proteins for SMA, we performed unbiased proteomic profiling on cerebrospinal fluid derived (CSF) from genetically proven SMA type 1-3 cases and afterwards performed ELISA studies on CSF and serum samples to validate the potential of a novel biomarker candidates in both body fluids. To further decipher the pathophysiological impact of this biomarker, immunofluorescence studies were carried out on spinal cord and skeletal muscle derived from a 5q-SMA mouse model. Proteomics revealed increase of LARGE1 in CSF derived from adult patients showing a clinical response upon treatment with nusinersen. Moreover, LARGE1 levels were validated in CSF samples of further SMA patients (type 1-3) by ELISA. These studies also unveiled a distinguishment between groups in improvement of motor skills: adult patients do present with lowered level per se at baseline visit while no elevation upon treatment in the pediatric cohort can be observed. ELISA-based studies of serum samples showed no changes in the pediatric cohort but unraveled elevated level in adult patients responding to future intervention with nusinersen, while non-responders did not show a significant increase. Additional immunofluorescence studies of LARGE1 in MN and skeletal muscle of a SMA type 3 mouse model revealed an increase of LARGE1 during disease progression. Our combined data unraveled LARGE1 as a protein dysregulated in serum and CSF of SMA-patients (and in MN and skeletal muscle of SMA mice) holding the potential to serve as a disease marker for SMA and enabling to differentiate between patients responding and non-responding to therapy with nusinersen. - Source: PubMed
Publication date: 2024/03/12
Roos AndreasSchmitt Linda-IsabellHansmann ChristinaHezel StefanieSalmanian SchahinHentschel AndreasMeyer NancyMarina Adela DellaKölbel HeikeKleinschnitz ChristophSchara-Schmidt UlrikeLeo MarkusHagenacker Tim - Infection with Lassa virus (LASV) can cause Lassa fever, a haemorrhagic illness with an estimated fatality rate of 29.7%, but causes no or mild symptoms in many individuals. Here, to investigate whether human genetic variation underlies the heterogeneity of LASV infection, we carried out genome-wide association studies (GWAS) as well as seroprevalence surveys, human leukocyte antigen typing and high-throughput variant functional characterization assays. We analysed Lassa fever susceptibility and fatal outcomes in 533 cases of Lassa fever and 1,986 population controls recruited over a 7 year period in Nigeria and Sierra Leone. We detected genome-wide significant variant associations with Lassa fever fatal outcomes near GRM7 and LIF in the Nigerian cohort. We also show that a haplotype bearing signatures of positive selection and overlapping LARGE1, a required LASV entry factor, is associated with decreased risk of Lassa fever in the Nigerian cohort but not in the Sierra Leone cohort. Overall, we identified variants and genes that may impact the risk of severe Lassa fever, demonstrating how GWAS can provide insight into viral pathogenesis. - Source: PubMed
Publication date: 2024/02/07
Kotliar DylanRaju SiddharthTabrizi ShervinOdia IkponmwosaGoba AugustineMomoh MambuSandi John DembyNair ParvathyPhelan EricTariyal RidhiEromon Philomena EMehta SamarRobles-Sikisaka RefugioSiddle Katherine JStremlau MattJalloh SimbirieGire Stephen KWinnicki SarahChak BridgetSchaffner Stephen FPauthner MatthiasKarlsson Elinor KChapin Sarah RKennedy Sharon GBranco Luis MKanneh LansanaVitti Joseph JBroodie NishaGladden-Young AdrianneOmoniwa OmowunmiJiang Pan-PanYozwiak NathanHeuklom ShannonMoses Lina MAkpede George OAsogun Danny ARubins KathleenKales SusanHappi Anise NIruolagbe Christopher ODic-Ijiewere MercyIraoyah KellyOsazuwa Omoregie OOkonkwo Alexander KKunz StefanMcCormick Joseph BKhan S HumarrHonko Anna NLander Eric SOldstone Michael B AHensley LisaFolarin Onikepe AOkogbenin Sylvanus AGünther StephanOllila Hanna MTewhey RyanOkokhere Peter OSchieffelin John SAndersen Kristian GReilly Steven KGrant Donald SGarry Robert FBarnes Kayla GHappi Christian TSabeti Pardis C - Interpretation of disease-causing genetic variants remains a challenge in human genetics. Current costs and complexity of deep mutational scanning methods hamper crowd-sourcing approaches toward genome-wide resolution of variants in disease-related genes. Our framework, Saturation Mutagenesis-Reinforced Functional assays (SMuRF), addresses these issues by offering simple and cost-effective saturation mutagenesis, as well as streamlining functional assays to enhance the interpretation of unresolved variants. Applying SMuRF to neuromuscular disease genes and , we generated functional scores for over 99.8% of all possible coding single nucleotide variants and resolved 310 clinically reported variants of uncertain significance with high confidence, enhancing clinical variant interpretation in dystroglycanopathies. SMuRF also demonstrates utility in predicting disease severity, resolving critical structural regions, and providing training datasets for the development of computational predictors. Our approach opens new directions for enabling variant-to-function insights for disease genes in a manner that is broadly useful for crowd-sourcing implementation across standard research laboratories. - Source: PubMed
Publication date: 2023/11/27
Ma KaiyueNg Kenneth KHuang ShushuLake Nicole JXu JennyLek AngelaGe LinWoodman Keryn GKoczwara Katherine EHo VincentO'Connor Christine LJoseph SoumyaBrindley Melinda ACampbell Kevin PLek Monkol - Non-membrane-bound biomolecular condensates have been proposed to represent an important mode of subcellular organization in diverse biological settings. However, the fundamental principles governing the spatial organization and dynamics of condensates at the atomistic level remain unclear. The Lge1 protein is required for histone H2B ubiquitination and its N-terminal intrinsically disordered fragment (Lge1) undergoes robust phase separation. This study connects single- and multi-chain all-atom molecular dynamics simulations of Lge1 with the in vitro behavior of Lge1 condensates. Analysis of modeled protein-protein interactions elucidates the key determinants of Lge1 condensate formation and links configurational entropy, valency, and compactness of proteins inside the condensates. A newly derived analytical formalism, related to colloid fractal cluster formation, describes condensate architecture across length scales as a function of protein valency and compactness. In particular, the formalism provides an atomistically resolved model of Lge1 condensates on the scale of hundreds of nanometers starting from individual protein conformers captured in simulations. The simulation-derived fractal dimensions of condensates of Lge1 and its mutants agree with their in vitro morphologies. The presented framework enables a multiscale description of biomolecular condensates and embeds their study in a wider context of colloid self-organization. - Source: PubMed
Publication date: 2023/07/20
Polyansky Anton AGallego Laura DEfremov Roman GKöhler AlwinZagrovic Bojan