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CWC27 (gene symbol: CWC27, UniProt: Q6UX04) encodes the spliceosome-associated protein CWC27 homolog in humans (rajiv2018structuralandfunctional pages 1-3). The protein is also known by several alternative names, including SDCCAG10 (Serologically Defined Colon Cancer Antigen 10), NY-CO-10, and Cyp54 (rajiv2018structuralandfunctional pages 1-3, jurkova2026humancyclophilins—anemerging pages 1-2). CWC27 belongs to the cyclophilin-type peptidyl-prolyl isomerase (PPIase) family and is classified among the eight human nuclear cyclophilins, also referred to as "spliceophilins" due to their association with the spliceosome (rajiv2018structuralandfunctional pages 1-3).
The CWC27 protein consists of two distinct structural regions: an N-terminal cyclophilin-like domain (CLD) containing the characteristic PPIase fold, and a large C-terminal region composed of low-complexity, repetitive sequences (rajiv2018structuralandfunctional pages 1-3, rajiv2018structuralandfunctional pages 10-14). The N-terminal domain (~183 amino acids) adopts the canonical cyclophilin fold characterized by eight antiparallel β-sheets and two α-helices (rajiv2018structuralandfunctional pages 1-3). In contrast, the C-terminal extension (approximately 200 residues) is elongated, solvent-exposed, and largely unstructured, with its detailed function remaining incompletely characterized (rajiv2018structuralandfunctional pages 10-14, bertrand2022cwc27associatedwith pages 2-4).
The cyclophilin-like domain contains the conserved proline-binding pocket characteristic of the cyclophilin family. However, structural analysis reveals that CWC27 has undergone a critical substitution in the active site. While canonical cyclophilins possess a tryptophan residue (Trp121 in the reference cyclophilin PPIA) that is essential for catalytic activity, CWC27 harbors a glutamic acid substitution at position 122 (Glu122) in the S1 proline-binding pocket (rajiv2018structuralandfunctional pages 10-14, davis2010structuralandbiochemical pages 3-4). This substitution is key to understanding CWC27's non-catalytic function.
Despite belonging to the cyclophilin family, CWC27 is catalytically inactive as a peptidyl-prolyl cis-trans isomerase (davis2010structuralandbiochemical pages 1-2, davis2010structuralandbiochemical pages 3-4, bertrand2022cwc27associatedwith pages 2-4). Comprehensive biochemical characterization of the human cyclophilin family demonstrated that CWC27 (SDCCAG10) lacks measurable PPIase activity against standard tetrapeptide substrates, a finding that distinguishes it from most other cyclophilins (davis2010structuralandbiochemical pages 1-2, davis2010structuralandbiochemical pages 3-4). This loss of catalytic function is directly attributable to the Glu122 substitution in the active site, which renders the enzyme incompetent for proline isomerization (rajiv2018structuralandfunctional pages 10-14).
While CWC27 cannot catalyze prolyl isomerization, it retains the ability to bind proline-containing peptides (rajiv2018structuralandfunctional pages 10-14, bertrand2022cwc27associatedwith pages 2-4). This preserved binding capacity, despite loss of catalytic activity, suggests that CWC27 functions primarily through protein-protein interactions rather than enzymatic catalysis (breafernandez2019expandingtheclinical pages 1-3, bertrand2022cwc27associatedwith pages 2-4). Family-wide ligand binding studies confirm that CWC27 does not bind cyclosporin A (CsA), the canonical cyclophilin inhibitor, consistent with its altered active site architecture (davis2010structuralandbiochemical pages 3-4).
CWC27 is localized to the nucleus and cytosol, with its primary functional activity occurring in the nuclear compartment (jurkova2026humancyclophilins—anemerging pages 1-2). Consistent with other nuclear cyclophilins involved in splicing, CWC27 localizes to nuclear speckles, subnuclear domains enriched in splicing factors and pre-mRNA processing machinery (rajiv2018structuralandfunctional pages 1-3). This nuclear localization is essential for its role in pre-mRNA splicing and spliceosome function.
CWC27 functions as a splicing factor within the major spliceosome, the large ribonucleoprotein complex responsible for removing introns from precursor messenger RNAs (rajiv2018structuralandfunctional pages 1-3, bertrand2022cwc27associatedwith pages 1-2, wan2020howisprecursor pages 1-2). The spliceosome undergoes dynamic assembly through sequential stages: assembly (E, A, pre-B, B complexes), activation (Bact complex), catalysis (B, C, C complexes), and disassembly (P, ILS complexes) (wan2020howisprecursor pages 1-2). CWC27 is specifically enriched in the activated Bact spliceosome and is present with moderate abundance in the C complex, but is released prior to the stable formation of the B* complex (rajiv2018structuralandfunctional pages 10-14, zhan2024molecularbasisfor pages 1-2, wan2020howisprecursor pages 8-10).
Cryo-electron microscopy (cryo-EM) structures of human spliceosomes at near-atomic resolution have revealed the precise positioning of CWC27 within the Bact complex (rajiv2018structuralandfunctional pages 10-14, zhan2024molecularbasisfor pages 1-2, schmitzova2023structuralbasisof pages 1-2). In these structures, the cyclophilin-like domain of CWC27 makes contacts with several spliceosomal components, including PRPF8 (a central scaffolding protein), BUD31, RNF113 (RING finger protein 113), and U5 snRNP 200 kDa helicase (rajiv2018structuralandfunctional pages 10-14). These interactions position CWC27 at the spliceosome surface where it can coordinate recruitment and remodeling of additional factors during activation.
A critical function of CWC27 is its formation of a heterodimer with CWC22, another spliceosomal protein (bertrand2022cwc27associatedwith pages 1-2, bertrand2022cwc27associatedwith pages 2-4, schlautmann2020adayin pages 3-5). The CWC27–CWC22 complex serves as a landing platform for recruiting eIF4A3, the DEAD-box RNA helicase that forms the core of the exon junction complex (EJC) (schlautmann2020adayin pages 1-3, schlautmann2020adayin pages 3-5). The EJC is a multi-protein complex deposited on mRNAs approximately 20-24 nucleotides upstream of exon-exon junctions following splicing, and it plays essential roles in downstream mRNA metabolism including export, translation, and nonsense-mediated decay (schlautmann2020adayin pages 1-3).
The sequential recruitment model proposes that CWC22 initially binds to the spliceosome alone, followed by CWC27 association to form the CWC27/CWC22 heterodimer, which then recruits eIF4A3 (schlautmann2020adayin pages 3-5). Following eIF4A3 recruitment, CWC27 dissociates from the spliceosome before complete EJC assembly, as its continued presence would sterically clash with RBM8A, another EJC core component (schlautmann2020adayin pages 3-5). This step-wise assembly pathway highlights CWC27's role as a transient assembly factor rather than a permanent spliceosome component.
During the transition from the pre-catalytic B complex to the catalytically activated B* complex, the spliceosome undergoes extensive remodeling driven by ATP-dependent RNA helicases (wan2020howisprecursor pages 1-2, zhan2024molecularbasisfor pages 1-2, schmitzova2023structuralbasisof pages 1-2). CWC27 participates in this critical activation stage. Structural studies from 2023-2024 have provided detailed molecular choreography of this process. In the Bact complex, the branch site (BS) of the pre-mRNA is sequestered approximately 50 Å away from the 5' splice site and shielded by proteins including CWC27 (schmitzova2023structuralbasisof pages 1-2, wan2020howisprecursor pages 8-10). The DEAH-box helicase PRP2, assisted by its co-activator SPP2, pulls on the 3' end of the intron, leading to dissociation of the SF3a/SF3b complexes, RES complex, and importantly, both CWC24 and CWC27 (schmitzova2023structuralbasisof pages 1-2, wan2020howisprecursor pages 8-10). This remodeling allows the branch site to move into proximity with the 5' splice site for catalysis.
Recent 2024 studies capturing six intermediate states between B and B* complexes (pre-Bact, Bact-I, Bact-II, Bact-III, Bact-IV, and post-Bact) demonstrate that CWC27 is present in earlier Bact states but absent in later post-Bact intermediates, confirming its release during this critical transition (zhan2024molecularbasisfor pages 1-2).
While CWC27's role in splicing was inferred from in vitro biochemical studies and structural analyses, direct in vivo validation came from studies of a mouse model carrying a frameshift mutation (Cwc27K338fs/K338fs) (bertrand2022cwc27associatedwith pages 1-2, bertrand2022cwc27associatedwith pages 4-6, bertrand2022cwc27associatedwith pages 2-4). This mouse model exhibits progressive retinal degeneration, with retinal dysfunction detectable by electroretinography at 3 months of age and photoreceptor loss evident at 4 months (bertrand2022cwc27associatedwith pages 2-4).
RNA-sequencing analysis of the Cwc27K338fs/K338fs mouse retina provided the first direct evidence that CWC27 functions as a splicing factor in vivo (bertrand2022cwc27associatedwith pages 1-2, bertrand2022cwc27associatedwith pages 4-6). Compared to wild-type controls, the mutant retina exhibited 257 differential splicing events, with the most abundant defects being intron retention followed by exon skipping (bertrand2022cwc27associatedwith pages 4-6). These splicing pattern changes are consistent with those observed in other splicing factor-associated disease models, including retinitis pigmentosa caused by mutations in PRPF31, PRPF8, and other core spliceosomal components (bertrand2022cwc27associatedwith pages 1-2).
Gene ontology analysis revealed that differentially spliced genes in the mutant retina were enriched for visual physiology pathways and included several inherited retinal disease genes such as Cnga1 (cyclic nucleotide-gated channel alpha 1), Prpf6 (pre-mRNA processing factor 6), and Rpgrip1 (retinitis pigmentosa GTPase regulator interacting protein 1) (bertrand2022cwc27associatedwith pages 4-6). Single-cell RNA-sequencing demonstrated that rod photoreceptors and Müller glial cells showed the largest number of differentially expressed genes, with rod photoreceptors exhibiting downregulation of mitochondrial transcripts and Müller cells showing upregulation of inflammatory genes (bertrand2022cwc27associatedwith pages 4-6).
The mouse model studies suggest that CWC27 loss leads to aberrant splicing, which in turn activates endoplasmic reticulum (ER) stress pathways, as evidenced by positive CHOP staining in the mutant retina (bertrand2022cwc27associatedwith pages 1-2, bertrand2022cwc27associatedwith pages 4-6). This ER stress response likely contributes to the progressive photoreceptor degeneration observed in the model. Importantly, the disease mechanism appears to stem from defective splicing rather than loss of cyclophilin enzymatic activity, given that CWC27 lacks PPIase activity (bertrand2022cwc27associatedwith pages 1-2, bertrand2022cwc27associatedwith pages 2-4).
Biallelic deleterious variants in CWC27 cause a rare autosomal recessive condition classified as a spliceosomopathy (griffin2020spliceosomopathiesdiseasesand pages 1-7, breafernandez2019expandingtheclinical pages 1-3). The phenotypic spectrum includes retinal degeneration/retinitis pigmentosa as the cardinal feature, along with variable additional manifestations such as short stature, skeletal anomalies (including brachydactyly), neurological defects, hypergonadotropic hypogonadism, dental anomalies, and cataracts (griffin2020spliceosomopathiesdiseasesand pages 1-7, breafernandez2019expandingtheclinical pages 1-3).
CWC27-related disorders belong to the broader category of spliceosomopathies, diseases caused by mutations in genes encoding spliceosome components (griffin2020spliceosomopathiesdiseasesand pages 1-7). A striking feature of spliceosomopathies is their tissue specificity despite the ubiquitous expression of spliceosomal proteins. For example, mutations in PRPF31, PRPF8, PRPF6, and SNRNP200 predominantly cause retinitis pigmentosa, while mutations in other spliceosomal genes cause myelodysplastic syndromes or craniofacial disorders such as mandibulofacial dysostosis (griffin2020spliceosomopathiesdiseasesand pages 1-7). The mechanisms underlying this tissue specificity remain an active area of investigation, but likely involve differential sensitivity of specific cell types to splicing perturbations, with photoreceptors being particularly vulnerable (bertrand2022cwc27associatedwith pages 1-2, griffin2020spliceosomopathiesdiseasesand pages 1-7).
Major advances in understanding CWC27 function have come from recent cryo-EM structural studies. Schmitzová et al. (2023) reported structures of the BAQR spliceosome, an intermediate stalled between PRP2 and Aquarius helicase actions, providing unprecedented detail on CWC27's interactions during catalytic activation (schmitzova2023structuralbasisof pages 1-2). Zhan et al. (2024) captured six distinct intermediate states of the human Bact complex, revealing the molecular choreography of spliceosome activation and the ordered flux of components including CWC27 (zhan2024molecularbasisfor pages 1-2).
Rogalska et al. (2024) conducted transcriptome-wide analysis of splicing networks following systematic knockdown of 305 spliceosome components and regulators in human cancer cells. This study revealed that CWC27 knockdown, which links to exon junction complex assembly, produces specific splicing regulatory effects, confirming its specialized function within the core spliceosome machinery.
A comprehensive 2026 review by Jurkova et al. discusses human cyclophilins as an emerging class of drug targets (jurkova2026humancyclophilins—anemerging pages 1-2, jurkova2026humancyclophilins—anemerging pages 9-11). While CWC27's lack of PPIase activity makes it an unlikely target for traditional cyclophilin inhibitors like cyclosporin derivatives, understanding its role in splicing could inform therapeutic strategies for CWC27-related spliceosomopathies and potentially for modulating splicing in other disease contexts.
| Category | Finding for human CWC27 | Evidence / details | Citation |
|---|---|---|---|
| Gene identity | CWC27 is the approved human gene; major aliases include SDCCAG10, NY-CO-10, serologically defined colon cancer antigen 10, and Cyp54 | Matches the requested UniProt-centered identity and the spliceosome-associated cyclophilin literature | (rajiv2018structuralandfunctional pages 1-3, jurkova2026humancyclophilins—anemerging pages 1-2) |
| Protein family | Nuclear cyclophilin-type spliceosome-associated protein | Classified among the human nuclear cyclophilins / “spliceophilins” | (rajiv2018structuralandfunctional pages 1-3, jurkova2026humancyclophilins—anemerging pages 1-2) |
| Protein architecture | N-terminal cyclophilin/PPIase-like domain plus a large C-terminal low-complexity, repetitive, largely unstructured region | Review and disease papers describe a structured N-terminus and elongated solvent-exposed C-terminus of unknown/interaction-focused function | (rajiv2018structuralandfunctional pages 10-14, bertrand2022cwc27associatedwith pages 2-4) |
| Structural size/features | Only the isomerase-like N-terminal domain has been structurally resolved in detail in spliceosome studies; roughly ~200 C-terminal residues remain structurally uncharacterized in cryo-EM models | Cryo-EM models place the PPIase-like domain in Bact complexes, while the distal C-terminus is not resolved | (rajiv2018structuralandfunctional pages 10-14) |
| Enzymatic status | Catalytically inactive as a peptidyl-prolyl cis-trans isomerase | Despite cyclophilin fold membership, CWC27 lacks measurable PPIase activity | (breafernandez2019expandingtheclinical pages 1-3, bertrand2022cwc27associatedwith pages 2-4) |
| Active-site alteration | In the S1/proline-binding pocket, canonical catalytic Trp is replaced by Glu122 | This Glu122 substitution is the key structural explanation for loss of isomerase activity | (rajiv2018structuralandfunctional pages 10-14) |
| Cyclosporin binding | Does not bind cyclosporin A under tested conditions | Family-wide biochemical analysis found no evidence of CsA binding for SDCCAG10/CWC27 | (davis2010structuralandbiochemical pages 3-4) |
| Substrate specificity / ligand preference | Retains the ability to bind proline-containing peptides/proline, but does not catalyze cis-trans isomerization | Literature describes preserved proline recognition despite loss of catalytic turnover; likely supports interaction-based rather than enzymatic function | (rajiv2018structuralandfunctional pages 10-14, breafernandez2019expandingtheclinical pages 1-3, bertrand2022cwc27associatedwith pages 2-4) |
| Primary molecular role | Splicing factor / spliceosome-associated scaffold rather than enzyme | Current understanding is that CWC27 contributes through protein-protein interactions during spliceosome activation and EJC recruitment | (bertrand2022cwc27associatedwith pages 1-2, bertrand2022cwc27associatedwith pages 2-4, schlautmann2020adayin pages 3-5) |
| Subcellular localization | Primarily nuclear; broader cyclophilin tables also list nucleus and cytosol | Functional role is nuclear because it acts on the spliceosome during pre-mRNA splicing | (jurkova2026humancyclophilins—anemerging pages 1-2, schlautmann2020adayin pages 3-5) |
| Spliceosome stage | Enriched in the activated Bact spliceosome and present with moderate abundance in C complex; released before stable B* progression / complete EJC assembly | Structural and functional studies place CWC27 in late assembly/activation stages of the major spliceosome | (rajiv2018structuralandfunctional pages 10-14, bertrand2022cwc27associatedwith pages 2-4, wan2020howisprecursor pages 8-10) |
| Spliceosome neighborhood | In Bact, the PPIase-like domain contacts PRPF8, BUD31, RNF113, and U5 snRNP 200K in different structural states | These contacts position CWC27 at the spliceosome surface where it can coordinate factor recruitment/remodeling | (rajiv2018structuralandfunctional pages 10-14) |
| Key protein-protein interaction | Forms a heterodimer with CWC22 | The CWC27–CWC22 complex is proposed to create a landing platform for EJC factor recruitment | (bertrand2022cwc27associatedwith pages 1-2, bertrand2022cwc27associatedwith pages 2-4, schlautmann2020adayin pages 3-5) |
| Link to EJC assembly | Helps recruit EIF4A3 (core EJC helicase) via the CWC27/CWC22 platform | CWC27 leaves before full EJC assembly, consistent with a transient assembly-factor role | (bertrand2022cwc27associatedwith pages 1-2, bertrand2022cwc27associatedwith pages 2-4, schlautmann2020adayin pages 3-5) |
| Functional pathway | Participates in pre-mRNA splicing and mechanistically links spliceosome activation to exon junction complex deposition | Places CWC27 in the broader RNA-processing pathway rather than a standalone catalytic pathway | (schlautmann2020adayin pages 1-3, schlautmann2020adayin pages 3-5, wan2020howisprecursor pages 8-10) |
| In vivo functional evidence | Mouse Cwc27 mutant retina shows 257 differential splicing events versus wild type | Most abundant defects were intron retention followed by exon skipping; supports bona fide in vivo splicing-factor function | (bertrand2022cwc27associatedwith pages 4-6) |
| Splicing-sensitive genes/examples | Differentially spliced retinal genes include Cnga1, Prpf6, and Rpgrip1 | These changes help connect CWC27 dysfunction to retinal physiology and disease | (bertrand2022cwc27associatedwith pages 4-6) |
| Disease association | Biallelic deleterious variants cause a CWC27-related spliceosomopathy with retinal degeneration/retinitis pigmentosa, short stature, skeletal anomalies, and neurological features | Human genetics and review literature consistently place retinal degeneration at the core of the phenotype spectrum | (griffin2020spliceosomopathiesdiseasesand pages 1-7, breafernandez2019expandingtheclinical pages 1-3, bertrand2022cwc27associatedwith pages 2-4) |
| Retinal degeneration evidence | In the Cwc27K338fs/K338fs mouse, retinal dysfunction appears by 3 months and photoreceptor loss by 4 months | Provides direct in vivo support for a causal role in retinal degeneration pathogenesis | (bertrand2022cwc27associatedwith pages 2-4) |
| Mechanistic disease interpretation | Aberrant splicing in mutant retina is associated with ER-stress/CHOP positivity and cell-type-specific transcriptomic disruption, especially in rod photoreceptors and Müller glia | Supports the view that disease arises from splicing defects rather than loss of cyclophilin enzymatic catalysis | (bertrand2022cwc27associatedwith pages 1-2, bertrand2022cwc27associatedwith pages 4-6) |
Table: This table summarizes the key molecular, biochemical, cellular, and disease-related properties of human CWC27 from the cited literature. It highlights why CWC27 is best understood as a catalytically inactive spliceosomal cyclophilin that helps organize splicing and EJC recruitment, with strong links to retinal degeneration.
CWC27 represents a fascinating example of molecular evolution within the cyclophilin family. Despite lacking catalytic peptidyl-prolyl isomerase activity due to a critical active site substitution (Glu122), CWC27 has been repurposed as a structural and scaffolding component of the spliceosome. Its primary function is to facilitate recruitment of the exon junction complex during pre-mRNA splicing through formation of a transient landing platform with CWC22. Loss of CWC27 function leads to widespread splicing defects, particularly intron retention and exon skipping, which cause tissue-specific pathology most prominently affecting the retina. The recent structural and functional characterization of CWC27 highlights the complexity of spliceosome assembly and the critical importance of non-catalytic factors in orchestrating this essential cellular process.
Key Research Papers (with URLs and dates):
Davis et al. (2010) - Structural and Biochemical Characterization of the Human Cyclophilin Family. PLoS Biology 8(7):e1000439. https://doi.org/10.1371/journal.pbio.1000439
Rajiv & Davis (2018) - Structural and Functional Insights into Human Nuclear Cyclophilins. Biomolecules 8(4):161. https://doi.org/10.3390/biom8040161
Brea-Fernández et al. (2019) - Expanding the clinical and molecular spectrum of the CWC27-related spliceosomopathy. Journal of Human Genetics 64:1133-1136. https://doi.org/10.1038/s10038-019-0664-7
Griffin & Saint-Jeannet (2020) - Spliceosomopathies: Diseases and mechanisms. Developmental Dynamics 249:1038-1046. https://doi.org/10.1002/dvdy.214
Wan et al. (2020) - How Is Precursor Messenger RNA Spliced by the Spliceosome? Annual Review of Biochemistry 89:333-358. https://doi.org/10.1146/annurev-biochem-013118-111024
Schlautmann & Gehring (2020) - A Day in the Life of the Exon Junction Complex. Biomolecules 10(6):866. https://doi.org/10.3390/biom10060866
Bertrand et al. (2022) - Cwc27, associated with retinal degeneration, functions as a splicing factor in vivo. Human Molecular Genetics 31(8):1278-1292. https://doi.org/10.1093/hmg/ddab319
Schmitzová et al. (2023) - Structural basis of catalytic activation in human splicing. Nature 617:842-850. https://doi.org/10.1038/s41586-023-06049-w (Published May 2023)
Zhan et al. (2024) - Molecular basis for the activation of human spliceosome. Nature Communications 15:6348. https://doi.org/10.1038/s41467-024-50785-0 (Published July 2024)
Rogalska et al. (2024) - Transcriptome-wide splicing network reveals specialized regulatory functions of the core spliceosome. Science 386(6721):551-560. https://doi.org/10.1126/science.adn8105 (Published November 2024)
Jurkova et al. (2026) - Human Cyclophilins—An Emerging Class of Drug Targets. Medicinal Research Reviews 46(2):475-512. https://doi.org/10.1002/med.70021 (Published October 2025, volume dated 2026)
References
(rajiv2018structuralandfunctional pages 1-3): Carol Rajiv and Tara L. Davis. Structural and functional insights into human nuclear cyclophilins. Biomolecules, Nov 2018. URL: https://doi.org/10.3390/biom8040161, doi:10.3390/biom8040161. This article has 54 citations.
(jurkova2026humancyclophilins—anemerging pages 1-2): Katarina Jurkova, Hana Navratilova, Kamil Musilek, and Ondrej Benek. Human cyclophilins—an emerging class of drug targets. Medicinal Research Reviews, 46:475-512, Oct 2026. URL: https://doi.org/10.1002/med.70021, doi:10.1002/med.70021. This article has 1 citations and is from a domain leading peer-reviewed journal.
(rajiv2018structuralandfunctional pages 10-14): Carol Rajiv and Tara L. Davis. Structural and functional insights into human nuclear cyclophilins. Biomolecules, Nov 2018. URL: https://doi.org/10.3390/biom8040161, doi:10.3390/biom8040161. This article has 54 citations.
(bertrand2022cwc27associatedwith pages 2-4): Renae Elaine Bertrand, Jun Wang, Yumei Li, Xuesen Cheng, Keqing Wang, Peter Stoilov, and Rui Chen. Cwc27, associated with retinal degeneration, functions as a splicing factor in vivo. Human molecular genetics, 31:1278-1292, Nov 2022. URL: https://doi.org/10.1093/hmg/ddab319, doi:10.1093/hmg/ddab319. This article has 19 citations and is from a domain leading peer-reviewed journal.
(davis2010structuralandbiochemical pages 3-4): Tara L. Davis, John R. Walker, Valérie Campagna-Slater, Patrick J. Finerty, Ragika Paramanathan, Galina Bernstein, Farrell MacKenzie, Wolfram Tempel, Hui Ouyang, Wen Hwa Lee, Elan Z. Eisenmesser, and Sirano Dhe-Paganon. Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases. PLoS Biology, 8:e1000439, Jul 2010. URL: https://doi.org/10.1371/journal.pbio.1000439, doi:10.1371/journal.pbio.1000439. This article has 385 citations and is from a highest quality peer-reviewed journal.
(davis2010structuralandbiochemical pages 1-2): Tara L. Davis, John R. Walker, Valérie Campagna-Slater, Patrick J. Finerty, Ragika Paramanathan, Galina Bernstein, Farrell MacKenzie, Wolfram Tempel, Hui Ouyang, Wen Hwa Lee, Elan Z. Eisenmesser, and Sirano Dhe-Paganon. Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases. PLoS Biology, 8:e1000439, Jul 2010. URL: https://doi.org/10.1371/journal.pbio.1000439, doi:10.1371/journal.pbio.1000439. This article has 385 citations and is from a highest quality peer-reviewed journal.
(breafernandez2019expandingtheclinical pages 1-3): Alejandro J. Brea-Fernández, Paloma Cabanas, David Dacruz-Álvarez, Pilar Caamaño, Jacobo Limeres, and Lourdes Loidi. Expanding the clinical and molecular spectrum of the cwc27-related spliceosomopathy. Journal of Human Genetics, 64:1133-1136, Sep 2019. URL: https://doi.org/10.1038/s10038-019-0664-7, doi:10.1038/s10038-019-0664-7. This article has 16 citations and is from a peer-reviewed journal.
(bertrand2022cwc27associatedwith pages 1-2): Renae Elaine Bertrand, Jun Wang, Yumei Li, Xuesen Cheng, Keqing Wang, Peter Stoilov, and Rui Chen. Cwc27, associated with retinal degeneration, functions as a splicing factor in vivo. Human molecular genetics, 31:1278-1292, Nov 2022. URL: https://doi.org/10.1093/hmg/ddab319, doi:10.1093/hmg/ddab319. This article has 19 citations and is from a domain leading peer-reviewed journal.
(wan2020howisprecursor pages 1-2): Ruixue Wan, Rui Bai, Xiechao Zhan, and Yigong Shi. How is precursor messenger rna spliced by the spliceosome? Jun 2020. URL: https://doi.org/10.1146/annurev-biochem-013118-111024, doi:10.1146/annurev-biochem-013118-111024. This article has 177 citations and is from a domain leading peer-reviewed journal.
(zhan2024molecularbasisfor pages 1-2): Xiechao Zhan, Yichen Lu, and Yigong Shi. Molecular basis for the activation of human spliceosome. Nature Communications, Jul 2024. URL: https://doi.org/10.1038/s41467-024-50785-0, doi:10.1038/s41467-024-50785-0. This article has 24 citations and is from a highest quality peer-reviewed journal.
(wan2020howisprecursor pages 8-10): Ruixue Wan, Rui Bai, Xiechao Zhan, and Yigong Shi. How is precursor messenger rna spliced by the spliceosome? Jun 2020. URL: https://doi.org/10.1146/annurev-biochem-013118-111024, doi:10.1146/annurev-biochem-013118-111024. This article has 177 citations and is from a domain leading peer-reviewed journal.
(schmitzova2023structuralbasisof pages 1-2): Jana Schmitzová, Constantin Cretu, Christian Dienemann, Henning Urlaub, and Vladimir Pena. Structural basis of catalytic activation in human splicing. Nature, 617:842-850, May 2023. URL: https://doi.org/10.1038/s41586-023-06049-w, doi:10.1038/s41586-023-06049-w. This article has 70 citations and is from a highest quality peer-reviewed journal.
(schlautmann2020adayin pages 3-5): Lena P. Schlautmann and Niels H. Gehring. A day in the life of the exon junction complex. Biomolecules, 10:866, Jun 2020. URL: https://doi.org/10.3390/biom10060866, doi:10.3390/biom10060866. This article has 113 citations.
(schlautmann2020adayin pages 1-3): Lena P. Schlautmann and Niels H. Gehring. A day in the life of the exon junction complex. Biomolecules, 10:866, Jun 2020. URL: https://doi.org/10.3390/biom10060866, doi:10.3390/biom10060866. This article has 113 citations.
(bertrand2022cwc27associatedwith pages 4-6): Renae Elaine Bertrand, Jun Wang, Yumei Li, Xuesen Cheng, Keqing Wang, Peter Stoilov, and Rui Chen. Cwc27, associated with retinal degeneration, functions as a splicing factor in vivo. Human molecular genetics, 31:1278-1292, Nov 2022. URL: https://doi.org/10.1093/hmg/ddab319, doi:10.1093/hmg/ddab319. This article has 19 citations and is from a domain leading peer-reviewed journal.
(griffin2020spliceosomopathiesdiseasesand pages 1-7): Casey Griffin and Jean‐Pierre Saint‐Jeannet. Spliceosomopathies: diseases and mechanisms. Developmental Dynamics, 249:1038-1046, Jun 2020. URL: https://doi.org/10.1002/dvdy.214, doi:10.1002/dvdy.214. This article has 105 citations and is from a peer-reviewed journal.
(jurkova2026humancyclophilins—anemerging pages 9-11): Katarina Jurkova, Hana Navratilova, Kamil Musilek, and Ondrej Benek. Human cyclophilins—an emerging class of drug targets. Medicinal Research Reviews, 46:475-512, Oct 2026. URL: https://doi.org/10.1002/med.70021, doi:10.1002/med.70021. This article has 1 citations and is from a domain leading peer-reviewed journal.