LIN28 (LIN28A / LIN28B)

LIN28 is an RNA-binding protein that functions as the master post-transcriptional repressor of the let-7 microRNA family. In development it is a heterochronic timing factor, first characterized in Caenorhabditis elegans and broadly conserved; in embryonic and pluripotent cells it is highly expressed and actively suppressed upon differentiation. Its two human paralogs — LIN28A and LIN28B — share the same biochemical mechanism but differ in subcellular localization and expression pattern. In aging biology, LIN28 is relevant on at least three axes: (1) it is a required component of reprogramming cocktails that overcome the senescence barrier to iPSC generation (the Lapasset 2011 OSKMNL cocktail); (2) LIN28A reactivation in adult murine tissues enhances regenerative capacity in some tissues (hair follicle, pinnal, neonatal digit) via let-7 suppression and direct enhancement of bioenergetic metabolism (both glycolysis and OxPhos), though not all adult tissues respond; and (3) the LIN28/let-7/IGF pathway is a conserved regulator of glucose metabolism and insulin sensitivity, placing LIN28 at the intersection of nutrient sensing and stem-cell aging.

Identity: two paralogs

Field	LIN28A	LIN28B
UniProt	Q9H9Z2 (LN28A_HUMAN) — Swiss-Prot reviewed	Q6ZN17 (LN28B_HUMAN) — Swiss-Prot reviewed
NCBI Gene	79727	389421
HGNC	HGNC:15986 (symbol LIN28A)	HGNC:32207 (symbol LIN28B)
Ensembl	ENSG00000131914	ENSG00000187772
Chromosomal locus	1p36.11	6q16.3–q21
Protein length	209 amino acids	250 amino acids
Gene aliases	CSDD1, LIN28, ZCCHC1, LIN-28	CSDD2
Mouse ortholog	Lin28a (NCBI Gene 83557; designated Tex17/Gm10299 in early records)	Lin28b

Canonical page: This page uses LIN28A as primary (UniProt Q9H9Z2; most commonly referenced in reprogramming and regeneration literature). LIN28B-specific biology is noted in the body where the paralogs diverge. Both paralogs are listed in aliases: so [[lin28]] links resolve for either symbol.

Disambiguation: No pathways/lin28.md exists; pathway-level coverage is under [[oct4-sox2-nanog]] (planned stub) and [[insulin-igf1]]. This protein page is the canonical [[lin28]], [[lin28a]], and [[lin28b]] resolution.

Domain structure

Both LIN28A and LIN28B contain the same two-module RNA-binding architecture ¹:

Cold-shock domain (CSD): An ~70-residue beta-barrel fold, originally identified in bacterial cold-shock proteins but used here for sequence-specific RNA recognition. In LIN28, the CSD contacts the GGAG tetra-nucleotide motif in the terminal loop of pre-let-7 substrates.
Two CCHC-type zinc fingers (ZF1, ZF2, Cys–Cys–His–Cys coordination): Bind single-stranded RNA. Zinc fingers contact the conserved 3’-GGAG motif of pre-let-7 and are required for recruiting TUT4/TUT7 to the complex.

Together the CSD and CCHC zinc fingers constitute a bipartite RNA-binding unit. The CSD contacts the apical loop of pre-let-7; the zinc fingers stabilize the interaction at the 3’ side ². This bipartite engagement is sufficient for LIN28 to block Dicer-mediated processing and to present the pre-let-7 3’ end to TUT4/TUT7 for oligouridylation.

Paralog difference in localization: LIN28A is predominantly cytoplasmic (P bodies); LIN28B is predominantly nucleolar. This difference means LIN28A acts mainly post-transcriptionally on pre-let-7 exported to the cytoplasm, whereas LIN28B can additionally suppress primary let-7 transcripts in the nucleus — an earlier step in the biogenesis pathway. gap/needs-replication for the full functional consequences of this distinction in human contexts.

Developmental function: heterochronic timing gene

LIN28 was first identified in C. elegans as a heterochronic gene — mutations cause developmental events to execute at incorrect larval stages ³. In Moss et al. 1997, lin-28 was shown to encode a cytoplasmic cold-shock-domain protein regulated by the lin-4 small RNA; it controls the transition from L2-to-L3 larval fate ¹.

In mammals, LIN28 expression is high in embryonic and fetal tissues and declines sharply with differentiation and postnatal development. Key tissues where LIN28 is expressed in early development include:

Embryonic stem cells and iPSCs
Primordial germ cells
Fetal liver, fetal brain, placenta
Undifferentiated spermatogonia (LIN28A) and elongating spermatids / Leydig cells (LIN28B) ⁴

In adult somatic tissue, both paralogs are silenced under physiological conditions. Re-expression in adult tissues is strongly associated with either active regenerative programs or malignant transformation.

Mechanism: the LIN28/let-7 bistable switch

Post-transcriptional repression of let-7 biogenesis

LIN28 acts as a master suppressor of the entire let-7 microRNA family. The mechanistic cascade is ²⁵⁶:

LIN28 binds pre-let-7 in the cytoplasm via its CSD and CCHC zinc fingers, recognizing the GGAG motif in the terminal loop.
LIN28 recruits TUT4 (ZCCHC11) and/or TUT7 (ZCCHC6) — non-canonical poly(A) polymerases that add an oligouridine tail to the 3’ end of pre-let-7.
Oligouridylated pre-let-7 is refractory to Dicer processing and is directed to degradation.
Result: the mature let-7 family is not produced, allowing LIN28 target mRNAs (including HMGA2, IGF2BP1/2/3, IMP1/2/3, and members of the insulin-PI3K-mTOR signaling cascade) to be translated.

Bistable switch architecture

The LIN28/let-7 axis forms a double-negative feedback loop:

LIN28 represses let-7 biogenesis
let-7 targets the LIN28 mRNA for translational repression

This mutual inhibition creates a bistable switch with two stable states: a pluripotent/fetal/stem-cell state (LIN28 high, let-7 low) and a differentiated/somatic state (LIN28 low/absent, let-7 high). The transition between states is digital rather than graded, making LIN28 a binary switch for the fetal-to-adult developmental transition ⁷. gap/unsourced for quantitative bistability modeling; the bistable-switch framing is well-established in the literature but the parameters of the switch in human cells are not confirmed from a primary source on this page.

let-7 target landscape

When LIN28 suppresses let-7, the consequent de-repressed mRNAs include:

HMGA2 — high-mobility group chromatin protein; fetal growth; oncogenic when re-expressed in adult tissue
IGF2BP1/2/3 (IMP1/2/3) — RNA-binding proteins that stabilize oncofetal transcripts; targets of let-7
IGF1R, INSR, IRS2 — insulin-PI3K pathway components; let-7 suppresses insulin sensitivity when LIN28 is absent ⁸
c-MYC — partial regulation via let-7 family members

Role in reprogramming

Thomson 5-factor iPSC cocktail (human)

Yu et al. 2007 (Science) demonstrated that OCT4 + SOX2 + NANOG + LIN28 (± KLF4) delivered by lentiviral vectors to human somatic cells generates iPSCs — the first human iPSC paper alongside Takahashi & Yamanaka 2007 ⁹. This cocktail is important because it lacks c-MYC, reducing the oncogenic risk inherent to the original OSKM protocol. LIN28 is proposed to substitute for c-MYC, in part by suppressing let-7 targets that restrict proliferation and self-renewal; the exact mechanism of LIN28’s contribution to human cell reprogramming efficiency is not fully characterized. gap/no-mechanism

Lapasset 2011: overcoming the senescence barrier (OSKMNL)

Standard four-factor OSKM (OCT4 + SOX2 + KLF4 + c-MYC) does not efficiently reprogram senescent cells. Lapasset et al. 2011 (Genes & Development) showed that a six-factor cocktail — OSKMNL (OCT4 + SOX2 + KLF4 + c-MYC + NANOG + LIN28) — successfully generated iPSCs from replicatively senescent human fibroblasts (74-year-old donor, senescent after 51 population doublings) and centenarian cells (92–, 94–, 96–, and 101-year-old donors) with reprogramming efficiency ~0.06% ¹⁰. The OSNL combination (OCT4 + SOX2 + NANOG + LIN28, i.e., without KLF4 and c-MYC — the Thomson cocktail) was also tested on senescent cells and failed to produce iPSC colonies after 40 d; standard OSKM was also insufficient ¹⁰. The full six-factor combination is specifically required. The resulting iPSCs:

Expressed endogenous pluripotency genes (OCT4, SOX2, NANOG, REX1)
Reset telomere length to levels comparable with hESCs
Restored youthful mitochondrial function and global gene expression profiles
Retained full directed-differentiation capacity into all three germ layers

The specific contribution of LIN28 versus NANOG in enabling OSKMNL to overcome the senescence barrier is not dissected in Lapasset 2011 — it is not established whether LIN28 alone, NANOG alone, or both together are individually required. This is an unresolved question. gap/no-mechanism

Partial reprogramming context

Standard partial reprogramming protocols (OSK or cyclic OSKM) do NOT include LIN28. LIN28 is a full-reprogramming factor relevant to overcoming the senescence barrier in aged cells, not a standard component of partial epigenetic reset strategies. See partial-reprogramming for the comparative evidence.

Aging relevance

LIN28A reactivation and tissue regeneration

Shyh-Chang et al. 2013 (Cell) — the central study of LIN28 in adult tissue repair — used doxycycline-inducible Lin28a transgenic mice to show that restoring Lin28a expression in adult tissues dramatically enhances regenerative capacity ¹¹:

Hair follicle regeneration: Adult Lin28a-expressing mice exhibited significantly faster hair regrowth after shaving compared to controls; the effect operates by promoting anagen in hair follicles during telogen.
Neonatal digit/cartilage/bone repair: Lin28a-expressing neonatal mice showed significantly enhanced regrowth of amputated digit tips (soft tissue and bone). Adult digit repair (5-week-old hindlimb) showed no significant enhancement (Figure S2, referenced in text: “some adult tissues such as adult digits and the adult heart do not show improved tissue repair”) — the digit-repair benefit is age-dependent and context-dependent.
Pinnal (ear) tissue repair: Transgenic mice showed faster closure of 2 mm ear-punch wounds, with increased connective tissue and Ki67 staining; local dox-inducible LIN28B induction in the ear was insufficient to promote pinnal repair (suggesting a Lin28a-specific mechanism).
Mechanism: Lin28a’s pro-regenerative effect required both glycolysis and oxidative phosphorylation (OxPhos); inhibiting OxPhos with antimycin-A (complex III inhibitor) abolished the regenerative enhancement in vivo (Figure 7B). Glycolysis inhibition with 3BP or 2DG similarly abolished the effect. The mechanism has two components: (1) let-7 suppression, which is necessary but insufficient to phenocopy Lin28a overexpression; (2) direct Lin28a binding to metabolic enzyme mRNAs (Pfkp, Pdha1, Idh3b, Sdha, Ndufb3, Ndufb8), let-7-independent, which enhances both glycolysis and OxPhos flux. The authors conclude that Lin28a reprograms cellular bioenergetics toward an embryonic metabolic state to promote repair.

Dimension	Status
Pathway conserved in humans?	yes — LIN28A/B expression, let-7 suppression, and bioenergetic reprogramming are all present in human cells
Regenerative phenotype conserved in humans?	unknown — no equivalent human tissue-regeneration experiment exists
Replicated in humans?	no — all regeneration evidence is murine ¹¹

gap/needs-human-replication — neonatal digit-regrowth, hair follicle, and pinnal tissue repair experiments are mouse-only; adult digit repair was NOT significantly enhanced even in the mouse model.

LIN28/let-7 axis in glucose metabolism and insulin sensitivity

Zhu et al. 2011 (Cell) demonstrated that Lin28a/LIN28B overexpression in transgenic mice promotes insulin-sensitized glucose metabolism resistant to high-fat-diet-induced diabetes ⁸. The mechanism: let-7 suppresses IGF1R, INSR, and IRS2 — core components of the insulin-PI3K-mTOR signaling axis. When LIN28 is present and let-7 is low, these mRNAs are translated at higher levels, increasing insulin sensitivity. Conversely, loss of Lin28a impairs glucose homeostasis. This places LIN28/let-7 as a regulator of deregulated-nutrient-sensing, with let-7 acting as an endogenous suppressor of insulin-pathway responsiveness.

Human relevance: let-7 target genes are enriched for SNPs associated with type 2 diabetes and fasting glucose control in GWAS ⁸. gap/needs-replication — the human genetic evidence is indirect (SNP enrichment, not LIN28 loss-of-function association).

Dimension	Status
Insulin-pathway regulation by let-7 conserved in humans?	yes — let-7 targets IGF1R/INSR in human cells
Metabolic phenotype conserved in humans?	partial — GWAS enrichment supports let-7 target relevance; LIN28 direct evidence absent
Replicated in humans?	no — no human LIN28 gain/loss-of-function metabolic studies

Developmental timing, puberty, and longevity associations

Zhu et al. 2010 (Nature Genetics) showed that Lin28a transgenic mice have increased body size and delayed puberty onset, phenocopying human genetic associations of LIN28B locus variants with age at menarche, height, and puberty timing identified in GWAS ¹². This connects the LIN28/let-7 axis to the developmental timing programs that influence both reproductive span and, potentially, healthy longevity — though the causal path from LIN28/let-7 to aging endpoints in humans is not established. gap/needs-human-replication

Decline in adult tissue and stem-cell exhaustion

In adult somatic tissue, LIN28 expression is essentially absent. The developmental silencing of LIN28 (and corresponding rise in let-7) contributes to the functional limitation of adult stem-cell populations:

Let-7 suppresses HMGA2 and IGF2BP oncofetal programs in adult stem cells, reducing their proliferative and regenerative potential
This represents one molecular mechanism underlying stem-cell-exhaustion: the switch from fetal to adult state is associated with the LIN28-off / let-7-high epigenetic state that is less regeneratively permissive

The specific contribution of LIN28 silencing to aging-associated decline in tissue regeneration — versus other mechanisms of stem-cell exhaustion — is not established. gap/no-mechanism

Oncogenic risk of LIN28 reactivation

LIN28 is re-expressed in many aggressive human cancers: Wilms tumor, hepatocellular carcinoma, germ cell tumors, medulloblastoma (LIN28B), and various other solid tumors ¹³. The mechanism mirrors the regeneration biology: LIN28 suppresses let-7-mediated tumor suppression, de-repressing oncofetal programs (HMGA2, Myc pathway, IGF pathway). LIN28B expression decreases with age in developing human cerebellum and is re-expressed in aggressive medulloblastoma subtypes ¹³.

This oncogenic risk is the central translational tension for any therapeutic LIN28 reactivation strategy — directly analogous to the c-MYC risk in OSKM reprogramming. Any regenerative medicine application of LIN28 must contend with its pro-tumorigenic potential.

No approved human therapy uses LIN28 as a direct therapeutic target. All evidence for regenerative benefit is preclinical (mouse). gap/long-term-unknown

Key interactors

Interactor	Nature of interaction	Functional relevance
TUT4 (ZCCHC11)	Directly recruited by LIN28 CCHC zinc fingers	Adds oligouridine tail to pre-let-7; required for LIN28-mediated let-7 suppression ²
TUT7 (ZCCHC6)	Alternative TUTase recruited by LIN28	Partially redundant with TUT4; also oligouridylates pre-let-7 ⁶
oct4	Co-expressed in iPSC reprogramming cocktails	LIN28 is the “L” in the Thomson SONL / Thomson-Lapasset OSKMNL cocktails
sox2	Co-expressed in iPSC cocktails	Core pluripotency network partner
nanog	Co-expressed in OSKMNL cocktail	Co-required to overcome senescence barrier in aged cells
klf4	Co-expressed in OSKMNL cocktail	Part of the six-factor reprogramming combination
c-myc	Co-expressed in OSKMNL cocktail; let-7 partially regulates c-Myc	LIN28 and c-Myc are co-present in full reprogramming but diverge in therapeutic strategy
HMGA2	let-7 target; de-repressed when LIN28 is high	Oncofetal chromatin regulator; fetal stem-cell proliferation; tumor marker
IGF1R / INSR	let-7 targets; de-repressed when LIN28 is high	Insulin-IGF receptor signaling; metabolic regulation ⁸

Pathway membership

insulin-igf1 — LIN28/let-7 modulates IGF1R and INSR expression; metabolic arm
oct4-sox2-nanog — LIN28 is a co-factor in human iPSC cocktails; not a core pluripotency TF but functionally embedded in this network (planned stub)

Note: LIN28 does not have a canonical role in standard aging-pathway signaling (mTOR, AMPK, sirtuin) under physiological conditions in adult somatic tissue. Its aging relevance operates entirely through developmental de-silencing or therapeutic reactivation.

Limitations and gaps

gap/needs-human-replication — All direct experimental evidence for LIN28’s pro-regenerative effects (digit repair, wound healing, hair regrowth) is from transgenic mouse models; no equivalent human gain-of-function tissue-repair data exist.

gap/no-mechanism — The specific functional contribution of LIN28 versus NANOG in allowing OSKMNL to reprogram senescent cells is not dissected (Lapasset 2011 added both factors together; individual necessity untested).

gap/no-mechanism — The specificity determinants that allow LIN28A reactivation to enhance tissue repair without triggering tumorigenesis in adult mice are not characterized; the threshold between regenerative and oncogenic LIN28 expression levels is unknown.

gap/long-term-unknown — Long-term safety of LIN28 reactivation in adult somatic tissues (tumor risk, effects on immune surveillance, germline implications) is not established in any human model.

gap/needs-replication — The bioenergetic-reprogramming mechanism proposed by Shyh-Chang 2013 (Lin28a → let-7 suppression + direct metabolic enzyme mRNA binding → enhanced glycolysis and OxPhos → tissue repair) is from a single-lab mouse study; independent mechanistic replication in a separate laboratory is needed.

gap/needs-human-replication — The glucose-metabolism/insulin-sensitization phenotype (Zhu 2011) is mouse-derived; human LIN28B GWAS SNP enrichment in type-2-diabetes loci is indirect support but not causal.

gap/needs-canonical-id — GenAge entry for LIN28A/B not confirmed via REST API (database query returned null; may not have a curated entry; verify directly at genomics.senescence.info/genes).

Cross-references

Entity	Relationship
partial-reprogramming	LIN28 is a required component of the OSKMNL senescent-cell reprogramming cocktail (Lapasset 2011); not used in standard OSK partial reprogramming
oct4	Co-reprogramming factor; see Thomson 5-factor and Lapasset 6-factor cocktails
sox2	Core pluripotency partner
nanog	Co-required with LIN28 in OSKMNL; see nanog for the detailed OSKMNL mechanism
klf4	Co-expressed in OSKMNL cocktail
c-myc	Both LIN28 and c-MYC are omitted from safer OSK protocols; c-MYC is the canonical oncogenic risk; LIN28 is the let-7-suppressing risk
induced-pluripotent-stem-cells	LIN28 is part of the Thomson and Lapasset reprogramming cocktails for human iPSC derivation
epigenetic-alterations	LIN28/OSKMNL resets the epigenetic aging program in senescent cells in vitro
stem-cell-exhaustion	LIN28 silencing contributes to adult stem cell’s reduced regenerative state
deregulated-nutrient-sensing	LIN28/let-7 regulates IGF1R, INSR expression; insulin sensitivity link
insulin-igf1	LIN28 modulates the strength of insulin-IGF signaling via let-7 repression
mus-musculus	All in vivo regeneration and metabolism experiments were conducted in mouse
caenorhabditis-elegans	Founding organism for heterochronic lin-28 characterization (Ambros, Moss, Ruvkun lineage)

Footnotes

doi:10.1016/s0092-8674(00)81906-6 · Moss EG, Lee RC, Ambros V · Cell 1997 · in-vivo (C. elegans genetics) · Original characterization of lin-28 as a cold-shock-domain protein that controls developmental timing and is regulated by lin-4 RNA; first description of CSD + CCHC zinc finger architecture · model: C. elegans ↩ ↩²
doi:10.1016/j.cell.2009.08.002 · Heo I, Joo C, Kim YK, Ha M, Yoon MJ, Cho J, Yeom KH, Han J, Kim VN · Cell 2009 · in-vitro (biochemical + cell-line) · TUT4 adds oligouridine tails to pre-let-7 upon LIN28 recruitment; LIN28 GGAG-loop recognition required; oligouridylated pre-let-7 is Dicer-refractory · model: human HEK293 + murine embryonic cells ↩ ↩² ↩³
doi:10.1126/science.6494891 · Ambros V, Horvitz HR · Science 1984 · in-vivo (C. elegans) · Founding characterization of heterochronic mutants including lin-28; establishes the heterochronic gene class · model: C. elegans ↩
doi:10.3390/ijms23137245 · Krsnik D, Marić T, Bulić-Jakuš F, Sinčić N, Bojanac AK · International Journal of Molecular Sciences 2022 · review · LIN28A/B expression in testicular cell types across lifespan; LIN28A in undifferentiated spermatogonia; LIN28B in elongating spermatids and Leydig cells; aging-related expression changes; association with testicular cancer · recency-search result (2022) ↩
doi:10.1038/nsmb.1676 · Hagan JP, Piskounova E, Gregory RI · Nature Structural & Molecular Biology 2009 · in-vitro + cell-line · Lin28 directly recruits TUTase Zcchc11 (TUT4) to inhibit let-7 maturation; first demonstration of the LIN28-TUTase complex in mouse ESCs · model: mouse ESCs ↩
doi:10.1261/rna.034538.112 · Thornton JE, Chang HM, Piskounova E, Gregory RI · RNA 2012 · in-vitro + cell-line · LIN28-mediated let-7 suppression is carried out by alternative TUTases TUT4 and TUT7 (Zcchc11 and Zcchc6); both are recruited; partially redundant · model: human and mouse cell lines ↩ ↩²
doi:10.1089/cell.2017.0015 · Farzaneh M, Attari F, Khoshnam SE · Cellular Reprogramming 2017 · review · LIN28/let-7 double-negative feedback loop as bistable switch during pluripotency, reprogramming, and tumorigenicity; gap/unsourced for quantitative switch parameters in human cells ↩
doi:10.1016/j.cell.2011.08.033 · Zhu H, Shyh-Chang N, Segrè AV et al. (Daley GQ lab) · Cell 2011 · in-vivo (transgenic) + GWAS enrichment analysis · model: Mus musculus + human GWAS data · Lin28a/LIN28B overexpression promotes insulin sensitivity and resists HFD-induced diabetes; let-7 suppresses IGF1R, INSR, IRS2; let-7 targets enriched for T2D + fasting-glucose GWAS SNPs ↩ ↩² ↩³ ↩⁴
doi:10.1126/science.1151526 · Yu J, Vodyanik MA, Smuga-Otto K, Antosiewicz-Bourget J, Frane JL, Tian S, Nie J, Jonsdottir GA, Ruotti V, Stewart R, Slukvin II, Thomson JA · Science 2007 · in-vitro (lentiviral transduction) · model: human foreskin fibroblasts · OCT4 + SOX2 + NANOG + LIN28 (±KLF4) generates human iPSCs; c-MYC-free; LIN28 is the “L” in the Thomson cocktail ↩
doi:10.1101/gad.173922.111 · Lapasset L, Milhavet O, Prieur A, Besnard E, Babled A, Aït-Hamou N, Leschik J, Pellestor F, Ramirez JM, De Vos J, Lehmann S, Lemaitre JM · Genes & Development 2011 · in-vitro · model: human fibroblasts (74-year-old senescent donor; 92–, 94–, 96–, and 101-year-old centenarian donors) · 6-factor OSKMNL required to reprogram senescent/centenarian cells; OSNL (without KLF4 and c-MYC) and standard OSKM both insufficient; efficiency ~0.06%; iPSCs reset telomere length, gene expression, mitochondrial function; aging markers erased ↩ ↩²
doi:10.1016/j.cell.2013.09.059 · Shyh-Chang N, Zhu H, de Soysa TY, Shinoda G, Seligson MT, Tsanov KM, Nguyen L, Asara JM, Cantley LC, Daley GQ · Cell 2013 · in-vivo (dox-inducible Lin28a transgenic) · model: Mus musculus · Lin28a reactivation enhances hair follicle regrowth (adult), neonatal digit-tip repair, and pinnal tissue repair; adult digit repair was not significantly enhanced; requires both glycolysis and OxPhos (abolished by antimycin-A or 3BP/2DG in vivo); mechanism is partly let-7-independent (direct binding of metabolic enzyme mRNAs: Pfkp, Pdha1, Idh3b, Sdha, Ndufb3, Ndufb8); pharmacological glycolysis inhibition in WT ears enhanced pinnal repair, suggesting bioenergetic state is rate-limiting · single-lab; gap/needs-replication ↩ ↩²
doi:10.1038/ng.593 · Zhu H, Shah S, Shyh-Chang N et al. (Daley GQ lab) · Nature Genetics 2010 · in-vivo (transgenic) · model: Mus musculus + human GWAS · Lin28a transgenic mice show increased body size + delayed puberty; LIN28B locus variants associate with height and age-at-menarche in humans ↩
doi:10.1002/jcp.30946 · Maklad A, Sedeeq M, Wilson R, Heath JA, Gueven N, Azimi I · Journal of Cellular Physiology 2023 · in-vitro + observational (tumor tissue) · LIN28B elevated in aggressive medulloblastoma; LIN28B expression decreases with age in normal cerebellum; pharmacological LIN28 inhibition reduces tumor cell growth and stemness (CD133 suppression) · recency-search result (2023) ↩ ↩²

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