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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 target gene is Egf from Mus musculus (mouse), encoding pro-epidermal growth factor (prepro‑EGF/proEGF), a membrane-anchored precursor that is proteolytically processed to generate mature epidermal growth factor (EGF), the canonical ligand for EGFR/ErbB1. This identity is explicitly described in mouse primary studies that sequenced the 1217-aa precursor and examined its tissue distribution and processing, and in an authoritative review that synthesizes gene organization, precursor structure and physiology. (scott1985thestructureand pages 1-4, zeng2014epidermalgrowthfactor pages 2-4)
| Category | Key points | Best supporting sources |
|---|---|---|
| Identity | Target verified as Mus musculus Egf, UniProt P01132, encoding pro-epidermal growth factor / prepro-EGF, the precursor of mature EGF. Literature distinguishes the mouse membrane-anchored precursor from mature soluble EGF. | (zeng2014epidermalgrowthfactor pages 2-2, zeng2014epidermalgrowthfactor pages 2-4, scott1985thestructureand pages 1-4) |
| Protein architecture | Mouse prepro-EGF is a large type I transmembrane glycoprotein of about 1217 aa with an N-terminal signal peptide, multiple EGF-like repeats in the extracellular region, the 53-aa mature EGF segment near the C-terminus, a single transmembrane domain, and a short cytoplasmic tail; potential N-glycosylation and multiple dibasic cleavage sites are present. A figure-based domain map shows seven EGF-like peptides, the mature EGF moiety, glycosylation sites, and candidate processing sites. | (zeng2014epidermalgrowthfactor pages 2-2, scott1985thestructureand pages 4-7, scott1985thestructureand pages 1-4, scott1985thestructureand media d2d35de8) |
| Processing/biogenesis | Mature EGF is produced by proteolytic cleavage/shedding from membrane pro-EGF. Processing is tissue-specific: submaxillary gland efficiently processes/stores mature low-MW EGF in secretory granules, whereas kidney contains predominantly unprocessed high-MW precursor and urinary high-MW EGF species, implying partial distal proteolysis rather than complete maturation in situ. In platelets, cleavage between the EGF domain and TM segment can release biologically active HMW-EGF; ADAMDEC1 was shown to mediate this in a platelet context. | (zeng2014epidermalgrowthfactor pages 2-2, chen2017thesolubleprotease pages 1-2, scott1985thestructureand pages 4-7, lakshmanan1990identificationofproepidermal pages 1-3) |
| Localization/expression | Highest expression is reported in submaxillary/salivary gland and kidney. In kidney, Egf mRNA/protein localize mainly to distal convoluted tubules and thick ascending limb/apical tubular membranes; expression is also reported in tooth buds and lower levels in mammary gland, pancreas, intestine, ovary, spleen, lung, pituitary, and liver. | (zeng2014epidermalgrowthfactor pages 2-4, scott1985thestructureand pages 4-7, scott1985thestructureand pages 1-4, lakshmanan1990identificationofproepidermal pages 1-3) |
| Molecular function | The primary function is EGFR ligand activity: mature EGF, and in some contexts pro-EGF itself, binds EGFR/ErbB1, triggering receptor dimerization and tyrosine kinase activation to regulate cell proliferation, differentiation, survival, migration, and epithelial repair. Membrane-bound precursor may additionally support juxtacrine/paracrine signaling. | (zeng2014epidermalgrowthfactor pages 2-2, zeng2014epidermalgrowthfactor pages 2-4, fisher1990metabolismandeffects pages 2-3) |
| Pathways | Canonical downstream pathways include Ras/Raf/MEK/ERK, PI3K/AKT/mTOR, JAK/STAT, and PLC/PKC; older mechanistic work also links EGF signaling to Na+/H+ exchange, intracellular Ca2+ changes, and increased nutrient transport. | (zeng2014epidermalgrowthfactor pages 2-4, fisher1990metabolismandeffects pages 2-3) |
| Phenotypes/models | Egf knockout mice reportedly show no overt gross phenotype, consistent with redundancy among EGFR ligands. In contrast, transgenic EGF overexpression causes low birth weight/stunted growth and reproductive defects, supporting dosage-sensitive developmental roles. | (zeng2014epidermalgrowthfactor pages 2-4) |
| Quantitative data | Reported values include: mouse prepro-EGF 1217 aa; mature EGF 53 aa (~6 kDa); plasma EGF about 1 ng/mL; adult male submaxillary gland EGF about 1000 ng/mg wet tissue versus about 70 ng/mg in females; submaxillary gland:kidney protein ratio about 2000:1 despite only about 2:1 mRNA ratio; male:female submaxillary mRNA about 10:1; urinary pro-EGF species detected at about 165, 116, 97, 66, and 56 kDa. | (zeng2014epidermalgrowthfactor pages 2-2, scott1985thestructureand pages 4-7, lakshmanan1990identificationofproepidermal pages 1-3) |
| Notes/limitations | Direct recent (2023–2024) mouse Egf-specific primary literature is limited relative to the broader EGFR ligand field; many newer studies focus on EGFR or other ligands (e.g., HB-EGF, TGF-α). Some cleavage mechanisms are context-dependent, and evidence for specific sheddases of mouse renal/salivary pro-EGF remains less definitive than the general membrane-precursor model. | (zeng2014epidermalgrowthfactor pages 2-4, chen2017thesolubleprotease pages 1-2, scott1985thestructureand pages 4-7) |
Table: This table condenses the key functional-annotation findings for mouse Egf (UniProt P01132), covering identity, protein structure, processing, localization, signaling, phenotypes, and quantitative observations. It is useful as a citation-linked summary of the strongest evidence already gathered.
Mouse prepro‑EGF is a large type I transmembrane glycoprotein (~1217 amino acids, ~133 kDa predicted core) with an N‑terminal signal peptide, a large extracellular region containing multiple cysteine-rich EGF-like repeats, a single transmembrane helix near the C-terminus, and a short cytoplasmic tail. (scott1985thestructureand pages 1-4, zeng2014epidermalgrowthfactor pages 2-4)
A key concept is that EGF is not synthesized as a standalone secreted peptide, but as part of this precursor; the mature EGF ligand is a 53-aa (~6–8 kDa) segment located immediately N‑terminal to the transmembrane region that can be released by proteolysis. (zeng2014epidermalgrowthfactor pages 2-2, zeng2014epidermalgrowthfactor pages 2-4)
A figure from the original mouse precursor characterization visually maps: (i) multiple EGF-like peptides, (ii) the mature EGF domain, (iii) N‑glycosylation sites, (iv) dibasic candidate processing sites, and (v) the transmembrane anchor. (scott1985thestructureand media d2d35de8)
“Processing” refers to proteolytic cleavage of proEGF to release soluble EGF-containing ligands. In the mouse submaxillary gland, EGF is synthesized and processed and only the mature ~6 kDa EGF species is detected in secretory granules, consistent with regulated exocytotic release. (zeng2014epidermalgrowthfactor pages 2-2)
A second important concept is that processing is tissue- and context-dependent: kidney expresses high Egf mRNA but predominantly retains high-molecular-weight precursor forms, with little evidence of complete maturation to 6 kDa EGF in situ. (scott1985thestructureand pages 4-7, lakshmanan1990identificationofproepidermal pages 1-3)
The primary molecular function of EGF (and in some contexts proEGF) is binding to EGFR (ErbB1/HER1), triggering receptor dimerization and activation of EGFR’s intrinsic tyrosine kinase, thereby controlling cellular proliferation, differentiation, survival and motility—especially in epithelial contexts. (zeng2014epidermalgrowthfactor pages 2-4, fisher1990metabolismandeffects pages 2-3)
Mouse prepro‑EGF was deduced from cDNA as a 1217-aa precursor with a signal peptide, multiple EGF-like motifs, potential N-glycosylation sites, and a ~20-aa hydrophobic transmembrane segment near the C-terminus. (scott1985thestructureand pages 1-4, scott1985thestructureand pages 4-7)
Evidence from early mouse work supports a membrane-anchored precursor model, including the hydrophobic C-terminal segment that could span the plasma membrane and a basic C-terminus that could stabilize membrane association. (scott1985thestructureand pages 4-7)
In kidney, proEGF is reported to accumulate as prepro‑EGF associated with the apical membrane of epithelial cells; mature 6 kDa EGF is not readily detectable in kidney by immunostaining/biochemical assays in the reviewed and primary literature. (zeng2014epidermalgrowthfactor pages 2-4, lakshmanan1990identificationofproepidermal pages 1-3)
Mouse Egf mRNA is highest in submaxillary (salivary) gland and is also surprisingly high in the kidney. In situ hybridization localizes kidney Egf mRNA predominantly to the cortex and especially to distal convoluted tubules. (scott1985thestructureand pages 4-7)
The same mouse study reports additional expression (descending) in lactating mammary gland, pancreas, small intestine, ovary, spleen, lung, pituitary, and liver. (scott1985thestructureand pages 4-7)
A strong male-biased expression occurs in mouse submaxillary gland: the mRNA level is ~10:1 male:female in the classic dot-blot analysis, and adult male submaxillary gland contains far higher EGF protein than females (quantitatively summarized in the later review). (scott1985thestructureand pages 4-7, zeng2014epidermalgrowthfactor pages 2-2)
In secretory tissues such as the mouse submaxillary gland, EGF is synthesized and processed and stored in secretory granules; only the mature ~6 kDa EGF is detected in those granules and released via exocytosis. Adrenergic stimulation (e.g., phenylephrine or stress) can dramatically increase EGF levels in saliva and blood. (zeng2014epidermalgrowthfactor pages 2-2, zeng2014epidermalgrowthfactor pages 2-4)
Quantitatively, the review reports very high submaxillary gland EGF in adult male mice (~1000 ng/mg wet tissue) compared with females (~70 ng/mg), with plasma EGF around ~1 ng/mL and no sex difference in plasma. (zeng2014epidermalgrowthfactor pages 2-2)
Despite high kidney Egf mRNA, early experimental work found a striking discordance between mRNA and protein: the submaxillary:kidney EGF protein ratio ~2000:1 versus only ~2:1 at mRNA level, and metabolic labeling/immunoprecipitation showed kidney predominantly contains an ~130 kDa precursor with no clear evidence of mature EGF production under those conditions. (scott1985thestructureand pages 4-7)
Urine and kidney extracts contain high-molecular-weight EGF-immunoreactive species consistent with proEGF and partial proteolysis products. In adult mouse urine, immunoblotting detected a major proEGF band at ~165 kDa and additional EGF-containing species at ~116, 97, 66, and 56 kDa, while 6 kDa EGF was not detected by those assays. (lakshmanan1990identificationofproepidermal pages 1-3)
In a platelet system (human-focused but mechanistically informative for proEGF processing biology), proEGF was found on platelet membranes and converted to a soluble high-molecular-weight EGF by a single cleavage between the EGF domain and the transmembrane region, generating an EGFR-activating ligand; the study identified ADAMDEC1 as the soluble protease mediating this conversion in activated platelets. (chen2017thesolubleprotease pages 1-2)
EGF binding activates EGFR tyrosine kinase and triggers multiple downstream cascades including Ras/Raf/MEK/ERK, PI3K/AKT/mTOR, JAK/STAT, and PLC/PKC, shaping cell proliferation, differentiation and apoptosis and broader physiology such as organ development, regeneration and ion transport. (zeng2014epidermalgrowthfactor pages 2-4)
Mechanistic endocrine-review evidence also links EGF stimulation to early physiological outputs including activation of Na+/H+ exchange (alkalinization), increased intracellular Ca2+, and increased amino acid and glucose transport; receptor complexes are internalized and degraded in lysosomes, and prolonged receptor occupancy can be required for mitogenesis. (fisher1990metabolismandeffects pages 2-3)
Given the localization of Egf mRNA/proEGF to distal nephron segments (distal convoluted tubule; apical membrane association) and the observation of limited mature EGF release in kidney, one interpretation advanced in the early mouse precursor study is that unprocessed membrane proEGF could support specialized functions in distal tubular physiology, where Na+/H+ exchange is prominent and growth factor signaling can regulate this antiporter. (scott1985thestructureand pages 4-7)
Multiple sources report that Egf-null mice show no overt phenotype, consistent with compensatory signaling by other EGFR ligands. In a widely cited genetic study, targeted removal of EGF (with amphiregulin and TGFα combinations) produced animals that were generally viable and fertile, but revealed strong mammary phenotypes when amphiregulin was absent. (luetteke1999targetedinactivationof pages 1-2, sibilia2007theepidermalgrowth pages 2-4)
Molecular validation in the mammary-development study includes northern and western evidence that EGF transcript/protein products are absent from salivary gland and kidney (and mature ~6 kDa EGF not detected) in EGF-null animals, confirming true ligand loss. (luetteke1999targetedinactivationof pages 2-3)
In the Egf/Areg/Tgfa combinatorial knockout framework, amphiregulin is essential for pubertal ductal outgrowth, while EGF and TGFα support lactogenesis. Triple-null dams frequently failed to nurse effectively; triple-null glands had poorly organized/differentiated alveoli and reduced milk-gene expression, and Stat5a phosphorylation was conspicuously decreased in AR-deficient contexts (especially double/triple nulls), linking EGFR-ligand signaling to lactation-associated STAT activation. (luetteke1999targetedinactivationof pages 1-2, luetteke1999targetedinactivationof pages 6-7)
Transgenic mice widely expressing an engineered EGF precursor were “consistently born at half the normal weight” and reached almost 80% of normal weight as adults, with associated reductions in serum IGFBP-3 and changes in growth plate chondrocytes/osteoblast localization. (chan2000expressionofepidermal pages 1-2)
Direct 2023–2024 mouse studies focused specifically on Egf/proEGF (as opposed to EGFR signaling broadly or other ligands) are relatively sparse in the retrieved full texts; however, several 2024 studies provide updated mechanistic context for EGFR-ligand biology relevant to interpreting Egf function.
A 2024 preprint quantitatively differentiates EGFR ligands by binding affinity and shedding sensitivity, classifying EGF among high-affinity ligands (apparent Kd 0.1–1 nM) and noting that ADAM17-mediated shedding occurs for several ligands but not for EGF (nor BTC) in the cited probe-based shedding assays. The work links ADAM17-dependent ligand shedding to propagation of ERK activation waves during collective migration and reports that low-affinity ligands can act as long-range signal transmitters; in vivo, EREG-deficient ERK-biosensor mice show impaired ERK wave propagation and cell migration during skin wound repair. These results refine how different EGFR ligands (including EGF) may contribute to spatial signaling dynamics in tissues. (deguchi2024lowaffinityligandsof pages 1-4)
In a 2024 mouse study of seizure-induced hippocampal remodeling, EGFR signaling is shown to be a key driver of conversion of neural stem cells into reactive phenotypes, with EGFR inhibition by gefitinib preventing reactive NSC induction and preserving neurogenesis. Quantitatively, hippocampal ERK1/2 phosphorylation increased ~8-fold at 1.5 h post-kainic acid and remained ~10–20-fold elevated later; EGFR abundance increased and became significant at 72 h (~15-fold, P=0.043). Although the ligand emphasized is HB-EGF rather than EGF, the study exemplifies modern in vivo pharmacologic and signaling readouts used to interrogate EGFR-ligand axes in mouse biology. (pastoralonso2024hbegfactivatesegfr pages 1-2)
A 2024 meeting abstract reports that EGF signaling maintains hepatocyte ECM1 expression via STAT1 S727 phosphorylation and promoter binding, and that IFNγ/NRF2 disrupts this axis in chronic liver disease contexts. The excerpted material does not provide detailed quantitative measurements, so these conclusions should be treated as preliminary until full peer-reviewed data are available. (li2024egfstat1maintainedecm1expression pages 1-5)
Mouse genetics for pathway dissection. Egf null and combinatorial EGFR-ligand knockouts (e.g., Egf/Areg/Tgfa) are used to separate ligand-specific versus redundant functions in vivo, notably in mammary gland morphogenesis and lactation. (luetteke1999targetedinactivationof pages 1-2, luetteke1999targetedinactivationof pages 6-7)
In vivo pharmacologic EGFR inhibition. EGFR inhibitors with clinical use (e.g., gefitinib) are applied in mouse models to modulate EGFR-dependent tissue remodeling (e.g., the hippocampal neurogenic niche after seizures). (pastoralonso2024hbegfactivatesegfr pages 1-2)
Live biosensor imaging of ERK dynamics. ERK-biosensor mice enable quantitative measurement of EGFR-ligand-dependent ERK waves during physiological processes such as epidermal wound repair, supporting systems-level modeling of ligand diffusion/activation. (deguchi2024lowaffinityligandsof pages 1-4)
Ligand redundancy is a core principle. Multiple authoritative reviews and mouse genetics papers converge on the conclusion that loss of a single ligand such as EGF can be phenotypically mild because other EGFR ligands provide compensatory signaling; stronger phenotypes emerge under combinatorial ligand loss or receptor perturbation. (luetteke1999targetedinactivationof pages 1-2, sibilia2007theepidermalgrowth pages 2-4)
Tissue-specific processing is central to Egf biology. The classical mouse precursor studies and later review emphasize that distinct tissues (submaxillary gland vs kidney) handle the same precursor very differently—salivary gland efficiently produces mature EGF for secretion, whereas kidney exhibits membrane-associated proEGF and urinary high-MW forms, implying regulated or incomplete maturation/shedding. This has major implications for annotating Egf’s “site of action”: in many tissues it may function as a membrane-anchored ligand reservoir rather than a source of abundant soluble 6 kDa EGF. (scott1985thestructureand pages 4-7, lakshmanan1990identificationofproepidermal pages 1-3, zeng2014epidermalgrowthfactor pages 2-4)
Recency gap for Egf-specific primary work. The most definitive mechanistic and localization evidence for mouse Egf/proEGF in the retrieved texts is classic (1985–1990) with a consolidating review (2014). Recent (2023–2024) work retrieved here is largely EGFR-ligand-field focused or emphasizes other ligands (e.g., HB-EGF, EREG), and therefore should be used to contextualize Egf rather than replace Egf-specific evidence. (scott1985thestructureand pages 4-7, zeng2014epidermalgrowthfactor pages 2-4, deguchi2024lowaffinityligandsof pages 1-4, pastoralonso2024hbegfactivatesegfr pages 1-2)
Sheddase specificity is context-dependent. A 2024 preprint summarizes probe-based evidence that ADAM17 sheds many EGFR ligands but not EGF in that experimental setup; this does not exclude other proteases or contexts for proEGF processing (as illustrated by platelet ADAMDEC1-mediated cleavage in a different system). (deguchi2024lowaffinityligandsof pages 1-4, chen2017thesolubleprotease pages 1-2)
References
(scott1985thestructureand pages 1-4): J. Scott, S. Patterson, L. Rall, G. I. Bell, R. Crawford, J. Penschow, H. Niall, and J. Coghlan. The structure and biosynthesis of epidermal growth factor precursor. Journal of Cell Science, 1985:19-28, Feb 1985. URL: https://doi.org/10.1242/jcs.1985.supplement_3.3, doi:10.1242/jcs.1985.supplement_3.3. This article has 64 citations and is from a domain leading peer-reviewed journal.
(zeng2014epidermalgrowthfactor pages 2-4): Fenghua Zeng and Raymond C. Harris. Epidermal growth factor, from gene organization to bedside. Seminars in cell & developmental biology, 28:2-11, Apr 2014. URL: https://doi.org/10.1016/j.semcdb.2014.01.011, doi:10.1016/j.semcdb.2014.01.011. This article has 311 citations and is from a peer-reviewed journal.
(zeng2014epidermalgrowthfactor pages 2-2): Fenghua Zeng and Raymond C. Harris. Epidermal growth factor, from gene organization to bedside. Seminars in cell & developmental biology, 28:2-11, Apr 2014. URL: https://doi.org/10.1016/j.semcdb.2014.01.011, doi:10.1016/j.semcdb.2014.01.011. This article has 311 citations and is from a peer-reviewed journal.
(scott1985thestructureand pages 4-7): J. Scott, S. Patterson, L. Rall, G. I. Bell, R. Crawford, J. Penschow, H. Niall, and J. Coghlan. The structure and biosynthesis of epidermal growth factor precursor. Journal of Cell Science, 1985:19-28, Feb 1985. URL: https://doi.org/10.1242/jcs.1985.supplement_3.3, doi:10.1242/jcs.1985.supplement_3.3. This article has 64 citations and is from a domain leading peer-reviewed journal.
(scott1985thestructureand media d2d35de8): J. Scott, S. Patterson, L. Rall, G. I. Bell, R. Crawford, J. Penschow, H. Niall, and J. Coghlan. The structure and biosynthesis of epidermal growth factor precursor. Journal of Cell Science, 1985:19-28, Feb 1985. URL: https://doi.org/10.1242/jcs.1985.supplement_3.3, doi:10.1242/jcs.1985.supplement_3.3. This article has 64 citations and is from a domain leading peer-reviewed journal.
(chen2017thesolubleprotease pages 1-2): Rui Chen, Ge Jin, and Thomas M. McIntyre. The soluble protease adamdec1 released from activated platelets hydrolyzes platelet membrane pro-epidermal growth factor (egf) to active high-molecular-weight egf. Journal of Biological Chemistry, 292:10112-10122, Jun 2017. URL: https://doi.org/10.1074/jbc.m116.771642, doi:10.1074/jbc.m116.771642. This article has 40 citations and is from a domain leading peer-reviewed journal.
(lakshmanan1990identificationofproepidermal pages 1-3): J. Lakshmanan, E.C. Salido, R. Lam, L. Barajas, and D.A. Fisher. Identification of pro-epidermal growth factor and high molecular weight epidermal growth factors in adult mouse urine. Biochemical and biophysical research communications, 173 3:902-11, Dec 1990. URL: https://doi.org/10.1016/s0006-291x(05)80871-x, doi:10.1016/s0006-291x(05)80871-x. This article has 20 citations and is from a peer-reviewed journal.
(fisher1990metabolismandeffects pages 2-3): DELBERT A. FISHER and JAYARAMAN LAKSHMANAN. Metabolism and effects of epidermal growth factor and related growth factors in mammals. Endocrine reviews, 11 3:418-42, Aug 1990. URL: https://doi.org/10.1210/edrv-11-3-418, doi:10.1210/edrv-11-3-418. This article has 510 citations and is from a domain leading peer-reviewed journal.
(luetteke1999targetedinactivationof pages 1-2): Noreen C. Luetteke, Ting Hu Qiu, Suzanne E. Fssssenton, Kelly L. Troyer, Richard F. Riedel, Aileen Chang, and David C. Lee. Targeted inactivation of the egf and amphiregulin genes reveals distinct roles for egf receptor ligands in mouse mammary gland development. Development, 126:2739-2750, Jun 1999. URL: https://doi.org/10.1242/dev.126.12.2739, doi:10.1242/dev.126.12.2739. This article has 698 citations and is from a domain leading peer-reviewed journal.
(sibilia2007theepidermalgrowth pages 2-4): Maria Sibilia, Renate Kroismayr, Beate M. Lichtenberger, Anuradha Natarajan, Manfred Hecking, and Martin Holcmann. The epidermal growth factor receptor: from development to tumorigenesis. Differentiation; research in biological diversity, 75 9:770-87, Nov 2007. URL: https://doi.org/10.1111/j.1432-0436.2007.00238.x, doi:10.1111/j.1432-0436.2007.00238.x. This article has 468 citations.
(luetteke1999targetedinactivationof pages 2-3): Noreen C. Luetteke, Ting Hu Qiu, Suzanne E. Fssssenton, Kelly L. Troyer, Richard F. Riedel, Aileen Chang, and David C. Lee. Targeted inactivation of the egf and amphiregulin genes reveals distinct roles for egf receptor ligands in mouse mammary gland development. Development, 126:2739-2750, Jun 1999. URL: https://doi.org/10.1242/dev.126.12.2739, doi:10.1242/dev.126.12.2739. This article has 698 citations and is from a domain leading peer-reviewed journal.
(luetteke1999targetedinactivationof pages 6-7): Noreen C. Luetteke, Ting Hu Qiu, Suzanne E. Fssssenton, Kelly L. Troyer, Richard F. Riedel, Aileen Chang, and David C. Lee. Targeted inactivation of the egf and amphiregulin genes reveals distinct roles for egf receptor ligands in mouse mammary gland development. Development, 126:2739-2750, Jun 1999. URL: https://doi.org/10.1242/dev.126.12.2739, doi:10.1242/dev.126.12.2739. This article has 698 citations and is from a domain leading peer-reviewed journal.
(chan2000expressionofepidermal pages 1-2): Siu-Yuen Chan and Richard Wing-Chuen Wong. Expression of epidermal growth factor in transgenic mice causes growth retardation*. The Journal of Biological Chemistry, 275:38693-38698, Dec 2000. URL: https://doi.org/10.1074/jbc.m004189200, doi:10.1074/jbc.m004189200. This article has 108 citations.
(deguchi2024lowaffinityligandsof pages 1-4): Eriko Deguchi, Shuhao Lin, Daiki Hirayama, Kimiya Matsuda, Akira Tanave, Kenta Sumiyama, Shinya Tsukiji, Tetsuhisa Otani, Mikio Furuse, Alexander Sorkin, Michiyuki Matsuda, and Kenta Terai. Low-affinity ligands of the epidermal growth factor receptor are long-range signal transmitters during collective cell migration of epithelial cells. bioRxiv, Sep 2024. URL: https://doi.org/10.1101/2024.09.25.614853, doi:10.1101/2024.09.25.614853. This article has 1 citations.
(pastoralonso2024hbegfactivatesegfr pages 1-2): Oier Pastor-Alonso, Irene Durá, Sara Bernardo-Castro, Emilio Varea, Teresa Muro-García, Soraya Martín-Suárez, Juan Manuel Encinas-Pérez, and Jose Ramon Pineda. Hb-egf activates egfr to induce reactive neural stem cells in the mouse hippocampus after seizures. Life Science Alliance, 7:e202201840, Jul 2024. URL: https://doi.org/10.26508/lsa.202201840, doi:10.26508/lsa.202201840. This article has 9 citations and is from a peer-reviewed journal.
(li2024egfstat1maintainedecm1expression pages 1-5): Yujia Li, F. Link, Weiguo Fan, R. Feng, W. Piorońska, Z. Nwosu, K. Gould, C. Meyer, Seddik Hammad, H. Weng, Matthias P. Ebert, Steven Dooley, and Sai Wang. Egf/stat1-maintained ecm1 expression in hepatic homeostasis is disrupted by ifnγ/nrf2 in chronic liver diseases. 40. Jahrestagung der Deutschen Arbeitsgemeinschaft zum Studium der Leber, Jan 2024. URL: https://doi.org/10.1055/s-0043-1777485, doi:10.1055/s-0043-1777485. This article has 0 citations.