C9ORF95 Human
Description
Introduction to C9ORF95 Human
C9ORF95 was initially designated as "Chromosome 9 Open Reading Frame 95," indicating its original identification as a protein-coding sequence of unknown function located on chromosome 9 in the human genome. Subsequent research has established its identity as Nicotinamide Riboside Kinase 1 (NMRK1), a member of the uridine kinase family with significant roles in cellular metabolism .
The gene encoding this protein is located on human chromosome 9, and its product participates in crucial biochemical pathways related to NAD+ synthesis . NAD+ serves as an essential cofactor for multiple cellular redox processes linked to fuel utilization and energy metabolism, including the mitochondrial oxidative phosphorylation system . Additionally, NAD+ functions as a substrate for enzymes such as sirtuins and poly(ADP-ribose) polymerases (PARPs), which have wide-ranging effects on cellular function, aging, and disease processes .
Nomenclature and Identification
The protein initially characterized as C9ORF95 has accumulated several synonyms and identifiers in scientific literature and databases. Understanding these alternative designations is crucial for comprehensive literature searches and research.
Alternative Designations
C9ORF95 is now more commonly referred to as NMRK1 in scientific literature, reflecting its identified enzymatic function. The protein has been recorded under multiple names across different databases and research papers, as summarized in Table 1.
Table 1: Alternative Designations for C9ORF95 Human Protein
| Designation | Full Name | Context of Usage |
|---|---|---|
| NMRK1 | Nicotinamide Riboside Kinase 1 | Primary current designation |
| NRK1 | Nicotinamide Riboside Kinase 1 | Common abbreviation |
| NmR-K1 | Nicotinamide Riboside Kinase 1 | Alternative abbreviation |
| C9orf95 | Chromosome 9 Open Reading Frame 95 | Original designation |
| bA235O14.2 | Bacterial Artificial Chromosome Clone Identifier | Early research identifier |
| RP11-235O14.2 | Research Project Clone Identifier | Early research identifier |
| RNK1 | Ribosylnicotinamide Kinase 1 | Functional designation |
Gene and Protein Identifiers
The human NMRK1 gene and its protein product are cataloged in various biological databases under specific identifiers that facilitate research and cross-referencing.
Table 2: Database Identifiers for Human NMRK1
| Database | Identifier | Notes |
|---|---|---|
| Entrez Gene ID | 54981 | NCBI gene identifier |
| UniProt Accession | Q9NWW6 | Protein sequence database |
| RefSeq | NM_017881 | Transcript variant 1 reference sequence |
| RefSeq Protein | NP_060351.1 | Protein reference sequence |
| HGNC ID | HGNC:26057 | HUGO Gene Nomenclature Committee identifier |
| UniGene ID | Hs.494186 | Transcript sequence database identifier |
Molecular Structure and Characteristics
Human NMRK1 exhibits specific molecular characteristics that define its structure and biochemical properties, contributing to its enzymatic function in NAD+ metabolism pathways.
Primary Structure
The primary sequence of human NMRK1 consists of 199 amino acids, forming a protein with a molecular weight of approximately 23 kDa . The amino acid sequence is highly conserved across various species, indicating the evolutionary importance of this enzyme .
The full amino acid sequence of human NMRK1 is:
MKTFIIGISGVTNSGKTTLAKNLQKHLPNCSVISQDDFFKPESEIETDKNGFLQYDVLEALNMEKMMSAISCWMESARHSVVSTDQESAEEIPILIIEGFLLFNYKPLDTIWNRSYFLTIPYEECKRRRSTRVYQPPDSPGYFDGHVWPMYLKYRQEMQDITWEVVYLDGTKSEEDLFLQVYEDLIQELAKQKCLQVTA
Conserved Domains and Motifs
NMRK1 belongs to the uridine kinase family and contains several conserved domains and motifs that are characteristic of nucleoside kinases . These structural elements are crucial for substrate binding and catalytic activity.
Tertiary Structure
The crystal structure of human NMRK1 has been determined and deposited in the Protein Data Bank (PDB ID: 2QL6) . This structural data reveals that NMRK1 adopts a fold characteristic of the deoxynucleoside kinase and nucleoside monophosphate (NMP) kinase superfamily, despite low sequence conservation with other members of this group .
The active site of NMRK1 is located in a groove between the central parallel beta sheet core and the LID and NMP-binding domains . This structural arrangement facilitates substrate binding and catalysis during the phosphorylation reactions mediated by the enzyme.
Biological Function and Role in NAD+ Metabolism
NMRK1 plays a crucial role in NAD+ biosynthesis pathways, particularly in the salvage pathway utilizing nicotinamide riboside (NR) as a precursor.
Enzymatic Activity
NMRK1 functions as a kinase that catalyzes the phosphorylation of nicotinamide riboside (NR) to form nicotinamide mononucleotide (NMN), which is subsequently converted to NAD+ by nicotinamide mononucleotide adenylyltransferase (NMNAT) . Additionally, NMRK1 can phosphorylate nicotinic acid riboside (NaR) to form nicotinic acid mononucleotide (NaMN), which enters an alternative pathway for NAD+ synthesis .
Table 3: Enzymatic Reactions Catalyzed by NMRK1
| Substrate | Product | Co-factor | Pathway |
|---|---|---|---|
| Nicotinamide Riboside (NR) | Nicotinamide Mononucleotide (NMN) | ATP | NR → NMN → NAD+ |
| Nicotinic Acid Riboside (NaR) | Nicotinic Acid Mononucleotide (NaMN) | ATP | NaR → NaMN → NaAD → NAD+ |
| Tiazofurin | Tiazofurin Monophosphate | ATP | Antitumor drug activation |
| 3-Deazaguanosine | 3-Deazaguanosine Monophosphate | ATP | Antitumor drug activation |
NAD+ Metabolism Pathways
NAD+ is an essential cofactor for numerous cellular reactions, particularly those involved in energy metabolism and redox processes. It also serves as a substrate for enzymes such as sirtuins and PARPs, which play roles in cellular signaling, DNA repair, and aging processes .
Recent research has established that NMRK1 is necessary and rate-limiting for the use of exogenous NR and NMN for NAD+ synthesis . Interestingly, studies using stable isotope-labeled compounds have demonstrated that extracellular NMN is metabolized to NR before cellular uptake, highlighting the importance of NMRK1 in mediating the metabolic effects of both NR and NMN supplementation .
Expression Pattern
NMRK1 expression has been detected in various tissues across different species. In humans, the gene is expressed in multiple organs, although expression levels may vary by tissue type. The conservation of NMRK1 across species from humans to zebrafish suggests its fundamental importance in cellular metabolism .
Crystal Structure and Active Site
The three-dimensional structure of human NMRK1 provides valuable insights into its catalytic mechanism and substrate specificity.
Active Site Configuration
The active site of NMRK1 contains specific residues that interact with the substrates and mediate catalysis. The hydroxyl groups on the ribose moiety of NR are recognized by Asp56 and Arg129, while Asp36 serves as the general base in the catalytic mechanism . Mutation studies have confirmed the importance of these residues, as alterations to the active site configuration can abolish the catalytic activity of the enzyme .
Substrate Binding and Specificity
The structural features of NMRK1's active site explain its substrate specificity for NR and related compounds. The enzyme's ability to phosphorylate both NR and certain anticancer nucleoside analogs such as tiazofurin makes it relevant not only in NAD+ metabolism but also in the activation of therapeutic compounds .
Research Applications and Tools
Various research tools and reagents are available for studying NMRK1, facilitating both basic research and potential therapeutic investigations.
Recombinant Proteins
Several commercial sources offer recombinant human NMRK1 proteins for research purposes. These products typically consist of the NMRK1 sequence with various tags to aid in purification and detection.
Table 4: Available Recombinant NMRK1 Proteins
Genetic Tools
Various genetic tools for manipulating NMRK1 expression are available for research purposes, including:
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Overexpression systems using viral vectors, such as AAV-based expression systems
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Lysates from cells overexpressing NMRK1 for functional studies
These tools enable researchers to investigate the biological roles of NMRK1 in different cellular contexts and model systems.
Metabolic Significance and Research Findings
Research into NMRK1 has uncovered its significance in cellular metabolism and potential relevance to various physiological and pathological conditions.
NAD+ Precursor Metabolism
A key finding regarding NMRK1 is its essential role in mediating the metabolic effects of NR and NMN supplementation. Studies have demonstrated that NMRK1 is necessary and rate-limiting for using exogenous NR and NMN for NAD+ synthesis . Notably, genetic gain- and loss-of-function models have shown that NMRK1's role in driving NAD+ synthesis from other precursors, such as nicotinamide or nicotinic acid, is dispensable .
Research using stable isotope-labeled compounds has revealed that extracellular NMN must be metabolized to NR before cellular uptake and subsequent conversion to NAD+ . This finding explains the overlapping metabolic effects observed with NR and NMN supplementation and highlights the central role of NMRK1 in these processes .
Therapeutic Implications
The involvement of NMRK1 in NAD+ metabolism suggests potential therapeutic applications, particularly in conditions associated with NAD+ deficiency or dysregulation. Supplementation with NAD+ precursors like NR and NMN has shown protective effects against metabolic disease, neurodegenerative disorders, and age-related physiological decline in mammalian models . Given NMRK1's role in mediating these effects, targeting this enzyme or its pathways could represent a promising therapeutic strategy.
Additionally, NMRK1's ability to phosphorylate certain anticancer drugs, such as tiazofurin and 3-deazaguanosine, indicates its potential relevance in cancer therapy . Understanding NMRK1's structure and function could facilitate the development of more effective nucleoside analog-based therapeutics.
Future Research Directions
Despite significant advances in understanding NMRK1's structure and function, several areas warrant further investigation to fully elucidate its biological significance and therapeutic potential.
Tissue-Specific Functions
Further research into the tissue-specific expression and function of NMRK1 could provide insights into its role in different physiological contexts. Given that NAD+ metabolism is implicated in various aspects of cellular function and disease processes, understanding how NMRK1 contributes to tissue-specific NAD+ homeostasis is of considerable interest.
Pathological Relevance
The potential involvement of NMRK1 in pathological conditions, such as metabolic disorders, neurodegenerative diseases, and cancer, represents an important area for future research. Investigating how alterations in NMRK1 expression or function contribute to disease processes could reveal new therapeutic targets.
Therapeutic Applications
Building on the understanding of NMRK1's role in NAD+ metabolism, further research into targeted interventions that modulate NMRK1 activity or enhance its efficiency in utilizing NAD+ precursors could lead to novel therapeutic approaches. This includes optimizing NAD+ precursor supplementation strategies and developing specific modulators of NMRK1 function.
Product Specs
MQDITWEVVY LDGTKSEEDL FLQVYEDLIQ ELAKQKCLQV TA.
Q&A
What is C9ORF95/NMRK1 and what is its biochemical function?
C9ORF95/NMRK1 is a member of the uridine kinase family that plays a crucial role in NAD+ metabolism, which is vital for all organisms as both a coenzyme for oxidoreductases and as a source of ADPribosyl groups used in numerous biological reactions, including those associated with delaying aging in experimental systems . The primary function of NMRK1 is catalyzing the phosphorylation of nicotinamide riboside (NR) and nicotinic acid riboside (NaR) to form nicotinamide mononucleotide (NMN) and nicotinic acid mononucleotide (NaMN) . Additionally, C9ORF95 phosphorylates the antitumor drugs tiazofurin and 3-deazaguanosine, suggesting potential roles in experimental cancer research .
For studying this enzyme's function, researchers should consider using recombinant protein expression systems and kinase activity assays with radiolabeled substrates to accurately measure phosphorylation rates under various conditions. Mass spectrometry approaches can also be employed to analyze reaction products and confirm enzyme specificity.
What expression systems are recommended for producing recombinant C9ORF95/NMRK1?
For research applications, E. coli is the most commonly used expression system for producing recombinant C9ORF95, as evidenced by commercial preparations . For structural and functional studies, researchers can produce this protein with various tags, including His-tag and GST-tag, to facilitate purification through affinity chromatography . The available recombinant formats include:
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His-tagged protein (25.6kDa) produced in E. coli, offering a streamlined purification approach through nickel affinity chromatography
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GST-tagged protein (49.6kDa) produced in wheat germ in vitro systems, providing potentially improved solubility for certain applications
When designing expression studies, researchers should consider codon optimization for the expression system and include appropriate protease cleavage sites if tag removal is desired for downstream applications. The choice between bacterial and eukaryotic expression systems should be guided by the specific experimental requirements regarding protein folding and post-translational modifications.
What are optimal storage and handling conditions for C9ORF95/NMRK1 in experimental settings?
Commercial preparations of C9ORF95/NMRK1 protein are typically formulated in stabilizing buffers. The recommended storage conditions are:
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Short-term (2-4 weeks): Store at 4°C
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Long-term: Store frozen at -20°C or -80°C, depending on preparation
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For optimal stability: Add carrier protein (0.1% HSA or BSA) for long-term storage
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Avoid multiple freeze-thaw cycles which can lead to protein denaturation and loss of activity
Typical formulation contains:
Alternative formulations for GST-tagged versions may include:
For kinase activity assays, researchers should consider including ATP stability-enhancing components in reaction buffers, such as magnesium ions and fresh ATP preparations. Activity measurements should be conducted promptly after protein preparation or thawing to ensure maximum enzymatic function.
How can researchers effectively measure C9ORF95/NMRK1 enzyme kinetics?
To accurately assess C9ORF95/NMRK1 kinase activity, researchers should employ a multi-faceted approach:
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Direct Phosphorylation Assay: Measure the transfer of radiolabeled phosphate from ATP to nicotinamide riboside substrates, followed by thin-layer chromatography or HPLC separation of products.
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Coupled Enzyme Assays: Link NMRK1 activity to subsequent enzymatic reactions in the NAD+ biosynthesis pathway, monitoring NADH/NAD+ levels through fluorescence or absorbance.
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Mass Spectrometry: Quantify the conversion of NR to NMN or NaR to NaMN using LC-MS/MS for precise substrate-product analysis.
Researchers should generate Michaelis-Menten kinetics data by varying substrate concentrations while maintaining constant enzyme concentration. Kinetic parameters (Km, Vmax, kcat) should be calculated to characterize the enzyme's affinity for different substrates. Temperature and pH optima should also be determined through systematic variation of these parameters in the reaction environment.
What approaches are recommended for studying C9ORF95/NMRK1 expression patterns in human tissues?
Multiple complementary approaches should be employed to comprehensively study C9ORF95/NMRK1 expression patterns:
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Western Blotting: Using specific antibodies like the rabbit recombinant monoclonal NRK1 antibody (ab169548) at optimized dilutions (1/10000) for detection in various cell lines, including IM-9, LoVo, HT-29, and MCF7 which have demonstrated detectable expression levels .
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Flow Cytometry: For intracellular protein detection in single cells, enabling quantification across heterogeneous cell populations .
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RNA-seq/qPCR: For transcriptional profiling across tissues, providing quantitative mRNA expression data that can complement protein-level studies.
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Chromatin Accessibility Analysis: Consider using techniques like ATAC-seq to investigate transcriptional regulation of C9ORF95, particularly in disease states where epigenetic dysregulation may occur .
When analyzing expression patterns, researchers should be mindful of antibody specificity and validation requirements. Cross-validation using multiple detection methods is recommended, particularly when studying tissues where expression levels may be low or variable.
What is the relationship between C9ORF95 and neurodegenerative diseases?
While C9ORF95/NMRK1 itself has not been directly implicated in neurodegenerative diseases, the related gene C9ORF72 has been strongly associated with amyotrophic lateral sclerosis (ALS) and frontotemporal dementia through a hexanucleotide repeat expansion 'GGGGCC' . Studies have found that carriers of 17 or more repeats at the C9ORF72 locus carry a specific founder haplotype, suggesting a common ancestor for this mutation .
For researchers investigating potential connections between C9ORF95 and neurodegeneration, several methodological considerations are important:
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Clearly distinguish between C9ORF95 and C9ORF72 in experimental design and analysis
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Consider potential functional relationships in NAD+ metabolism pathways that might indirectly link C9ORF95 to neurodegeneration
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Design genotyping strategies that can accurately detect repeat expansions in related genes
Analysis of repeat lengths should be conducted using PCR-based methods or newer long-read sequencing technologies that can accurately capture expanded repeats. The distribution of repeat numbers across different populations should be carefully documented, as demonstrated in the cited psychiatric case-control study where no carriers of >30 repeats were found .
How might C9ORF95/NMRK1 function relate to vascular disorders and fibrosis?
While direct evidence from the provided sources is limited, the role of C9ORF95/NMRK1 in NAD+ metabolism suggests potential implications for vascular disorders and fibrotic diseases. NAD+ is crucial for cellular redox reactions and sirtuins that regulate numerous biological processes including vascular homeostasis.
When designing studies to investigate this relationship, researchers should consider:
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Examining C9ORF95/NMRK1 expression in endothelial cells from patients with vascular disorders like scleroderma, where aberrant angiogenesis occurs
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Utilizing epigenetic analysis techniques like those described for HDAC5 studies in scleroderma
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Implementing ATAC-seq methods to evaluate chromatin accessibility changes that might affect C9ORF95/NMRK1 expression in disease states
The study of scleroderma patients presented in the literature provides a methodological template for such investigations:
| Clinical Parameter | SSc (n=12) | Healthy volunteers (n=8) |
|---|---|---|
| Age (years) | 50.9 ± 4.2 | 49.8 ± 5.0 |
| Sex | F10/M2 | F6/M2 |
| Disease duration (years) | 3.4 ± 0.7 | N.A. |
| Modified Rodnan Skin Score | 14.3 ± 2.6 | N.A. |
This demographic matching approach should be employed when studying C9ORF95/NMRK1 in disease contexts to control for confounding variables .
What knockout/knockdown strategies are most effective for studying C9ORF95/NMRK1 function?
For effective genetic manipulation of C9ORF95/NMRK1, researchers should consider multiple complementary approaches:
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CRISPR/Cas9 Gene Editing: Design guide RNAs targeting early exons of the C9ORF95 gene, preferably creating frameshift mutations that result in complete protein loss. Validate knockout efficiency through sequencing, Western blotting, and enzyme activity assays.
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siRNA/shRNA Knockdown: For transient studies or when complete knockout is lethal, design RNA interference targeting conserved regions of the C9ORF95 transcript. Validate knockdown efficiency using qPCR and Western blotting.
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Inducible Systems: Consider doxycycline-inducible knockdown/knockout systems for temporal control of C9ORF95 expression, particularly useful for studying developmental or time-dependent processes.
When validating genetic manipulation, researchers should analyze NAD+ pathway metabolites using metabolomics approaches to confirm functional consequences of C9ORF95/NMRK1 reduction or elimination. Complementation studies with wild-type or mutant C9ORF95 can provide additional validation and functional insights.
How can researchers distinguish between the activities of C9ORF95/NMRK1 and other nicotinamide riboside kinases?
Distinguishing between the activities of C9ORF95/NMRK1 and other nicotinamide riboside kinases requires careful experimental design:
Researchers should use recombinant proteins of high purity (>90% as determined by SDS-PAGE) to ensure accurate comparative analyses between different kinases. Careful attention to reaction conditions is essential, as pH, ionic strength, and cofactor concentrations may differentially affect the activity of different kinases.
What are the challenges in studying post-translational modifications of C9ORF95/NMRK1?
Investigating post-translational modifications (PTMs) of C9ORF95/NMRK1 presents several technical challenges:
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Low Abundance: As a metabolic enzyme, C9ORF95/NMRK1 may be expressed at relatively low levels in many tissues, making enrichment strategies necessary for PTM detection.
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Identification of Modification Sites: Comprehensive mass spectrometry approaches are required to identify specific residues subject to phosphorylation, acetylation, ubiquitination, or other modifications.
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Functional Significance: Determining how PTMs affect enzyme activity requires site-directed mutagenesis to create modification-mimicking or modification-resistant forms of the protein.
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Regulation Dynamics: Temporal analysis of PTM patterns under various cellular conditions requires kinetic studies with synchronized cells or time-course experiments.
For robust PTM analysis, researchers should consider:
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Immunoprecipitation with specific antibodies followed by mass spectrometry
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Phospho-specific antibody development for key regulatory sites
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In vitro modification assays using purified kinases/acetyltransferases and recombinant C9ORF95/NMRK1
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Bioinformatic prediction of potential modification sites based on consensus sequences and structural accessibility
What bioinformatic approaches are useful for analyzing C9ORF95/NMRK1 in genomic datasets?
For comprehensive bioinformatic analysis of C9ORF95/NMRK1, researchers should employ multiple computational strategies:
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Chromatin Accessibility Analysis: Use tools like MACS2 for peak-calling in ATAC-seq data and diffReps for identifying differential chromatin accessibility between experimental conditions, as demonstrated in epigenetic studies .
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Literature Mining: Tools like IRIDESCENT can identify co-occurrences of C9ORF95/NMRK1 with relevant keywords (e.g., fibrosis, angiogenesis) in scientific literature, facilitating hypothesis generation .
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Haplotype Analysis: For genetic studies, use genome-wide association data to phase haplotypes at the C9ORF95 locus, enabling investigation of potential founder effects similar to those observed with C9ORF72 .
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Statistical Methods: Employ appropriate statistical tests based on data distribution; Mann-Whitney U test for non-parametric comparisons between groups and paired t-tests for before/after comparisons within the same subjects .
When analyzing sequencing data, researchers should apply rigorous quality control measures, including filtering improperly-paired alignments and those with mapping quality less than 4 using tools like SAMtools . Blacklisted genomic regions should be removed from peak analysis to prevent false positives .
How should researchers address contradictory findings regarding C9ORF95/NMRK1 function?
When confronted with contradictory findings in the literature regarding C9ORF95/NMRK1 function, researchers should implement a systematic approach:
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Methodological Comparison: Carefully analyze experimental conditions, cell types/tissues, and analytical techniques used in conflicting studies to identify potential sources of variability.
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Replication Studies: Design experiments that specifically address contradictions by incorporating conditions from both conflicting studies while maintaining consistent internal controls.
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Multi-omics Integration: Combine transcriptomic, proteomic, and metabolomic approaches to provide a more comprehensive view of C9ORF95/NMRK1 function across different contexts.
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Genetic Background Consideration: Evaluate whether genetic background differences might explain functional variations observed between studies, particularly in animal models or different cell lines.
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Isoform-Specific Analysis: Investigate whether alternative splicing or protein isoforms of C9ORF95/NMRK1 might exhibit different functional properties, potentially explaining apparently contradictory findings.
For publications addressing contradictions, researchers should present both supporting and contradicting evidence in a balanced manner, offering potential explanations for discrepancies and designing experiments specifically to resolve these conflicts.
What emerging technologies might advance C9ORF95/NMRK1 research?
Several cutting-edge technologies hold promise for advancing C9ORF95/NMRK1 research:
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Single-Cell Metabolomics: Emerging techniques for measuring metabolites at the single-cell level could reveal cell-type-specific roles of C9ORF95/NMRK1 in NAD+ metabolism that are masked in bulk tissue analyses.
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CRISPR Activation/Interference Screens: CRISPRa/CRISPRi libraries targeting regulatory elements of C9ORF95/NMRK1 could identify novel transcriptional regulators controlling its expression in different contexts.
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Spatial Transcriptomics/Proteomics: These technologies could map C9ORF95/NMRK1 expression patterns with subcellular resolution, potentially revealing specialized functions in distinct cellular compartments.
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Protein-Protein Interaction Mapping: BioID or APEX2 proximity labeling combined with mass spectrometry could identify novel interaction partners of C9ORF95/NMRK1, suggesting previously unrecognized functions.
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Structural Biology Advances: Cryo-EM and integrative structural biology approaches could provide atomic-resolution insights into substrate binding and catalytic mechanisms, facilitating rational drug design targeting C9ORF95/NMRK1.
Researchers should consider incorporating these emerging technologies into their experimental design while maintaining connections to established methodologies to ensure continuity with the existing knowledge base.
What are the most significant unresolved questions regarding C9ORF95/NMRK1 biology?
Despite advances in understanding C9ORF95/NMRK1, several fundamental questions remain unresolved:
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Physiological Regulation: The mechanisms controlling C9ORF95/NMRK1 expression and activity under different metabolic states remain poorly characterized. How do factors like redox status, energy balance, and circadian rhythms impact its function?
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Subcellular Localization: The precise subcellular distribution of C9ORF95/NMRK1 and how this might change under different conditions or in disease states requires further investigation.
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Substrate Preference in vivo: While in vitro studies have characterized substrate specificity, the preferred physiological substrates in different tissues and metabolic states remain uncertain.
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Isoform-Specific Functions: Whether alternative splicing generates functional variants of C9ORF95/NMRK1 with distinct properties or tissue-specific roles needs systematic investigation.
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Therapeutic Potential: The possibility of modulating C9ORF95/NMRK1 activity as a therapeutic strategy for conditions involving NAD+ metabolism dysregulation remains largely unexplored.
Addressing these questions will require integrative approaches combining genetic manipulation, biochemical analysis, and in vivo modeling in relevant physiological and pathological contexts. Researchers should design experiments that specifically target these knowledge gaps while building upon the solid foundation of existing C9ORF95/NMRK1 characterization.
Product Science Overview
The C9orf95 gene is composed of several exons and introns, which are segments of DNA that are transcribed into RNA. The exons are the coding regions that are ultimately translated into the protein, while the introns are non-coding regions that are spliced out during RNA processing. The protein encoded by C9orf95 is a recombinant protein, meaning it is produced through recombinant DNA technology, which involves inserting the gene into a host organism (such as bacteria) to produce the protein in large quantities.
Although the precise biological function of C9orf95 is not fully understood, it is thought to be involved in various cellular processes, including cell signaling, growth, and differentiation. Proteins encoded by ORFs like C9orf95 are often studied to understand their role in health and disease. Research on C9orf95 may provide insights into its potential involvement in certain medical conditions or its utility as a biomarker for disease.
Recombinant proteins like C9orf95 are valuable tools in scientific research and medicine. They can be used in various applications, including:
- Functional Studies: Researchers can study the function of C9orf95 by observing the effects of its overexpression or knockdown in cell lines or animal models.
- Drug Development: Understanding the role of C9orf95 in cellular processes can aid in the development of new therapeutic targets for diseases.
- Diagnostic Tools: Recombinant proteins can be used to develop diagnostic assays for detecting diseases or monitoring treatment responses.
