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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
Identity was verified before interpretation. The requested human protein is germ-cell alkaline phosphatase—GCAP, Nagao isozyme, or placental-like alkaline phosphatase—encoded by ALPG, historically and widely also called ALPPL2. It is a distinct member of the human alkaline-phosphatase family and must not be confused with placental alkaline phosphatase (ALPP/PLAP) or tissue-nonspecific alkaline phosphatase (ALPL/TNAP). The tissue-specific intestinal, placental, and germ-cell genes form a chromosome-2 cluster, whereas ALPL lies on chromosome 1. GCAP and PLAP are approximately 98% homologous and differ by only about 7–10 amino acids, explaining substantial antibody and biochemical-assay cross-reactivity (moss1992perspectivesinalkaline pages 1-1, roelofs1999heterogeneityinalkaline pages 1-2, koshida1997significanceofplacental pages 1-2).
ALPG is best annotated as an extracellular-facing, probably GPI-anchored metallo-phosphomonoesterase, EC 3.1.3.1. Its well-supported biochemical reaction is:
phosphate monoester + H₂O → alcohol + inorganic phosphate.
The enzyme family is broad rather than highly substrate-selective. No compelling ALPG-specific endogenous substrate or dedicated signaling pathway was identified in the retrieved literature. Its strongest direct biological evidence concerns expression in human germ cells and re-expression in testicular germ-cell neoplasia, especially carcinoma in situ/germ-cell neoplasia in situ and seminoma (fishman1990alkalinephosphataseisozymes pages 4-5, roelofs1999heterogeneityinalkaline pages 1-2).
| Annotation area | Key finding for human ALPG/ALPPL2 (UniProt P10696) | Evidence type | Key quantitative results | Evidence grade | Citations |
|---|---|---|---|---|---|
| Identity | Human ALPG/ALPPL2 corresponds to germ-cell alkaline phosphatase (GCAP), also called the Nagao/placental-like isozyme; it is a distinct tissue-specific alkaline-phosphatase gene in the chromosome-2 cluster and is extremely similar to placental ALP (ALPP), but separable at the transcript level from PLAP/ALPP. | Direct ALPG/GCAP evidence | GCAP reported as ~98% homologous to PLAP; placental and germ-cell forms differ by only ~7–10 amino acids. | Strong | (moss1992perspectivesinalkaline pages 1-1, roelofs1999heterogeneityinalkaline pages 1-2, koshida1997significanceofplacental pages 1-2) |
| Enzyme reaction | ALPG is an alkaline phosphatase (EC 3.1.3.1) and therefore catalyzes hydrolysis of phosphate monoesters to release inorganic phosphate under alkaline conditions. | Family inference anchored by isozyme identity | No ALPG-specific kinetic constants retrieved. | Moderate | (moss1992perspectivesinalkaline pages 1-1, jassas2023currentstatusof pages 6-7) |
| Substrate specificity | No high-confidence ALPG-specific physiological substrate was identified in the retrieved evidence; like other alkaline phosphatases, it is best described as broadly phosphomonoester-hydrolyzing rather than highly substrate-specific. | Mostly family inference; ALPG-specific literature limited | None retrieved for ALPG-specific natural substrates. | Limited | (jassas2023currentstatusof pages 5-6, jassas2023currentstatusof pages 6-7) |
| Cofactors/mechanism | Direct ALPG-specific cofactor data were not retrieved, but mammalian alkaline phosphatases are metalloenzymes using a phosphoserine intermediate and typically require 2 Zn2+ and 1 Mg2+ at the active site; an essential Ca2+ contribution is also described in the review literature. | Family inference | Active-site scheme reported for mammalian APs: 2 Zn2+, 1 Mg2+, plus essential Ca2+ contribution. | Moderate | (jassas2023currentstatusof pages 5-6, jassas2023currentstatusof pages 6-7) |
| Structure | GCAP/ALPG belongs to the tissue-specific AP subfamily with gene organization resembling PLAP and IAP; historical sequence data place GCAP near ~513 aa precursor length with mature protein in the high-480 aa range, consistent with a processed membrane enzyme. | Direct ALPG evidence plus family context | Predicted precursor length ~513 aa; mature length in 480s; six allelic variants reported historically. | Moderate | (fishman1990alkalinephosphataseisozymes pages 2-4) |
| Localization | ALPG is expected to be a cell-surface membrane protein attached by a COOH-terminal GPI anchor, like closely related placental and intestinal APs; older literature directly proved GPI anchoring for PLAP and predicted the same for GCAP, while family reviews state ALPs are membrane-associated via GPI. | Mixed: direct for AP family/PLAP, inferential for ALPG | No ALPG-specific microscopy/localization quantitation retrieved. | Moderate | (moss1992perspectivesinalkaline pages 1-1, fishman1990alkalinephosphataseisozymes pages 2-4) |
| Normal expression | GCAP/ALPG is a germ-cell/testis-associated alkaline phosphatase; older tissue studies and reviews indicate expression in normal testis and broader low-level placental-type AP immunoreactivity in some tissues, but high-confidence modern tissue-resolution data specific to ALPG were not retrieved here. | Direct ALPG evidence, but limited and partly assay-conflated with PLAP | Testis contains Nagao-type AP; assay studies detected placental-type ALP signal in lung, testis, small intestine, and colon, though isozyme discrimination was imperfect. | Limited-Moderate | (fishman1990alkalinephosphataseisozymes pages 4-5, hayashi1991improvedmonoclonalimmunocatalytic pages 6-8) |
| Cancer expression | ALPG/GCAP is strongly linked to testicular germ-cell neoplasia, especially CIS and seminoma; RT-PCR/primer-extension evidence indicates CIS and seminoma predominantly express GCAP, while embryonal carcinoma variably expresses GCAP or PLAP. | Direct ALPG evidence | Seminoma tissue showed GCAP/TUAP elevations reported historically at ~10–100×; IAP increases ~2–10×; CIS and seminoma predominantly GCAP-positive at transcript level. | Strong | (fishman1990alkalinephosphataseisozymes pages 4-5, roelofs1999heterogeneityinalkaline pages 1-2) |
| Clinical applications | Historically used mainly as a tumor marker axis in seminoma/testicular germ-cell tumors and in antibody-based detection approaches; because PLAP and GCAP are highly similar, many assays measured PLAP/PLAP-like activity rather than uniquely resolving ALPG. | Mixed: direct tumor relevance, imperfect isozyme specificity in assays | In 673 serum samples, PLAP-positive threshold >100 mKAU/L; serum PLAP elevated in ~51% of seminoma patients, mean ~5× normal; false positives 1.6%; combining PLAP + HCG-B + LDH gave 82% positive identification for seminoma. | Moderate | (fishman1990alkalinephosphataseisozymes pages 6-6, koshida1997significanceofplacental pages 1-2) |
| 2024 ALPPL2-FEV1 finding | In a 2024 proteomic/MR study, circulating ALPPL2 was one of the strongest observational serum correlates of lower FEV1, but available evidence did not support ALPPL2 as an MR-validated causal determinant of lung function. | Direct ALPPL2 evidence | AGES-Reykjavik observational n=1,479 across 4,782 SOMAmers: ALPPL2 beta = -0.087, 95% CI -0.113 to -0.061, p = 1.23×10^-10, FDR = 1.96×10^-7; ever-smokers beta = -0.097, p = 1.05×10^-7. MR used n=5,368 proteogenetic samples and FEV1 GWAS n=400,102; ALPPL2 was not among the eight FDR-significant MR proteins. | Strong for biomarker association; limited for causality | (axelsson2024proteomicassociationswith pages 4-6, axelsson2024proteomicassociationswith pages 6-7, axelsson2024proteomicassociationswith pages 1-2) |
Table: This table summarizes the current evidence for human ALPG/ALPPL2 function, localization, expression, and clinical relevance, while clearly separating direct ALPG-specific findings from broader alkaline-phosphatase family inference. It is useful for rapid evidence grading and for identifying where the literature remains sparse or assay-confounded.
The supplied description—human UniProt P10696, alkaline phosphatase germ-cell type, EC 3.1.3.1, aliases ALP-1, GCAP, Nagao isozyme, placental-like alkaline phosphatase—aligns with the historical molecular literature. Cloning work established that the seminoma-derived Nagao isozyme is encoded by a separate germ-cell alkaline-phosphatase gene rather than by ALPP itself. Reviews place this gene with ALPP and ALPI in the tissue-specific alkaline-phosphatase cluster at chromosome 2q34–q37/2q37 (roelofs1999heterogeneityinalkaline pages 1-2, fishman1990alkalinephosphataseisozymes pages 2-4, hayashi1991improvedmonoclonalimmunocatalytic pages 6-8).
The organism is therefore unequivocally Homo sapiens. No evidence concerning a similarly named non-human gene was used. The supplied InterPro/Pfam assignments—alkaline-phosphatase domain, active-site signature, and core fold—are consistent with the enzyme-family literature, which recognizes GCAP as one of four major human alkaline-phosphatase isozymes (jassas2023currentstatusof pages 5-6, roelofs1999heterogeneityinalkaline pages 1-2).
A critical nomenclature caveat is that older papers frequently use “placental-type,” “PLAP-like,” or even “PLAP” for measurements that do not molecularly distinguish ALPG from ALPP. Only transcript-resolving studies or explicitly GCAP-selective experiments should be treated as gene-specific.
ALPG is a phosphomonoester phosphohydrolase, EC 3.1.3.1. Alkaline phosphatases remove phosphate groups from diverse phosphate monoesters, with maximal assay activity under alkaline conditions. Accordingly, the defensible functional annotation is broad phosphomonoester hydrolysis, not a narrowly defined substrate-specific reaction (jassas2023currentstatusof pages 5-6, moss1992perspectivesinalkaline pages 1-1).
No high-confidence physiological substrate unique to ALPG was recovered. Common laboratory substrates such as p-nitrophenyl phosphate report generic alkaline-phosphatase activity but do not establish an endogenous substrate. Claims that ALPG directly controls DNA repair, cell-cycle progression, apoptosis, steroidogenesis, or gametogenesis appear in a 2023 review, but the retrieved material did not supply sufficiently precise ALPG-specific mechanistic experiments to establish these as direct pathways (jassas2023currentstatusof pages 5-6). Those proposed functions should therefore be considered hypotheses or broad associations rather than settled primary functions.
The following mechanism is strongly established for mammalian alkaline phosphatases but is principally a family-level inference for ALPG. A catalytic serine attacks the substrate phosphate, forming a covalent phosphoserine intermediate; hydrolysis then releases inorganic phosphate. In suitable conditions, an alcohol can replace water as acceptor, producing transphosphorylation. Mammalian alkaline phosphatases use a metal-containing active site, typically described as two Zn²⁺ and one Mg²⁺ per monomer, with an additional functionally important Ca²⁺ site in mammalian enzymes (jassas2023currentstatusof pages 5-6, jassas2023currentstatusof pages 6-7).
Because ALPG preserves the alkaline-phosphatase catalytic domain and active-site signature and is approximately 98% homologous to ALPP, this mechanism is a strong structural/evolutionary inference. Nevertheless, ALPG-specific metal stoichiometry, kinetic constants, substrate panel, and catalytic-residue mutagenesis were not recovered and should not be presented as directly measured for P10696.
Historical sequence analyses place GCAP among approximately 513-residue alkaline-phosphatase precursors, with a processed mature chain in the high-480-residue range. The tissue-specific ALP genes share similar exon–intron organization, consistent with recent gene duplication and functional conservation; six GCAP allelic variants were reported historically (fishman1990alkalinephosphataseisozymes pages 2-4).
Alkaline phosphatases function as homodimeric glycoproteins. ALPG is expected to enter the secretory pathway through an N-terminal signal peptide, undergo glycosylation and C-terminal processing, and be displayed as a mature membrane-associated enzyme. Dimerization and detailed domain architecture are supported most strongly by homologous mammalian AP structures rather than an ALPG-specific structure in the retrieved set (jassas2023currentstatusof pages 5-6, fishman1990alkalinephosphataseisozymes pages 2-4).
Human alkaline phosphatases are generally attached to the plasma membrane by a C-terminal glycosylphosphatidylinositol (GPI) anchor. This positions the catalytic domain on the extracellular/luminal face of the membrane, where it can hydrolyze extracellular phosphate monoesters. Soluble enzyme in serum or culture medium can arise through shedding, release, or membrane turnover (moss1992perspectivesinalkaline pages 1-1).
For GCAP specifically, older sequence-era literature explicitly described GPI attachment as expected by homology, while direct anchor chemistry had then been established for PLAP but not yet confirmed at the corresponding GCAP residue. Thus, extracellular-facing GPI-anchored plasma-membrane localization is highly plausible and consistent with UniProt precursor annotation, but the retrieved primary literature provides stronger direct evidence for the family/ALPP than for ALPG itself (fishman1990alkalinephosphataseisozymes pages 4-5, fishman1990alkalinephosphataseisozymes pages 2-4).
Direct historical evidence identifies Nagao-type/GCAP activity in normal human testis. GCAP is consequently described as germ-cell alkaline phosphatase and has also been reported in germ cells of ovary. However, claims of strict germ-cell exclusivity should be avoided: older immunocatalytic surveys detected placental-type ALP signals in lung, testis, intestine, and colon, but those assays often could not reliably separate ALPG from ALPP (fishman1990alkalinephosphataseisozymes pages 4-5, jassas2023currentstatusof pages 5-6, hayashi1991improvedmonoclonalimmunocatalytic pages 6-8).
The normal physiological purpose of ALPG remains poorly resolved. Its extracellular catalytic orientation suggests local regulation of phosphorylated molecules in the germ-cell microenvironment, but a particular natural substrate or indispensable germ-cell biochemical pathway has not been demonstrated in the retrieved evidence.
The strongest gene-specific functional context is testicular germ-cell neoplasia. Immunohistochemistry detects PLAP/GCAP-reactive protein in carcinoma in situ, seminoma, and embryonal carcinoma, but antibodies alone generally cannot separate the two nearly identical isozymes. Roelofs et al. addressed this limitation using RT-PCR and primer extension: carcinoma in situ and seminoma predominantly expressed GCAP transcripts, whereas embryonal carcinoma exhibited variable GCAP-versus-PLAP expression (published October 1999; https://doi.org/10.1002/(SICI)1096-9896(199910)189:2%3C236::AID-PATH411%3E3.0.CO;2-J) (roelofs1999heterogeneityinalkaline pages 1-2).
Historical biochemical measurements reported approximately 10–100-fold elevations of GCAP/TUAP activity in seminoma tissue, compared with roughly 2–10-fold increases in intestinal alkaline phosphatase. These data support GCAP as a differentiation-associated tumor antigen, but older isozyme terminology and assay cross-reactivity limit exact gene attribution (fishman1990alkalinephosphataseisozymes pages 4-5).
ALPG does not currently have a well-established receptor-like signaling role. The most defensible pathway placement is in extracellular phosphate-monoester metabolism at the cell surface. Family chemistry supports conversion of extracellular phosphorylated substrates to dephosphorylated products plus inorganic phosphate, but there is insufficient evidence to nominate a dominant ALPG substrate or downstream signaling cascade.
The 2023 medicinal-chemistry review proposed roles for GCAP in germ-cell maturation, steroidogenesis, DNA repair, cell-cycle progression, and apoptosis. These claims provide useful research hypotheses, but without direct substrate identification, loss-of-function rescue experiments, or ALPG-selective pharmacology, they should not be elevated to established mechanistic annotations (published May 2023; https://doi.org/10.1039/D3RA01888A) (jassas2023currentstatusof pages 5-6, jassas2023currentstatusof pages 6-7).
Placental-type alkaline-phosphatase immunostaining remains historically important for recognizing germ-cell tumors, particularly seminoma and precursor lesions. Its practical strength is strong tumor-associated expression; its central weakness is inability of many antibodies to distinguish ALPG/GCAP from ALPP/PLAP (roelofs1999heterogeneityinalkaline pages 1-2).
In a clinical series comprising 673 serum samples, a PLAP immunocatalytic threshold above 100 mKAU/L identified elevated serum signal in approximately 51% of seminoma patients, with a mean elevation around fivefold above normal. False-positive results occurred in 1.6% of samples. Combining PLAP with β-hCG and LDH yielded an 82% positive-identification rate for seminoma. Smoking can elevate PLAP-like serum measurements, and the assay depended on both intact immunoreactivity and catalytic activity, so these figures cannot be interpreted as performance of an ALPG-specific assay (published June 1997; https://doi.org/10.1046/j.1464-410X.1996.74324.x) (koshida1997significanceofplacental pages 1-2).
Antibody-based immunoassays, radiolocalization, and experimental radioimmunotherapy against placental-type ALP were explored historically. These approaches demonstrate targetability but do not establish an approved ALPG-selective therapy, and cross-reactivity with ALPP remains a major translational constraint (fishman1990alkalinephosphataseisozymes pages 4-5, fishman1990alkalinephosphataseisozymes pages 6-6).
The 2023 inhibitor review documents continued development of heterocyclic alkaline-phosphatase inhibitors. However, most compounds are not demonstrably selective for ALPG over the closely related ALPP and other human AP isozymes. Current medicinal chemistry therefore supports ALPG as a potentially druggable cell-surface enzyme but not yet as a clinically validated, isozyme-selective therapeutic target (jassas2023currentstatusof pages 5-6, jassas2023currentstatusof pages 6-7).
The most substantive 2023–2024 ALPPL2-specific development retrieved was a January 2024 proteomic study of forced expiratory volume. In 1,479 AGES-Reykjavik participants, 4,782 serum SOMAmer measurements were tested against FEV₁. ALPPL2 was among the strongest observational associations: β = −0.087, 95% CI −0.113 to −0.061, P = 1.23×10⁻¹⁰, FDR = 1.96×10⁻⁷. Among ever-smokers, β was −0.097 with P = 1.05×10⁻⁷ (published January 2024; https://doi.org/10.1186/s12931-023-02587-z) (axelsson2024proteomicassociationswith pages 4-6, axelsson2024proteomicassociationswith pages 6-7).
The causal analysis used genotype/proteomic data from 5,368 participants and an FEV₁ GWAS of 400,102 individuals. Of 257 instrumented proteins, eight passed the MR false-discovery threshold, but ALPPL2 was not reported among them; strong colocalization was reported only for THBS2. Reverse MR also produced no significant protein effects after multiple-testing correction. Therefore, circulating ALPPL2 is currently an observational biomarker of lower FEV₁, not a demonstrated causal regulator of lung function (axelsson2024proteomicassociationswith pages 4-6, axelsson2024proteomicassociationswith pages 1-2).
This result should also be interpreted cautiously because affinity reagents may recognize closely related isoforms or protein complexes. Orthogonal mass spectrometry or ALPG-specific immunoassays would be needed to establish that the circulating signal uniquely represents P10696.
The literature supports three conclusions with high confidence:
Major unresolved issues are the identity and in-vivo concentration of physiological substrates, direct ALPG-specific kinetic constants and metal dependence, definitive modern cell-resolution expression maps, the biological consequence of enzymatic activity in germ cells and tumors, and development of reagents selective over ALPP. Assertions about broad signaling, fertility, or cancer-driving roles should remain provisional until supported by ALPG-selective perturbation and rescue experiments.
Overall, ALPG should presently be regarded primarily as a cell-surface alkaline-phosphatase enzyme and germ-cell/tumor differentiation antigen—not as a proven signaling receptor or validated causal oncogene.
References
(moss1992perspectivesinalkaline pages 1-1): D W Moss. Perspectives in alkaline phosphatase research. Clinical chemistry, 38 12:2486-92, Dec 1992. URL: https://doi.org/10.1093/clinchem/38.12.2486, doi:10.1093/clinchem/38.12.2486. This article has 133 citations and is from a highest quality peer-reviewed journal.
(roelofs1999heterogeneityinalkaline pages 1-2): Helene Roelofs, Thomas Manes, Ton Janszen, Jos� L. Mill�n, J. Wolter Oosterhuis, and Leendert H. J. Looijenga. Heterogeneity in alkaline phosphatase isozyme expression in human testicular germ cell tumours: an enzyme‐/immunohistochemical and molecular analysis. The Journal of Pathology, 189:236-244, Oct 1999. URL: https://doi.org/10.1002/(sici)1096-9896(199910)189:2<236::aid-path411>3.0.co;2-j, doi:10.1002/(sici)1096-9896(199910)189:2<236::aid-path411>3.0.co;2-j. This article has 55 citations.
(koshida1997significanceofplacental pages 1-2): K. Koshida, Tadao Uchibayashi, Hajime Yamamoto, and Kazuyuki Hirano. Significance of placental alkaline phosphatase (plap) in the monitoring of patients with seminoma. British journal of urology, 77 1:138-42, Jun 1997. URL: https://doi.org/10.1046/j.1464-410x.1996.74324.x, doi:10.1046/j.1464-410x.1996.74324.x. This article has 44 citations.
(fishman1990alkalinephosphataseisozymes pages 4-5): William H. Fishman. Alkaline phosphatase isozymes: recent progress. Clinical biochemistry, 23 2:99-104, Apr 1990. URL: https://doi.org/10.1016/0009-9120(90)80019-f, doi:10.1016/0009-9120(90)80019-f. This article has 213 citations and is from a peer-reviewed journal.
(jassas2023currentstatusof pages 6-7): Rabab S. Jassas, Nafeesa Naeem, Amina Sadiq, Rabia Mehmood, Noof A. Alenazi, Munirah M. Al-Rooqi, Ehsan Ullah Mughal, Reem I. Alsantali, and Saleh A. Ahmed. Current status of n-, o-, s-heterocycles as potential alkaline phosphatase inhibitors: a medicinal chemistry overview. RSC Advances, 13:16413-16452, May 2023. URL: https://doi.org/10.1039/d3ra01888a, doi:10.1039/d3ra01888a. This article has 29 citations and is from a peer-reviewed journal.
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(hayashi1991improvedmonoclonalimmunocatalytic pages 6-8): Hayashi, Yuji, Mitani, Takahiko, Kurono, Masayasu, Hirano, Kazuyuki, Kyozo, Iino, Domar, Ulla, Stigbrand, and Torgny. Improved monoclonal immunocatalytic assays (micas) for human alkaline phosphatase isozymes. ArXiv, 41:71, Sep 1991. URL: https://doi.org/10.14921/jscc1971b.20.3_125, doi:10.14921/jscc1971b.20.3_125. This article has 12 citations.
(fishman1990alkalinephosphataseisozymes pages 6-6): William H. Fishman. Alkaline phosphatase isozymes: recent progress. Clinical biochemistry, 23 2:99-104, Apr 1990. URL: https://doi.org/10.1016/0009-9120(90)80019-f, doi:10.1016/0009-9120(90)80019-f. This article has 213 citations and is from a peer-reviewed journal.
(axelsson2024proteomicassociationswith pages 4-6): Gisli Thor Axelsson, Thorarinn Jonmundsson, Youngjae Woo, Elisabet Alexandra Frick, Thor Aspelund, Joseph J. Loureiro, Anthony P. Orth, Lori L. Jennings, Gunnar Gudmundsson, Valur Emilsson, Valborg Gudmundsdottir, and Vilmundur Gudnason. Proteomic associations with forced expiratory volume: a mendelian randomisation study. Respiratory Research, Jan 2024. URL: https://doi.org/10.1186/s12931-023-02587-z, doi:10.1186/s12931-023-02587-z. This article has 8 citations and is from a domain leading peer-reviewed journal.
(axelsson2024proteomicassociationswith pages 6-7): Gisli Thor Axelsson, Thorarinn Jonmundsson, Youngjae Woo, Elisabet Alexandra Frick, Thor Aspelund, Joseph J. Loureiro, Anthony P. Orth, Lori L. Jennings, Gunnar Gudmundsson, Valur Emilsson, Valborg Gudmundsdottir, and Vilmundur Gudnason. Proteomic associations with forced expiratory volume: a mendelian randomisation study. Respiratory Research, Jan 2024. URL: https://doi.org/10.1186/s12931-023-02587-z, doi:10.1186/s12931-023-02587-z. This article has 8 citations and is from a domain leading peer-reviewed journal.
(axelsson2024proteomicassociationswith pages 1-2): Gisli Thor Axelsson, Thorarinn Jonmundsson, Youngjae Woo, Elisabet Alexandra Frick, Thor Aspelund, Joseph J. Loureiro, Anthony P. Orth, Lori L. Jennings, Gunnar Gudmundsson, Valur Emilsson, Valborg Gudmundsdottir, and Vilmundur Gudnason. Proteomic associations with forced expiratory volume: a mendelian randomisation study. Respiratory Research, Jan 2024. URL: https://doi.org/10.1186/s12931-023-02587-z, doi:10.1186/s12931-023-02587-z. This article has 8 citations and is from a domain leading peer-reviewed journal.