The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The requested target—human CRISP2 (cysteine-rich secretory protein 2; CRISP-2; TPX-1/TPX1; CT36)—is correctly matched to UniProt accession P16562. A human sperm study explicitly maps mass-spectrometry peptides onto the two UniProt isoforms P16562-1 and P16562-2, confirming that the reviewed literature is aligned to the same protein identity (masai2025novelinsightsinto pages 11-11, masai2025novelinsightsinto pages 14-15). Reported aliases in the human study include TPX1 and AA1 (masai2025novelinsightsinto pages 38-40), consistent with the provided UniProt description.
CRISP2 belongs to the CRISP family within the broader CAP superfamily (also called SCP/PR-1/Antigen 5). Authoritative reviews define CRISPs as typically two-domain proteins comprising an N-terminal CAP domain plus a C-terminal cysteine-rich CRISP domain (CRD/ICR + hinge) stabilized by multiple disulfide bonds; the N-terminal CAP domain is often implicated in protein–protein/cell–cell interactions in reproduction, while the C-terminal CRISP domain has been linked to ion-channel regulatory activity (gibbs2008thecapsuperfamily pages 4-4, gibbs2008thecapsuperfamily pages 3-4, gibbs2008thecapsuperfamily pages 4-5).
CRISP2 is best understood as a non-enzymatic structural/interaction protein in sperm biology rather than a metabolic enzyme: it is positioned in reviews as a reproductive tract–associated CAP/CRISP protein implicated in sperm development, capacitation-associated signaling, and gamete interaction, with proposed ion-channel/Ca2+ modulation roles (gibbs2008thecapsuperfamily pages 17-17, gibbs2008thecapsuperfamily pages 18-19).
An authoritative review notes CRISP2 is produced during spermatogenesis and localizes to key sperm compartments (acrosome, accessory tail structures, developing germ-cell membrane) (gibbs2008thecapsuperfamily pages 17-17). A recent human-focused primary study further refines this with direct tissue imaging and biochemical characterization (masai2025novelinsightsinto pages 1-1).
In human testis sections, immunostaining shows CRISP2 signal across germ-cell stages:
- Primary spermatocytes: faint nuclear puncta.
- Round spermatids: more intense, homogeneous nuclear signal.
- Early elongated spermatids: intense nuclear spots with additional cytoplasmic signal.
- Late elongated spermatids: CRISP2 also seen in the flagellum and the equatorial segment (EqS) of the acrosome; late nuclei may appear negative, possibly reflecting chromatin condensation.
These observations were supported by antibody controls and confocal imaging (masai2025novelinsightsinto pages 6-7, masai2025novelinsightsinto pages 7-8).
In human epididymis, CRISP2 staining is observed in sperm within the lumen (including a dense spot at the basal head region and along the flagellum), while the epididymal epithelium is negative (masai2025novelinsightsinto pages 5-6). In ejaculated sperm, CRISP2 is reported in the cytoplasmic droplet, flagellum, and EqS, consistent with roles in motility and gamete fusion (masai2025novelinsightsinto pages 1-1).
Review-level synthesis places CRISP2 in sperm Ca2+ signaling through ryanodine receptor (RyR)-mediated Ca2+ release and broader ion-channel modulation (gibbs2008thecapsuperfamily pages 17-17, gibbs2008thecapsuperfamily pages 18-19). A 2023 ejaculate-based shotgun proteomics study explicitly annotates CRISP2 as potentially regulating ion channels and thereby calcium fluxes during sperm capacitation (shkrigunov2023theapplicationof pages 8-9).
A major 2024 development is biochemical evidence that CRISP2 participates in sterol binding and sterol export in a yeast-based functional model and that this activity can be strongly regulated by A1BG:
- Binding partner/regulator: Human A1BG binds CRISP2 with high affinity (MST Kd values reported around 13.72 ± 2.5 nM; also ~10.3 ± 2.4 nM under Mg2+ conditions) (atab2024alpha1bglycoprotein(a1bg) pages 2-4, atab2024alpha1bglycoprotein(a1bg) pages 12-13).
- Functional inhibition: Coexpression of A1BG with CRISP2 (or related CAP proteins) reduced sterol secretion by >50% in vivo (yeast export assay) (atab2024alpha1bglycoprotein(a1bg) pages 2-4, atab2024alpha1bglycoprotein(a1bg) pages 1-2).
- Ligand binding: CRISP2 binds cholesterol sulfate with reported Kd values ranging from low micromolar to nanomolar depending on assay conditions; binding is blocked by A1BG (atab2024alpha1bglycoprotein(a1bg) pages 2-4, atab2024alpha1bglycoprotein(a1bg) pages 12-13, atab2024alpha1bglycoprotein(a1bg) pages 9-11).
- Cation dependence: The A1BG–CRISP2 interaction is Mg2+-dependent; Zn2+ cannot substitute in restoring binding after EDTA chelation (atab2024alpha1bglycoprotein(a1bg) pages 11-12, atab2024alpha1bglycoprotein(a1bg) pages 12-13).
Mechanistically, these findings reinforce the CAP-domain concept of ligand binding and extend CRISP2 beyond purely “ion-channel regulator” framing toward lipid/sterol handling that may be relevant in reproductive tract fluids and sperm membranes (atab2024alpha1bglycoprotein(a1bg) pages 1-2, atab2024alpha1bglycoprotein(a1bg) pages 2-4).
A 2023 study evaluating ejaculate-based shotgun proteomics quantified CRISP2 (P16562) across ejaculate, seminal plasma, and spermatozoa:
- Validated unique peptides: ejaculate 11; plasma 30; spermatozoa 8.
- NSAF (spectrum counting): ejaculate 0.49; plasma 0.383; spermatozoa 0.474.
The same source summarizes CRISP2 as potentially regulating ion-channel activity and Ca2+ flux during capacitation (shkrigunov2023theapplicationof pages 8-9). A table image excerpt corroborates these values (shkrigunov2023theapplicationof media 5dc187ee).
A 2024 Frontiers in Endocrinology review compiling clinical miRNA studies summarizes that:
- miR-27b is reported upregulated in a semen-based comparison (n=24 vs 24) and is listed as targeting CRISP2, associated with effects on sperm morphology and progressive motility (shi2024micrornasinspermatogenesis pages 3-4).
- The review also states that high miR-27b expression is associated with reduced progressive motility and shows a negative association with CRISP2 protein levels (shi2024micrornasinspermatogenesis pages 4-5).
Evidence in the review is largely summarized (often without effect sizes in table form), so the quantitative strength of these associations depends on the original primary studies (shi2024micrornasinspermatogenesis pages 4-5, shi2024micrornasinspermatogenesis pages 19-20).
A 2024 prospective seminal plasma proteomics study on azoospermia provides clinically relevant statistics (not CRISP2-specific but directly relevant to implementation of testis-derived protein markers):
- Azoospermia affects nearly 2% of men and accounts for 5–20% of male infertility.
- NOA comprises about 90% of azoospermia cases.
- Sperm retrieval success is >90% in obstructive azoospermia but only ~50% in NOA.
This underpins the value of non-invasive seminal plasma protein biomarkers to avoid unnecessary surgery and to triage patients for retrieval attempts (fietz2024proteomicbiomarkersin pages 2-3, fietz2024proteomicbiomarkersin pages 1-2).
CRISP2 is already operationally used as a measured component in high-throughput LC-MS/MS datasets of ejaculate, seminal plasma, and spermatozoa, enabling quantitative comparisons and pathway enrichment in male infertility screening pipelines (shkrigunov2023theapplicationof pages 8-9).
Seminal plasma proteomics is being developed as a non-invasive tool to distinguish OA vs NOA and predict intratesticular sperm presence to rationalize surgery recommendations (fietz2024proteomicbiomarkersin pages 2-3, fietz2024proteomicbiomarkersin pages 1-2). While CRISP2 is not the primary marker highlighted in the pages examined, it is cited among infertility-related proteins in referenced work within this literature context (fietz2024proteomicbiomarkersin pages 12-12).
A 2024 expert review argues that sperm/ejaculate proteomics has substantial potential to improve diagnostics, guide ART, and identify non-hormonal contraceptive targets; however, translation is constrained by the need for reliable, reproducible, affordable assays and extensive validation and regulatory work (parkes2024bringingproteomicsto pages 28-29, parkes2024bringingproteomicsto pages 6-7). The authors highlight a persistent gap between biomarker discovery and clinical adoption and stress the importance of integrating proteomics with clinical phenotypes, genetics, and robust in vivo validation (parkes2024bringingproteomicsto pages 29-31).
| Category | Key points | Evidence type (review/primary/proteomics) | Top citations (pqac-IDs) |
|---|---|---|---|
| Identity/domains | Human CRISP2 is UniProt P16562; recent human sperm work explicitly maps peptides to isoforms P16562-1 and P16562-2. It is a CAP superfamily/CRISP-family protein with an N-terminal CAP domain and a C-terminal cysteine-rich CRISP domain (including hinge/ICR features); the family is linked to ion-channel regulation and reproduction. | Primary + review | (masai2025novelinsightsinto pages 11-11, masai2025novelinsightsinto pages 38-40, gibbs2008thecapsuperfamily pages 3-4, gibbs2008thecapsuperfamily pages 4-4, gibbs2008thecapsuperfamily pages 4-5) |
| Expression | CRISP2 is the mammalian CRISP most tightly associated with testicular germ cells and spermatogenesis. In human tissue, expression is seen through spermatogenic stages and not in epididymal epithelium; in sperm proteomics it is repeatedly detected in ejaculated sperm. | Primary + review + proteomics | (masai2025novelinsightsinto pages 11-12, masai2025novelinsightsinto pages 6-7, masai2025novelinsightsinto pages 12-13, masai2025novelinsightsinto pages 1-1, shkrigunov2023theapplicationof pages 8-9) |
| Subcellular localization | In human testis, hCRISP2 localizes to nuclei of primary spermatocytes, round spermatids, and early elongated spermatids; later also to cytoplasm, flagellum, and equatorial segment. In ejaculated sperm, signal is reported in cytoplasmic droplet, flagellum, equatorial segment, and basal head/connecting-piece regions. Evidence comes from immunofluorescence/confocal z-stacks, antibody controls, western blotting, immunoprecipitation, and MS. | Primary | (masai2025novelinsightsinto pages 6-7, masai2025novelinsightsinto pages 8-9, masai2025novelinsightsinto pages 12-13, masai2025novelinsightsinto pages 1-1, masai2025novelinsightsinto pages 7-8, masai2025novelinsightsinto pages 5-6) |
| Molecular mechanisms | Current understanding supports CRISP2 as a structural/functional sperm protein rather than an enzyme. Review-level evidence places CRISP2 in Ca2+ signaling via regulation of ryanodine receptor-mediated Ca2+ flux and more broadly in ion-channel modulation relevant to motility, capacitation, and acrosome reaction. A 2024 JBC study also shows CRISP2 can bind sterol and mediate sterol export, adding a biochemical activity within the CAP domain framework. | Review + primary | (gibbs2008thecapsuperfamily pages 17-17, gibbs2008thecapsuperfamily pages 18-19, atab2024alpha1bglycoprotein(a1bg) pages 1-2, atab2024alpha1bglycoprotein(a1bg) pages 2-4, atab2024alpha1bglycoprotein(a1bg) pages 9-11) |
| Binding partners/regulators | CRISP2 is reported in sperm protein complexes and has literature-supported interactions with MAP3K11/MLK3 and GGN1; human sperm IP-MS recovered CRISP2 with co-detected proteins including ACR and ACRBP. In 2024, A1BG was shown to bind CRISP2 with high affinity and inhibit its sterol-binding/export activity; interaction requires Mg2+ and maps mainly to A1BG Ig3. | Primary + review + proteomics | (masai2025novelinsightsinto pages 38-40, gibbs2008thecapsuperfamily pages 17-17, atab2024alpha1bglycoprotein(a1bg) pages 1-2, atab2024alpha1bglycoprotein(a1bg) pages 11-12, atab2024alpha1bglycoprotein(a1bg) pages 5-7) |
| Disease/phenotype links | The strongest human disease link is male infertility, especially sperm motility-related phenotypes. Recent review summaries cite miR-27b/miR-27b-3p and miR-509-5p as CRISP2-related regulators in azoospermia/NOA or asthenozoospermia contexts; higher miR-27b is associated with impaired sperm morphology/progressive motility and inverse association with CRISP2 protein. Open Targets currently lists only weak target–disease association evidence for CRISP2 in male infertility. | Review + database | (shi2024micrornasinspermatogenesis pages 9-10, shi2024micrornasinspermatogenesis pages 3-4, shi2024micrornasinspermatogenesis pages 4-5, shi2024micrornasinspermatogenesis pages 19-20, OpenTargets Search: male infertility,asthenozoospermia,azoospermia,infertility-CRISP2) |
| Applications/biomarkers | CRISP2 is already used in sperm/ejaculate proteomics panels as a testis-specific or fertility-relevant protein and is discussed as a candidate biomarker for male infertility screening, though direct clinical implementation remains limited. Its localization and sperm-specificity also keep it of interest as a prospective fertility or contraceptive target. | Proteomics + review | (shkrigunov2023theapplicationof pages 8-9, atab2024alpha1bglycoprotein(a1bg) pages 1-2) |
| Key quantitative data | Human ejaculate proteomics (2023) reported CRISP2 validated unique peptides: ejaculate 11, seminal plasma 30, spermatozoa 8; NSAF values 0.49, 0.383, and 0.474, respectively. In 2024 biochemical studies, A1BG bound CRISP2 with Kd about 13.72 ± 2.5 nM (also ~10.3 ± 2.4 nM under Mg2+ conditions), Ig3 bound with Kd about 13.8 ± 1.14 nM, and A1BG coexpression inhibited CRISP2/Pry-family sterol secretion by >50%; CRISP2 bound cholesterol sulfate with reported Kd values in low micromolar to nanomolar/Mg2+-dependent assay ranges depending on assay conditions. | Proteomics + primary | (shkrigunov2023theapplicationof pages 8-9, atab2024alpha1bglycoprotein(a1bg) pages 11-12, atab2024alpha1bglycoprotein(a1bg) pages 2-4, atab2024alpha1bglycoprotein(a1bg) pages 5-7, atab2024alpha1bglycoprotein(a1bg) pages 12-13) |
Table: This table summarizes the current evidence-based functional annotation of human CRISP2 (UniProt P16562), including identity, localization, mechanisms, fertility links, and quantitative findings. It emphasizes recent 2023-2024 data where available while anchoring claims to authoritative reviews and primary studies.
References
(masai2025novelinsightsinto pages 11-11): Thibault Masai, Amandine Delnatte, Marie Dendievel, Denis Nonclercq, Annica Frau, Jean-François Simon, Vanessa Arcolia, Ruddy Wattiez, Baptiste Leroy, Patricia S Cuasnicu, Pascale Lybaert, and Elise Hennebert. Novel insights into human crisp2: localization in reproductive tissues and sperm, and molecular characterization. Biology of reproduction, 112:1167-1184, Mar 2025. URL: https://doi.org/10.1093/biolre/ioaf051, doi:10.1093/biolre/ioaf051. This article has 1 citations and is from a peer-reviewed journal.
(masai2025novelinsightsinto pages 14-15): Thibault Masai, Amandine Delnatte, Marie Dendievel, Denis Nonclercq, Annica Frau, Jean-François Simon, Vanessa Arcolia, Ruddy Wattiez, Baptiste Leroy, Patricia S Cuasnicu, Pascale Lybaert, and Elise Hennebert. Novel insights into human crisp2: localization in reproductive tissues and sperm, and molecular characterization. Biology of reproduction, 112:1167-1184, Mar 2025. URL: https://doi.org/10.1093/biolre/ioaf051, doi:10.1093/biolre/ioaf051. This article has 1 citations and is from a peer-reviewed journal.
(masai2025novelinsightsinto pages 38-40): Thibault Masai, Amandine Delnatte, Marie Dendievel, Denis Nonclercq, Annica Frau, Jean-François Simon, Vanessa Arcolia, Ruddy Wattiez, Baptiste Leroy, Patricia S Cuasnicu, Pascale Lybaert, and Elise Hennebert. Novel insights into human crisp2: localization in reproductive tissues and sperm, and molecular characterization. Biology of reproduction, 112:1167-1184, Mar 2025. URL: https://doi.org/10.1093/biolre/ioaf051, doi:10.1093/biolre/ioaf051. This article has 1 citations and is from a peer-reviewed journal.
(gibbs2008thecapsuperfamily pages 4-4): Gerard M. Gibbs, Kim Roelants, and Moira K. O'Bryan. The cap superfamily: cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins—roles in reproduction, cancer, and immune defense. Endocrine Reviews, 29:865-897, Dec 2008. URL: https://doi.org/10.1210/er.2008-0032, doi:10.1210/er.2008-0032. This article has 615 citations and is from a domain leading peer-reviewed journal.
(gibbs2008thecapsuperfamily pages 3-4): Gerard M. Gibbs, Kim Roelants, and Moira K. O'Bryan. The cap superfamily: cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins—roles in reproduction, cancer, and immune defense. Endocrine Reviews, 29:865-897, Dec 2008. URL: https://doi.org/10.1210/er.2008-0032, doi:10.1210/er.2008-0032. This article has 615 citations and is from a domain leading peer-reviewed journal.
(gibbs2008thecapsuperfamily pages 4-5): Gerard M. Gibbs, Kim Roelants, and Moira K. O'Bryan. The cap superfamily: cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins—roles in reproduction, cancer, and immune defense. Endocrine Reviews, 29:865-897, Dec 2008. URL: https://doi.org/10.1210/er.2008-0032, doi:10.1210/er.2008-0032. This article has 615 citations and is from a domain leading peer-reviewed journal.
(gibbs2008thecapsuperfamily pages 17-17): Gerard M. Gibbs, Kim Roelants, and Moira K. O'Bryan. The cap superfamily: cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins—roles in reproduction, cancer, and immune defense. Endocrine Reviews, 29:865-897, Dec 2008. URL: https://doi.org/10.1210/er.2008-0032, doi:10.1210/er.2008-0032. This article has 615 citations and is from a domain leading peer-reviewed journal.
(gibbs2008thecapsuperfamily pages 18-19): Gerard M. Gibbs, Kim Roelants, and Moira K. O'Bryan. The cap superfamily: cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins—roles in reproduction, cancer, and immune defense. Endocrine Reviews, 29:865-897, Dec 2008. URL: https://doi.org/10.1210/er.2008-0032, doi:10.1210/er.2008-0032. This article has 615 citations and is from a domain leading peer-reviewed journal.
(masai2025novelinsightsinto pages 1-1): Thibault Masai, Amandine Delnatte, Marie Dendievel, Denis Nonclercq, Annica Frau, Jean-François Simon, Vanessa Arcolia, Ruddy Wattiez, Baptiste Leroy, Patricia S Cuasnicu, Pascale Lybaert, and Elise Hennebert. Novel insights into human crisp2: localization in reproductive tissues and sperm, and molecular characterization. Biology of reproduction, 112:1167-1184, Mar 2025. URL: https://doi.org/10.1093/biolre/ioaf051, doi:10.1093/biolre/ioaf051. This article has 1 citations and is from a peer-reviewed journal.
(masai2025novelinsightsinto pages 6-7): Thibault Masai, Amandine Delnatte, Marie Dendievel, Denis Nonclercq, Annica Frau, Jean-François Simon, Vanessa Arcolia, Ruddy Wattiez, Baptiste Leroy, Patricia S Cuasnicu, Pascale Lybaert, and Elise Hennebert. Novel insights into human crisp2: localization in reproductive tissues and sperm, and molecular characterization. Biology of reproduction, 112:1167-1184, Mar 2025. URL: https://doi.org/10.1093/biolre/ioaf051, doi:10.1093/biolre/ioaf051. This article has 1 citations and is from a peer-reviewed journal.
(masai2025novelinsightsinto pages 7-8): Thibault Masai, Amandine Delnatte, Marie Dendievel, Denis Nonclercq, Annica Frau, Jean-François Simon, Vanessa Arcolia, Ruddy Wattiez, Baptiste Leroy, Patricia S Cuasnicu, Pascale Lybaert, and Elise Hennebert. Novel insights into human crisp2: localization in reproductive tissues and sperm, and molecular characterization. Biology of reproduction, 112:1167-1184, Mar 2025. URL: https://doi.org/10.1093/biolre/ioaf051, doi:10.1093/biolre/ioaf051. This article has 1 citations and is from a peer-reviewed journal.
(masai2025novelinsightsinto pages 5-6): Thibault Masai, Amandine Delnatte, Marie Dendievel, Denis Nonclercq, Annica Frau, Jean-François Simon, Vanessa Arcolia, Ruddy Wattiez, Baptiste Leroy, Patricia S Cuasnicu, Pascale Lybaert, and Elise Hennebert. Novel insights into human crisp2: localization in reproductive tissues and sperm, and molecular characterization. Biology of reproduction, 112:1167-1184, Mar 2025. URL: https://doi.org/10.1093/biolre/ioaf051, doi:10.1093/biolre/ioaf051. This article has 1 citations and is from a peer-reviewed journal.
(shkrigunov2023theapplicationof pages 8-9): Timur Shkrigunov, Victor Zgoda, Peter Klimenko, Anna Kozlova, Maria Klimenko, Andrey Lisitsa, Mark Kurtser, and Natalia Petushkova. The application of ejaculate-based shotgun proteomics for male infertility screening. Biomedicines, 12:49, Dec 2023. URL: https://doi.org/10.3390/biomedicines12010049, doi:10.3390/biomedicines12010049. This article has 2 citations.
(atab2024alpha1bglycoprotein(a1bg) pages 2-4): Ola El Atab, Barkha Gupta, Zhu Han, Jiri Stribny, Oluwatoyin A. Asojo, and Roger Schneiter. Alpha-1-b glycoprotein (a1bg) inhibits sterol-binding and export by crisp2. Journal of Biological Chemistry, 300:107910, Dec 2024. URL: https://doi.org/10.1016/j.jbc.2024.107910, doi:10.1016/j.jbc.2024.107910. This article has 4 citations and is from a domain leading peer-reviewed journal.
(atab2024alpha1bglycoprotein(a1bg) pages 12-13): Ola El Atab, Barkha Gupta, Zhu Han, Jiri Stribny, Oluwatoyin A. Asojo, and Roger Schneiter. Alpha-1-b glycoprotein (a1bg) inhibits sterol-binding and export by crisp2. Journal of Biological Chemistry, 300:107910, Dec 2024. URL: https://doi.org/10.1016/j.jbc.2024.107910, doi:10.1016/j.jbc.2024.107910. This article has 4 citations and is from a domain leading peer-reviewed journal.
(atab2024alpha1bglycoprotein(a1bg) pages 1-2): Ola El Atab, Barkha Gupta, Zhu Han, Jiri Stribny, Oluwatoyin A. Asojo, and Roger Schneiter. Alpha-1-b glycoprotein (a1bg) inhibits sterol-binding and export by crisp2. Journal of Biological Chemistry, 300:107910, Dec 2024. URL: https://doi.org/10.1016/j.jbc.2024.107910, doi:10.1016/j.jbc.2024.107910. This article has 4 citations and is from a domain leading peer-reviewed journal.
(atab2024alpha1bglycoprotein(a1bg) pages 9-11): Ola El Atab, Barkha Gupta, Zhu Han, Jiri Stribny, Oluwatoyin A. Asojo, and Roger Schneiter. Alpha-1-b glycoprotein (a1bg) inhibits sterol-binding and export by crisp2. Journal of Biological Chemistry, 300:107910, Dec 2024. URL: https://doi.org/10.1016/j.jbc.2024.107910, doi:10.1016/j.jbc.2024.107910. This article has 4 citations and is from a domain leading peer-reviewed journal.
(atab2024alpha1bglycoprotein(a1bg) pages 11-12): Ola El Atab, Barkha Gupta, Zhu Han, Jiri Stribny, Oluwatoyin A. Asojo, and Roger Schneiter. Alpha-1-b glycoprotein (a1bg) inhibits sterol-binding and export by crisp2. Journal of Biological Chemistry, 300:107910, Dec 2024. URL: https://doi.org/10.1016/j.jbc.2024.107910, doi:10.1016/j.jbc.2024.107910. This article has 4 citations and is from a domain leading peer-reviewed journal.
(shkrigunov2023theapplicationof media 5dc187ee): Timur Shkrigunov, Victor Zgoda, Peter Klimenko, Anna Kozlova, Maria Klimenko, Andrey Lisitsa, Mark Kurtser, and Natalia Petushkova. The application of ejaculate-based shotgun proteomics for male infertility screening. Biomedicines, 12:49, Dec 2023. URL: https://doi.org/10.3390/biomedicines12010049, doi:10.3390/biomedicines12010049. This article has 2 citations.
(shi2024micrornasinspermatogenesis pages 3-4): Ziyan Shi, Miao Yu, Tingchao Guo, Yu Sui, Zhiying Tian, Xiang Ni, Xinren Chen, Miao Jiang, Jingyi Jiang, Yongping Lu, and Meina Lin. Micrornas in spermatogenesis dysfunction and male infertility: clinical phenotypes, mechanisms and potential diagnostic biomarkers. Frontiers in Endocrinology, Feb 2024. URL: https://doi.org/10.3389/fendo.2024.1293368, doi:10.3389/fendo.2024.1293368. This article has 56 citations.
(shi2024micrornasinspermatogenesis pages 4-5): Ziyan Shi, Miao Yu, Tingchao Guo, Yu Sui, Zhiying Tian, Xiang Ni, Xinren Chen, Miao Jiang, Jingyi Jiang, Yongping Lu, and Meina Lin. Micrornas in spermatogenesis dysfunction and male infertility: clinical phenotypes, mechanisms and potential diagnostic biomarkers. Frontiers in Endocrinology, Feb 2024. URL: https://doi.org/10.3389/fendo.2024.1293368, doi:10.3389/fendo.2024.1293368. This article has 56 citations.
(shi2024micrornasinspermatogenesis pages 19-20): Ziyan Shi, Miao Yu, Tingchao Guo, Yu Sui, Zhiying Tian, Xiang Ni, Xinren Chen, Miao Jiang, Jingyi Jiang, Yongping Lu, and Meina Lin. Micrornas in spermatogenesis dysfunction and male infertility: clinical phenotypes, mechanisms and potential diagnostic biomarkers. Frontiers in Endocrinology, Feb 2024. URL: https://doi.org/10.3389/fendo.2024.1293368, doi:10.3389/fendo.2024.1293368. This article has 56 citations.
(fietz2024proteomicbiomarkersin pages 2-3): Daniela Fietz, Raouda Sgaier, Liza O’Donnell, Peter G. Stanton, Laura F. Dagley, Andrew I. Webb, Hans-Christian Schuppe, Thorsten Diemer, and Adrian Pilatz. Proteomic biomarkers in seminal plasma as predictors of reproductive potential in azoospermic men. Frontiers in Endocrinology, Apr 2024. URL: https://doi.org/10.3389/fendo.2024.1327800, doi:10.3389/fendo.2024.1327800. This article has 17 citations.
(fietz2024proteomicbiomarkersin pages 1-2): Daniela Fietz, Raouda Sgaier, Liza O’Donnell, Peter G. Stanton, Laura F. Dagley, Andrew I. Webb, Hans-Christian Schuppe, Thorsten Diemer, and Adrian Pilatz. Proteomic biomarkers in seminal plasma as predictors of reproductive potential in azoospermic men. Frontiers in Endocrinology, Apr 2024. URL: https://doi.org/10.3389/fendo.2024.1327800, doi:10.3389/fendo.2024.1327800. This article has 17 citations.
(fietz2024proteomicbiomarkersin pages 12-12): Daniela Fietz, Raouda Sgaier, Liza O’Donnell, Peter G. Stanton, Laura F. Dagley, Andrew I. Webb, Hans-Christian Schuppe, Thorsten Diemer, and Adrian Pilatz. Proteomic biomarkers in seminal plasma as predictors of reproductive potential in azoospermic men. Frontiers in Endocrinology, Apr 2024. URL: https://doi.org/10.3389/fendo.2024.1327800, doi:10.3389/fendo.2024.1327800. This article has 17 citations.
(parkes2024bringingproteomicsto pages 28-29): Rachel Parkes and Thomas X. Garcia. Bringing proteomics to bear on male fertility: key lessons. Expert Review of Proteomics, 21:181-203, Apr 2024. URL: https://doi.org/10.1080/14789450.2024.2327553, doi:10.1080/14789450.2024.2327553. This article has 7 citations and is from a peer-reviewed journal.
(parkes2024bringingproteomicsto pages 6-7): Rachel Parkes and Thomas X. Garcia. Bringing proteomics to bear on male fertility: key lessons. Expert Review of Proteomics, 21:181-203, Apr 2024. URL: https://doi.org/10.1080/14789450.2024.2327553, doi:10.1080/14789450.2024.2327553. This article has 7 citations and is from a peer-reviewed journal.
(parkes2024bringingproteomicsto pages 29-31): Rachel Parkes and Thomas X. Garcia. Bringing proteomics to bear on male fertility: key lessons. Expert Review of Proteomics, 21:181-203, Apr 2024. URL: https://doi.org/10.1080/14789450.2024.2327553, doi:10.1080/14789450.2024.2327553. This article has 7 citations and is from a peer-reviewed journal.
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