CHRAC1 (Q9NRG0) – Chromatin Accessibility Complex Subunit 1 in Human OpenAI o3-deep-research-2025-06-26 113 citations 2025-11-04T03:14:15.859762

CHRAC1 (Q9NRG0) – Chromatin Accessibility Complex Subunit 1 in Human

Overview and Key Concepts

CHRAC1 (Chromatin Accessibility Complex subunit 1, also known as CHRAC15 or YCL1) is a small (~15 kDa, 131 amino acids) protein that plays a structural role in chromatin remodeling and DNA replication. It was first identified as part of the CHRomatin Accessibility Complex (CHRAC), an ATP-dependent chromatin-remodeling complex originally discovered in Drosophila and later in mammals (jeccr.biomedcentral.com). CHRAC1 contains a histone-fold motif, a structural domain through which it heterodimerizes with another histone-fold protein, typically POLE3 (also called CHRAC17) (thebiogrid.org) (jeccr.biomedcentral.com). This CHRAC1–POLE3 pair is analogous to histone H2A–H2B dimers in structure (pmc.ncbi.nlm.nih.gov) and is a non-enzymatic accessory module within larger complexes. The CHRAC1/POLE3 heterodimer does not itself catalyze reactions, but it binds DNA and histones and is essential for the activity of the complexes it belongs to (pmc.ncbi.nlm.nih.gov) (pubmed.ncbi.nlm.nih.gov).

CHRAC1 is encoded on chromosome 8 (8q24.3) and is expressed in the nucleus in most human cells. It is predicted to be intracellular and indeed localizes to the nucleoplasm (chromatin-rich nuclear space) (www.proteinatlas.org). Consistent with a fundamental role in genome maintenance, CHRAC1 shows low tissue specificity, meaning it is expressed across a wide range of cell types (www.proteinatlas.org). In summary, CHRAC1 is a conserved chromatin-associated protein that serves as a structural subunit in critical nuclear complexes for DNA packaging and replication.

Molecular Function and Structure

Histone-Fold Protein and Heterodimer Formation: CHRAC1 belongs to a family of small histone-fold proteins that function in pairs. It forms a tight heterodimer with POLE3 (also known as CHRAC17), another histone-fold protein (thebiogrid.org) (jeccr.biomedcentral.com). This dimer resembles the histone H2A–H2B dimer in both structure and DNA-binding mode (pmc.ncbi.nlm.nih.gov). Structural modeling and alignments have shown that the Drosophila CHRAC-14/16 heterodimer (homologous to human CHRAC1/POLE3) superimposes onto an H2A–H2B dimer bound to DNA (pmc.ncbi.nlm.nih.gov), highlighting the evolutionary repurposing of histone-like modules in chromatin machinery. The CHRAC1–POLE3 dimer has a positively charged surface that can bind directly to double-stranded DNA (pmc.ncbi.nlm.nih.gov). This DNA-binding ability is unique among subunits of replicative polymerases and remodelers – in fact, inclusion of the histone-fold pair allows the holoenzymes containing CHRAC1 to grip nucleic acids more stably (pmc.ncbi.nlm.nih.gov). Both yeast and human studies have demonstrated that these subunits also associate with core histones: for example, the yeast homolog (Dpb4) can be chemically crosslinked to histone proteins on DNA (pmc.ncbi.nlm.nih.gov). This suggests the heterodimer can bridge DNA and nucleosomes, stabilizing protein–DNA interactions during chromatin remodeling and replication.

Association with Complexes: CHRAC1’s primary function is as a non-catalytic subunit of larger chromatin-associated complexes. It is a dedicated component of the CHRAC/ACF family of ISWI-type chromatin remodelers. In humans, the canonical ACF (ATP-utilizing Chromatin Assembly and Remodeling Factor) complex consists of the SNF2H ATPase (SMARCA5) and the large accessory subunit ACF1 (BAZ1A) (jeccr.biomedcentral.com). When CHRAC1 and POLE3 are incorporated, this forms the four-subunit CHRAC complex (consisting of SMARCA5, BAZ1A, CHRAC1, and POLE3) (jeccr.biomedcentral.com) (jeccr.biomedcentral.com). CHRAC1 directly interacts with ACF1 (BAZ1A) via its histone-fold partner, and this interaction is essential for the remodeler’s function (thebiogrid.org). Notably, CHRAC1 is historically referred to as “p15”, and POLE3 as “p17,” reflecting their molecular weights (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). These two subunits form a stable sub-complex that can attach to different machines: they are part of CHRAC, and intriguingly, one of them (POLE3/p17) is also a subunit of the DNA polymerase ε complex (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Polymerase ε (Pol ε), the leading-strand DNA polymerase in replication, has four subunits; two are large enzymatic subunits, and two are small histone-fold subunits (POLE3 and POLE4, historically p17 and p12) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Importantly, the p17/CHRAC17 subunit is shared between Pol ε and CHRAC in mammals (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov), whereas CHRAC1 (p15) is unique to the chromatin remodeling complex. This shared subunit reflects a conserved theme: in yeast, the Pol ε accessory subunit Dpb4 is also part of an ISWI remodeling complex (yeast Isw2 complex) (jeccr.biomedcentral.com). The presence of common subunits suggests functional coupling between replication and chromatin remodeling machineries.

Biochemical Activity: Although CHRAC1 itself has no enzymatic activity (it does not hydrolyze ATP or modify substrates), it is critical for the activity of its host complexes. In the context of ACF/CHRAC, CHRAC1–POLE3 acts as a modulatory module that enhances nucleosome remodeling. A key study in Molecular Cell (2004) demonstrated that adding the CHRAC1/POLE3 (p15/p17) pair to the ACF complex greatly facilitates nucleosome sliding and assembly on DNA (jeccr.biomedcentral.com) (jeccr.biomedcentral.com). In this study, the reconstituted human CHRAC complex showed more efficient ATP-dependent repositioning of nucleosomes than the two-subunit ACF core alone, indicating that CHRAC1 and its partner improve the remodeler’s ability to mobilize histone octamers (jeccr.biomedcentral.com) (jeccr.biomedcentral.com). The CHRAC1–POLE3 heterodimer is thought to nucleate contacts with the nucleosomal DNA or histones, aiding the SNF2H motor in gripping and moving nucleosomes (thebiogrid.org) (jeccr.biomedcentral.com). Direct interaction of the CHRAC1/POLE3 module with the ACF1 subunit is required for this stimulatory effect (thebiogrid.org), suggesting CHRAC1 acts as an adapter linking the ATPase complex to the nucleosome substrate.

Within the Pol ε holoenzyme, the analogous histone-fold pair (POLE3–POLE4) performs a different but related role. It has been shown to function as a histone chaperone – specifically binding histones H3–H4 and facilitating their proper assembly behind the replication fork (pubmed.ncbi.nlm.nih.gov). In a 2018 biochemical study, the POLE3/POLE4 subcomplex of Pol ε was found to selectively bind H3–H4 and promote replication-coupled nucleosome assembly, thereby maintaining chromatin integrity during DNA synthesis (pubmed.ncbi.nlm.nih.gov). By analogy, the CHRAC1–POLE3 dimer (which shares the POLE3 component) likely has a similar affinity for histones or DNA. In Pol ε, these small subunits also confer high affinity for double-stranded DNA, making Pol ε unique among DNA polymerases in its ability to stay attached to dsDNA without external clamps (pmc.ncbi.nlm.nih.gov). This property is crucial for holding and organizing DNA as the polymerase synthesizes the new strand. While CHRAC1 is not part of Pol ε, the shared architecture implies that CHRAC1’s presence in the CHRAC complex equips the chromatin remodeler with a DNA/histone-binding module analogous to Pol ε’s, reinforcing the idea that CHRAC1’s primary function is structural tethering: it helps position and stabilize the larger enzymatic subunits on chromatin substrates.

Biological Processes and Pathways

Chromatin Remodeling and Nucleosome Positioning: The defining role of CHRAC1 is in chromatin remodeling. CHRAC1-containing complexes (ACF/CHRAC) use the energy of ATP (via the ISWI ATPase SNF2H) to reposition nucleosomes along DNA. CHRAC was originally purified (in Drosophila) by its ability to increase chromatin accessibility – chromatin reconstituted with CHRAC was more easily cut by restriction enzymes (pmc.ncbi.nlm.nih.gov). This activity reflects the complex’s ability to slide nucleosomes and expose DNA regions. In addition, CHRAC can drive the formation of regularly spaced nucleosome arrays in vitro, organizing chromatin structure (pmc.ncbi.nlm.nih.gov). In general, ACF and CHRAC function as nucleosome spacing factors, converting irregular nucleosome distributions into evenly spaced, higher-order chromatin – a process often associated with repressive chromatin formation (jeccr.biomedcentral.com) (jeccr.biomedcentral.com). CHRAC1 is an essential part of this process: when CHRAC1/POLE3 are bound to ACF, the complex is optimized for sliding nucleosomes along DNA and assembling histones onto DNA in an orderly manner (jeccr.biomedcentral.com) (jeccr.biomedcentral.com). This is corroborated by experiments showing that removing or mutating the CHRAC1–POLE3 subunits impairs ATP-dependent nucleosome mobilization by ACF (jeccr.biomedcentral.com). Thus, CHRAC1’s broader structural role is to ensure chromatin remodelers can effectively reposition nucleosomes, which impacts DNA accessibility for transcription, replication, and repair.

Because of this role, CHRAC1 influences transcriptional regulation indirectly. By helping position nucleosomes, CHRAC1-containing complexes can either repress or activate gene expression depending on context. For instance, well-spaced nucleosome arrays formed by ACF/CHRAC are often linked to transcriptional repression (stabilizing a more condensed chromatin state) (jeccr.biomedcentral.com). However, chromatin remodelers can also enable transcription by clearing or sliding nucleosomes at promoters. A recent study provides a concrete example: CHRAC1 was found to interact with the transcriptional co-activator YAP (Yes-associated protein) and promote YAP-driven gene expression in cancer cells (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In this 2024 study (PeerJ, Jan 10 2024), Li et al. showed that CHRAC1 physically associates with YAP and is required for efficient transcription of YAP target oncogenes in breast and cervical cancer cells (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). CHRAC1 depletion led to reduced YAP target gene expression, suggesting that CHRAC1’s chromatin-remodeling function may facilitate opening of chromatin at YAP-regulated loci to enhance transcription (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). This illustrates how CHRAC1, through the CHRAC complex, can participate in specific gene regulatory programs – not by sequence-specific DNA binding, but by modulating nucleosome positioning at the behest of other DNA-binding factors.

DNA Replication and Epigenetic Maintenance: CHRAC1 is also important in the context of DNA replication. While it is not a core component of the replication fork machinery, its relationships to Pol ε and chromatin assembly tie it closely to replication processes. The leading-strand DNA polymerase ε, which synthesizes new DNA during S-phase, contains a histone-fold subcomplex (POLE3–POLE4) related to CHRAC1–POLE3. This subcomplex chaperones histones and helps re-deposit them onto newly replicated DNA (pubmed.ncbi.nlm.nih.gov). Because POLE3 is common to both Pol ε and CHRAC, there appears to be a division of labor: Pol ε (with POLE3–POLE4) handles immediate nucleosome reassembly, while CHRAC (with CHRAC1–POLE3) may assist in specialized contexts of replication, such as heterochromatin. Indeed, evidence suggests CHRAC is recruited during replication of heterochromatic regions to ensure proper chromatin is reformed. Two core components of CHRAC (SNF2H and ACF1) have been observed to colocalize with heterochromatin protein HP1β and with BrdU (newly synthesized DNA) during late S phase (pmc.ncbi.nlm.nih.gov). Late S-phase is when pericentromeric heterochromatin is replicated, and this colocalization indicates CHRAC is present at replication sites of silent repetitive DNA. Researchers propose that the shared POLE3/p17 subunit might serve as a molecular link, targeting both Pol ε and CHRAC to replicating heterochromatic regions (pmc.ncbi.nlm.nih.gov). In this model, Pol ε synthesizes DNA while CHRAC remodels nucleosomes in tandem, thereby maintaining the epigenetic state (silenced or open) of the DNA after replication (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Experimental support comes from yeast: disruption of Dpb4 (the yeast POLE3 homolog shared with yeast CHRAC) causes defects in inheriting silent chromatin at telomeres, showing equal parts loss and gain of silencing (pmc.ncbi.nlm.nih.gov). Similarly, in human cells, Pol ε and CHRAC cooperate to replicate through dense chromatin – Pol ε’s small subunits and CHRAC can both bind histones/DNA, helping to propagate chromatin structure onto daughter strands (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Moreover, cell-free replication assays have demonstrated a direct role for CHRAC in assisting DNA synthesis through chromatin: for example, adding purified human CHRAC to an in vitro replication system allowed more efficient duplication of nucleosomal DNA by repositioning nucleosomes at a replication origin that would otherwise block replication initiation (pmc.ncbi.nlm.nih.gov). This indicates CHRAC1’s complex actively helps overcome nucleosomal barriers during replication, ensuring that DNA replication progresses and that nucleosomes are properly reassembled afterward.

DNA Repair and Other Pathways: There is also evidence implicating CHRAC1-containing complexes in DNA damage responses. The ACF1–SNF2H remodeler (with which CHRAC1 associates in CHRAC) is known to be recruited to DNA double-strand breaks and contribute to repair. BAZ1A (ACF1) and SNF2H help load repair factors at breaks and promote non-homologous end joining, and loss of either makes cells hypersensitive to DNA damage (jeccr.biomedcentral.com) (jeccr.biomedcentral.com). CHRAC1 has not been singled out in these studies, but as part of the same complex it likely participates in chromatin relaxation around DNA breaks, facilitating repair factor access. Additionally, CHRAC1’s partner POLE3 has been linked to stabilizing replication forks under stress – recent work showed that loss of POLE3/POLE4 leads to replication gaps and hypersensitivity to PARP inhibitors (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). While these studies focused on Pol ε’s subunits, they underscore the importance of the histone-fold modules in maintaining genome stability. By extension, CHRAC1 (through CHRAC) contributes to safeguarding genome integrity during both routine DNA duplication and in response to genotoxic stress.

In summary, CHRAC1 functions at the crossroads of several fundamental pathways: it is a key adapter in ATP-dependent chromatin remodeling, it supports DNA replication-coupled chromatin assembly, and it likely plays auxiliary roles in transcription regulation and DNA repair by modulating nucleosome behavior. All these roles center on managing nucleosome positioning and stability, highlighting CHRAC1’s primary role as a structural keeper of chromatin states.

Cellular Localization

CHRAC1 is an intracellular, nuclear protein. It lacks any signal peptides or transmembrane domains, and consistent with its role in chromatin dynamics, it localizes to the cell nucleus, predominantly in the nucleoplasm (the chromatin-containing portion of the nucleus) (www.proteinatlas.org). High-resolution microscopy and cell fractionation experiments support this: CHRAC1 is found in the chromatin-bound fraction of nuclear extracts and co-localizes with known chromatin markers. For instance, as noted, components of the CHRAC complex including SNF2H and ACF1 (which would carry CHRAC1 with them) concentrate at pericentromeric heterochromatin foci marked by HP1 during S phase (pmc.ncbi.nlm.nih.gov). Additionally, Pol ε (which shares the POLE3 subunit) localizes to replication foci that overlap with sites of DNA synthesis (PCNA/BrdU foci) in S phase (pmc.ncbi.nlm.nih.gov), and by proxy CHRAC may be present in those same foci to assist nucleosome assembly. Immunofluorescence studies in cancer cells also show CHRAC1 nuclear localization. In a recent study, CHRAC1 and YAP were observed to interact in the nucleus; CHRAC1 showed punctate nuclear staining and co-localized with YAP in transcriptionally active nuclear regions (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). No evidence exists for CHRAC1 functioning outside the nucleus—it is fundamentally tied to chromatin, which is a nuclear entity. Therefore, CHRAC1 carries out its function in the nuclear chromatin context, at sites where DNA is being read, copied, or repaired.

Recent Developments and Clinical Significance

Emerging research, particularly in the last few years, has highlighted CHRAC1’s relevance in disease (notably cancer) and its potential as a therapeutic target. The CHRAC1 gene is located at 8q24.3, a chromosomal region frequently amplified in cancers. A 2014 oncogenomic study (Mahmood et al., Carcinogenesis 2014) identified CHRAC1 as a driver gene within the 8q24.3 amplicon in breast cancer (jeccr.biomedcentral.com). In that RNA interference screen, CHRAC1 was one of a handful of genes whose knockdown impaired the proliferation and survival of breast cancer cells harboring the 8q24 amplification (jeccr.biomedcentral.com) (jeccr.biomedcentral.com). This indicates that overexpression of CHRAC1 can confer a growth advantage to tumor cells. Expanding on this, a pan-cancer analysis (2021) found that CHRAC1 and its complex members are frequently upregulated or amplified in multiple tumor types. Transcriptomic data from The Cancer Genome Atlas (TCGA) show concurrent overexpression of BAZ1A (ACF1), CHRAC1, and POLE3 in diverse cancers including esophageal carcinoma, hepatocellular carcinoma, gastric cancer, and breast carcinoma (jeccr.biomedcentral.com) (jeccr.biomedcentral.com). In many tumors, at least two subunits of the CHRAC complex are aberrantly co-amplified or overexpressed, suggesting selective pressure to boost CHRAC activity in cancer cells (jeccr.biomedcentral.com) (jeccr.biomedcentral.com). This makes sense in light of CHRAC1’s function: increased chromatin remodeling capacity might enable cancer cells to more easily reprogram gene expression or tolerate replication stress. For example, CHRAC1 was found to be upregulated in cisplatin-resistant ovarian cancer cell lines and in metastatic lung tumors, with CHRAC1 knockdown reducing migration and invasion of those cancer cells (pmc.ncbi.nlm.nih.gov). These observations imply CHRAC1 contributes to therapy resistance and aggressive phenotypes, possibly by altering chromatin to activate survival pathways.

One of the most striking recent findings is CHRAC1’s connection to the Hippo signaling pathway via YAP. As mentioned, PeerJ (2024) reported that CHRAC1 physically interacts with YAP and enhances the transcription of YAP target genes, which include many pro-proliferative and anti-apoptotic factors (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Functionally, silencing CHRAC1 in breast and cervical cancer models suppressed tumor cell proliferation and tumor growth in vivo, correlating with reduced expression of YAP-driven oncogenes (pmc.ncbi.nlm.nih.gov). Clinically, CHRAC1 protein levels were found to be elevated in patient tumor samples (breast and cervical cancers), and high CHRAC1 expression was associated with poorer patient survival, higher tumor grade, and increased metastasis (pmc.ncbi.nlm.nih.gov). This positions CHRAC1 as not only a biomarker of aggressive disease but also a potential therapeutic target. If CHRAC1 is required for the oncogenic gene expression program (like YAP’s program), drugs that inhibit the CHRAC complex or disrupt CHRAC1–YAP interaction might curb tumor growth. Indeed, interest in targeting chromatin remodelers in cancer is growing, and CHRAC1 lies at the intersection of chromatin regulation and oncogenic signaling.

Beyond cancer, CHRAC1’s role in fundamental processes means that any dysregulation could have wide effects. As a coregulator of chromatin structure, CHRAC1 might be involved in disorders of genome instability or developmental epigenetic diseases, though these have not been well characterized yet. It’s worth noting that knocking out the mouse homolog of CHRAC1 has not been widely reported in literature – given its role, a complete CHRAC1 knockout might be embryonic lethal or cause severe proliferation defects, which would align with it being a housekeeping gene. Consortium databases do indicate CHRAC1 is essential for cell viability in various cell lines (for instance, CRISPR screens list CHRAC1 among genes needed for growth in culture (jeccr.biomedcentral.com) (jeccr.biomedcentral.com)), reinforcing that it is not easily dispensable.

Expert Commentary and Concluding Remarks

CHRAC1 exemplifies how small structural proteins can have outsized importance in genome regulation. As part of the ISWI-family chromatin remodelers, it alters the physical arrangement of nucleosomes, which is a fundamental mechanism for controlling access to DNA (jeccr.biomedcentral.com) (jeccr.biomedcentral.com). Experts note that the sharing of a subunit between a chromatin remodeler and a DNA polymerase is a remarkable evolutionary solution to couple nucleosome dynamics with DNA replication (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Dr. Zachary Pursell and Dr. Thomas Kunkel, in their comprehensive 2008 review of DNA Pol ε, highlighted the mystery of “why two entirely separate enzymatic activities should have such a shared subunit” (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). One hypothesis they offer is that the shared histone-fold subunit (POLE3/CHRAC17) could serve as a bridge between replication and chromatin assembly, ensuring that as the replication fork progresses, the chromatin structure is re-established immediately and correctly (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). CHRAC1, partnering in the CHRAC complex, appears to complement this by providing the chromatin remodeling horsepower needed especially in tightly packed regions.

Chromatin biology experts like Dr. Philippe Clapier have also underscored the importance of histone-fold proteins in chromatin transactions. In a 2017 review, Clapier et al. noted that histone-fold subunits (like CHRAC1 and its partners) not only serve as structural components but can act as “accessory DNA-binding modules” that increase the efficiency and targeting of remodeling enzymes (pmc.ncbi.nlm.nih.gov). The case of CHRAC1 validates this: without directly binding specific DNA sequences or catalyzing reactions, it nonetheless directs where and how the energy of SNF2H is applied on nucleosomes.

From a clinical perspective, cancer researchers (e.g. in the 2021 JECCR review) point out that ISWI complexes such as CHRAC are emerging as critical drivers in oncogenesis when deregulated (jeccr.biomedcentral.com) (jeccr.biomedcentral.com). The simultaneous up-regulation of CHRAC1 and its complex members in tumors suggests a selective advantage, possibly allowing cancer cells to rapidly restructure their chromatin for tumor-promoting gene expression programs (jeccr.biomedcentral.com) (jeccr.biomedcentral.com). The fact that CHRAC1 has been confirmed as a key gene in a recurrent breast cancer amplification (jeccr.biomedcentral.com) and that its loss impairs tumor growth (pmc.ncbi.nlm.nih.gov) makes it an exciting candidate for targeted research. Therapies that inhibit chromatin remodelers (sometimes termed “chromatin therapeutics”) could potentially exploit the cancer-specific dependency on CHRAC1. However, given CHRAC1’s essential role in normal cells, such approaches would require precision to avoid toxicity.

In conclusion, CHRAC1 is a multifaceted chromatin protein whose primary role is to support and enhance the machines that reorganize and replicate our genome. It anchors remodelers to nucleosomes, helping slide and assemble histones, and intersects with the replication fork to maintain chromatin continuity. Its activity is confined to the nucleus, where it safeguards genomic information flow – from DNA packaging to gene expression and replication. Ongoing research, especially in oncology, continues to shed light on CHRAC1’s importance. As our understanding grows, CHRAC1 stands as a compelling example of how even the smallest protein components of chromatin complexes can have broad impacts on cell fate and function, making it both a fundamental piece of the chromatin infrastructure and a potential node to target in diseases of genome dysregulation.

References:

Citations

  1. AnnotationURLCitation(end_index=705, start_index=498, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=Chromatin%20remodeling%20complexes%20containing%20the,complexes%20via%20association%20with%20different')
  2. AnnotationURLCitation(end_index=1066, start_index=879, title='The histone-fold protein complex CHRAC-15/17 enhances nucleosome sliding and assembly mediated by ACF. | BioGRID', type='url_citation', url='https://thebiogrid.org/114419/publication/the-histone-fold-protein-complex-chrac-1517-enhances-nucleosome-sliding-and-assembly-mediated-by-acf.html#:~:text=Read%20More')
  3. AnnotationURLCitation(end_index=1239, start_index=1067, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=match%20at%20L373%20Furthermore%2C%20CHRAC1,CHRAC%20complex%20%5B63')
  4. AnnotationURLCitation(end_index=1418, start_index=1316, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=,DNA%20Interaction')
  5. AnnotationURLCitation(end_index=1780, start_index=1652, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=match%20at%20L914%20%CE%B5%20and,linked%20to')
  6. AnnotationURLCitation(end_index=1950, start_index=1781, title='POLE3-POLE4 Is a Histone H3-H4 Chaperone that Maintains Chromatin Integrity during DNA Replication - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/30217558/#:~:text=Maintenance%20of%20epigenetic%20integrity%20relies,to%20selectively%20bind%20to%20histones')
  7. AnnotationURLCitation(end_index=2303, start_index=2161, title='CHRAC1 protein expression summary - The Human Protein Atlas', type='url_citation', url='https://www.proteinatlas.org/ENSG00000104472-CHRAC1#:~:text=Subcellular%20location,i%7D%20Low%20tissue%20specificity')
  8. AnnotationURLCitation(end_index=2604, start_index=2462, title='CHRAC1 protein expression summary - The Human Protein Atlas', type='url_citation', url='https://www.proteinatlas.org/ENSG00000104472-CHRAC1#:~:text=Subcellular%20location,i%7D%20Low%20tissue%20specificity')
  9. AnnotationURLCitation(end_index=3287, start_index=3037, title='The histone-fold protein complex CHRAC-15/17 enhances nucleosome sliding and assembly mediated by ACF. | BioGRID', type='url_citation', url='https://thebiogrid.org/114419/publication/the-histone-fold-protein-complex-chrac-1517-enhances-nucleosome-sliding-and-assembly-mediated-by-acf.html#:~:text=%5BACF%5D%29%20associates%20with%20histone,17%20interacts%20with%20another')
  10. AnnotationURLCitation(end_index=3460, start_index=3288, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=match%20at%20L373%20Furthermore%2C%20CHRAC1,CHRAC%20complex%20%5B63')
  11. AnnotationURLCitation(end_index=3650, start_index=3548, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=,DNA%20Interaction')
  12. AnnotationURLCitation(end_index=3927, start_index=3825, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=,DNA%20Interaction')
  13. AnnotationURLCitation(end_index=4253, start_index=4125, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=match%20at%20L914%20%CE%B5%20and,linked%20to')
  14. AnnotationURLCitation(end_index=4596, start_index=4468, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=match%20at%20L914%20%CE%B5%20and,linked%20to')
  15. AnnotationURLCitation(end_index=4950, start_index=4795, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=match%20at%20L922%20propagate%20a,%CE%B5%20through%20Dpb4%2C%20with%20a')
  16. AnnotationURLCitation(end_index=5695, start_index=5504, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=BAZ1A%20forms%20ACF%20complexes%20together,the%20ACF%20complex%2C%20BAZ1A%20stimulates')
  17. AnnotationURLCitation(end_index=6007, start_index=5833, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=%28SMARCA1%2F5%20and%20RSF1%29%2C%20ACF,5%20%28SMARCA1%2F5%2C%20BAZ2B')
  18. AnnotationURLCitation(end_index=6180, start_index=6008, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=match%20at%20L373%20Furthermore%2C%20CHRAC1,CHRAC%20complex%20%5B63')
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  20. AnnotationURLCitation(end_index=6849, start_index=6688, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=remodeling%20complexes%20came%20with%20the,of%20human%20Pol%20%CE%B5%2C%20p12')
  21. AnnotationURLCitation(end_index=6978, start_index=6850, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=match%20at%20L914%20%CE%B5%20and,linked%20to')
  22. AnnotationURLCitation(end_index=7337, start_index=7180, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=subunits%2C%20called%20p15%20and%20p17,of%20human%20Pol%20%CE%B5%2C%20p12')
  23. AnnotationURLCitation(end_index=7494, start_index=7338, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=homology%20to%20the%20unique%20HFM,the%20two%20complexes%2C%20but%20this')
  24. AnnotationURLCitation(end_index=7870, start_index=7709, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=remodeling%20complexes%20came%20with%20the,of%20human%20Pol%20%CE%B5%2C%20p12')
  25. AnnotationURLCitation(end_index=8042, start_index=7871, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=purified%20CHRAC%20in%20multiple%20species,that%20the%20human%20p12%2Fp17%20heterodimer')
  26. AnnotationURLCitation(end_index=8291, start_index=8130, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=remodeling%20complexes%20came%20with%20the,of%20human%20Pol%20%CE%B5%2C%20p12')
  27. AnnotationURLCitation(end_index=8448, start_index=8292, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=homology%20to%20the%20unique%20HFM,the%20two%20complexes%2C%20but%20this')
  28. AnnotationURLCitation(end_index=8860, start_index=8673, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=together%20with%20Ioc2%20and%20Ioc4,activation%20until%20signal%20thresholds%20are')
  29. AnnotationURLCitation(end_index=9627, start_index=9455, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=match%20at%20L373%20Furthermore%2C%20CHRAC1,CHRAC%20complex%20%5B63')
  30. AnnotationURLCitation(end_index=9808, start_index=9628, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=Furthermore%2C%20CHRAC1%20and%20POLE3%20interaction,CHRAC%20complex%20%5B63')
  31. AnnotationURLCitation(end_index=10241, start_index=10069, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=match%20at%20L373%20Furthermore%2C%20CHRAC1,CHRAC%20complex%20%5B63')
  32. AnnotationURLCitation(end_index=10422, start_index=10242, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=Furthermore%2C%20CHRAC1%20and%20POLE3%20interaction,CHRAC%20complex%20%5B63')
  33. AnnotationURLCitation(end_index=10835, start_index=10585, title='The histone-fold protein complex CHRAC-15/17 enhances nucleosome sliding and assembly mediated by ACF. | BioGRID', type='url_citation', url='https://thebiogrid.org/114419/publication/the-histone-fold-protein-complex-chrac-1517-enhances-nucleosome-sliding-and-assembly-mediated-by-acf.html#:~:text=%5BACF%5D%29%20associates%20with%20histone,17%20interacts%20with%20another')
  34. AnnotationURLCitation(end_index=11008, start_index=10836, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=match%20at%20L373%20Furthermore%2C%20CHRAC1,CHRAC%20complex%20%5B63')
  35. AnnotationURLCitation(end_index=11368, start_index=11118, title='The histone-fold protein complex CHRAC-15/17 enhances nucleosome sliding and assembly mediated by ACF. | BioGRID', type='url_citation', url='https://thebiogrid.org/114419/publication/the-histone-fold-protein-complex-chrac-1517-enhances-nucleosome-sliding-and-assembly-mediated-by-acf.html#:~:text=%5BACF%5D%29%20associates%20with%20histone,17%20interacts%20with%20another')
  36. AnnotationURLCitation(end_index=11909, start_index=11740, title='POLE3-POLE4 Is a Histone H3-H4 Chaperone that Maintains Chromatin Integrity during DNA Replication - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/30217558/#:~:text=Maintenance%20of%20epigenetic%20integrity%20relies,to%20selectively%20bind%20to%20histones')
  37. AnnotationURLCitation(end_index=12299, start_index=12130, title='POLE3-POLE4 Is a Histone H3-H4 Chaperone that Maintains Chromatin Integrity during DNA Replication - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/30217558/#:~:text=Maintenance%20of%20epigenetic%20integrity%20relies,to%20selectively%20bind%20to%20histones')
  38. AnnotationURLCitation(end_index=12743, start_index=12615, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=match%20at%20L914%20%CE%B5%20and,linked%20to')
  39. AnnotationURLCitation(end_index=13842, start_index=13680, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=match%20at%20L879%20CHRAC%20was,disorganized%20nucleosomes%20formed%20in%20the')
  40. AnnotationURLCitation(end_index=14232, start_index=14060, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=CHRAC%20was%20initially%20purified%20from,disorganized%20nucleosomes%20formed%20in%20the')
  41. AnnotationURLCitation(end_index=14665, start_index=14458, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=Chromatin%20remodeling%20complexes%20containing%20the,complexes%20via%20association%20with%20different')
  42. AnnotationURLCitation(end_index=14857, start_index=14666, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=BAZ1A%20forms%20ACF%20complexes%20together,the%20ACF%20complex%2C%20BAZ1A%20stimulates')
  43. AnnotationURLCitation(end_index=15229, start_index=15057, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=match%20at%20L373%20Furthermore%2C%20CHRAC1,CHRAC%20complex%20%5B63')
  44. AnnotationURLCitation(end_index=15410, start_index=15230, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=Furthermore%2C%20CHRAC1%20and%20POLE3%20interaction,CHRAC%20complex%20%5B63')
  45. AnnotationURLCitation(end_index=15737, start_index=15565, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=match%20at%20L373%20Furthermore%2C%20CHRAC1,CHRAC%20complex%20%5B63')
  46. AnnotationURLCitation(end_index=16515, start_index=16308, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=Chromatin%20remodeling%20complexes%20containing%20the,complexes%20via%20association%20with%20different')
  47. AnnotationURLCitation(end_index=16975, start_index=16825, title='Chromatin accessibility complex subunit 1 enhances tumor growth by regulating the oncogenic transcription of YAP in breast and cervical cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10787542/#:~:text=In%20the%20current%20study%2C%20we,of%20YAP%20target%20genes%20in')
  48. AnnotationURLCitation(end_index=17152, start_index=16976, title='Chromatin accessibility complex subunit 1 enhances tumor growth by regulating the oncogenic transcription of YAP in breast and cervical cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10787542/#:~:text=Hippo%20pathway%2C%20thereby%20promoting%20tumorigenesis,YAP%20in%20breast%20and%20cervical')
  49. AnnotationURLCitation(end_index=17511, start_index=17361, title='Chromatin accessibility complex subunit 1 enhances tumor growth by regulating the oncogenic transcription of YAP in breast and cervical cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10787542/#:~:text=In%20the%20current%20study%2C%20we,of%20YAP%20target%20genes%20in')
  50. AnnotationURLCitation(end_index=17669, start_index=17512, title='Chromatin accessibility complex subunit 1 enhances tumor growth by regulating the oncogenic transcription of YAP in breast and cervical cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10787542/#:~:text=match%20at%20L53%20Hippo%20pathway%2C,YAP%20in%20breast%20and%20cervical')
  51. AnnotationURLCitation(end_index=18023, start_index=17873, title='Chromatin accessibility complex subunit 1 enhances tumor growth by regulating the oncogenic transcription of YAP in breast and cervical cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10787542/#:~:text=In%20the%20current%20study%2C%20we,of%20YAP%20target%20genes%20in')
  52. AnnotationURLCitation(end_index=18200, start_index=18024, title='Chromatin accessibility complex subunit 1 enhances tumor growth by regulating the oncogenic transcription of YAP in breast and cervical cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10787542/#:~:text=Hippo%20pathway%2C%20thereby%20promoting%20tumorigenesis,YAP%20in%20breast%20and%20cervical')
  53. AnnotationURLCitation(end_index=19122, start_index=18953, title='POLE3-POLE4 Is a Histone H3-H4 Chaperone that Maintains Chromatin Integrity during DNA Replication - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/30217558/#:~:text=Maintenance%20of%20epigenetic%20integrity%20relies,to%20selectively%20bind%20to%20histones')
  54. AnnotationURLCitation(end_index=19867, start_index=19702, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=Evidence%20from%20metazoan%20cells%20indicates,and%20BrdU%2C%20during%20S%20phase')
  55. AnnotationURLCitation(end_index=20352, start_index=20196, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=has%20been%20found%20in%20a,during%20which%20time%20heterochromatin%20is')
  56. AnnotationURLCitation(end_index=20690, start_index=20528, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=propagate%20a%20silenced%20state%2C%20or,%CE%B5%20through%20Dpb4%2C%20with%20a')
  57. AnnotationURLCitation(end_index=20847, start_index=20691, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=has%20been%20found%20in%20a,during%20which%20time%20heterochromatin%20is')
  58. AnnotationURLCitation(end_index=21225, start_index=21064, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=this%20region%20in%20opposition%20to,silencing%20and%20activation%20in%20this')
  59. AnnotationURLCitation(end_index=21606, start_index=21451, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=match%20at%20L922%20propagate%20a,%CE%B5%20through%20Dpb4%2C%20with%20a')
  60. AnnotationURLCitation(end_index=21769, start_index=21607, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=propagate%20a%20silenced%20state%2C%20or,%CE%B5%20through%20Dpb4%2C%20with%20a')
  61. AnnotationURLCitation(end_index=22305, start_index=22136, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=CHRAC%20may%20also%20contribute%2C%20directly,to%20rearrange%20the%20nucleosomes%20on')
  62. AnnotationURLCitation(end_index=23113, start_index=22932, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=In%20normal%20cells%2C%20BAZ1A%20is,strand%20breaks%20%28DSBs%29%20and%20DSB')
  63. AnnotationURLCitation(end_index=23300, start_index=23114, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=the%20KU70%2F80%20complex%20and%20formation,disruption%20of%20the%20ACF%20complex')
  64. AnnotationURLCitation(end_index=23856, start_index=23700, title='The loss of DNA polymerase epsilon accessory subunits POLE3–POLE4 leads to BRCA1-independent PARP inhibitor sensitivity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11229324/#:~:text=The%20loss%20of%20DNA%20polymerase,the%20levels%20of%20POLE3%2C%20POLE4')
  65. AnnotationURLCitation(end_index=23989, start_index=23857, title='The loss of DNA polymerase epsilon accessory subunits POLE3–POLE4 leads to BRCA1-independent PARP inhibitor sensitivity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11229324/#:~:text=Figure%201,the%20levels%20of%20POLE3%2C%20POLE4')
  66. AnnotationURLCitation(end_index=25213, start_index=25071, title='CHRAC1 protein expression summary - The Human Protein Atlas', type='url_citation', url='https://www.proteinatlas.org/ENSG00000104472-CHRAC1#:~:text=Subcellular%20location,i%7D%20Low%20tissue%20specificity')
  67. AnnotationURLCitation(end_index=25774, start_index=25609, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=Evidence%20from%20metazoan%20cells%20indicates,and%20BrdU%2C%20during%20S%20phase')
  68. AnnotationURLCitation(end_index=26088, start_index=25932, title='DNA Polymerase ε: A Polymerase Of Unusual Size (and Complexity) - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3694787/#:~:text=has%20been%20found%20in%20a,during%20which%20time%20heterochromatin%20is')
  69. AnnotationURLCitation(end_index=26575, start_index=26442, title='Chromatin accessibility complex subunit 1 enhances tumor growth by regulating the oncogenic transcription of YAP in breast and cervical cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10787542/#:~:text=activator%20Yes,were%20used%20to%20analyze%20the')
  70. AnnotationURLCitation(end_index=26726, start_index=26576, title='Chromatin accessibility complex subunit 1 enhances tumor growth by regulating the oncogenic transcription of YAP in breast and cervical cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10787542/#:~:text=In%20the%20current%20study%2C%20we,of%20YAP%20target%20genes%20in')
  71. AnnotationURLCitation(end_index=27593, start_index=27451, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=some%20oncogenic%20genes%20,resistant')
  72. AnnotationURLCitation(end_index=27919, start_index=27777, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=some%20oncogenic%20genes%20,resistant')
  73. AnnotationURLCitation(end_index=28101, start_index=27920, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=siRNA%20screen%20identifies%20RAD21%2C%20EIF3H%2C,2014%3B35%3A670%E2%80%9382')
  74. AnnotationURLCitation(end_index=28777, start_index=28593, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=Through%20TCGA%20database%20analysis%2C%20we,kinds%20of%20tumors%2C%20such%20as')
  75. AnnotationURLCitation(end_index=28962, start_index=28778, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=Through%20TCGA%20database%20analysis%2C%20we,kinds%20of%20tumors%2C%20such%20as')
  76. AnnotationURLCitation(end_index=29323, start_index=29139, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=Through%20TCGA%20database%20analysis%2C%20we,kinds%20of%20tumors%2C%20such%20as')
  77. AnnotationURLCitation(end_index=29506, start_index=29324, title='The emerging role of ISWI chromatin remodeling complexes in cancer | Journal of Experimental & Clinical Cancer Research | Full Text', type='url_citation', url='https://jeccr.biomedcentral.com/articles/10.1186/s13046-021-02151-x#:~:text=of%20abnormal%20copy%20numbers%20in,ESCC%2C%20while%20this%20region%20harbors')
  78. AnnotationURLCitation(end_index=30033, start_index=29903, title='Chromatin accessibility complex subunit 1 enhances tumor growth by regulating the oncogenic transcription of YAP in breast and cervical cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10787542/#:~:text=match%20at%20L108%20addition%2C%20CHRAC1,2021')
  79. AnnotationURLCitation(end_index=30647, start_index=30497, title='Chromatin accessibility complex subunit 1 enhances tumor growth by regulating the oncogenic transcription of YAP in breast and cervical cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10787542/#:~:text=In%20the%20current%20study%2C%20we,of%20YAP%20target%20genes%20in')
  80. AnnotationURLCitation(end_index=30824, start_index=30648, title='Chromatin accessibility complex subunit 1 enhances tumor growth by regulating the oncogenic transcription of YAP in breast and cervical cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10787542/#:~:text=Hippo%20pathway%2C%20thereby%20promoting%20tumorigenesis,YAP%20in%20breast%20and%20cervical')
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  82. AnnotationURLCitation(end_index=31566, start_index=31409, title='Chromatin accessibility complex subunit 1 enhances tumor growth by regulating the oncogenic transcription of YAP in breast and cervical cancer - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10787542/#:~:text=match%20at%20L53%20Hippo%20pathway%2C,YAP%20in%20breast%20and%20cervical')
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