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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
Target confirmed. The UniProt accession Q9PUR2 corresponds to zebrafish (Danio rerio) cryaba, which encodes an αB‑crystallin–type small heat shock protein (sHSP) (often termed αBa‑crystallin in zebrafish to distinguish it from the second paralog, αBb/cryabb). Zebrafish have two cryab paralogs (cryaba and cryabb) that arose from the teleost genome duplication. This paralog relationship (cryaba vs cryabb) is repeatedly emphasized in zebrafish lens/cataract literature and in zebrafish proteostasis studies. (rossen2025zebrafishasa pages 3-4, posner2021effectsofαcrystallin pages 1-3, park2023interplaybetweennrf2 pages 1-2)
Paralog/orthology context. A zebrafish crystallin review reports cryaba encodes a ~168 aa protein with ~61% homology to human CRYAB/HSPB5, while cryabb is ~180 aa (~58% homology). The same review summarizes that cryaba has lower baseline chaperone activity than cryabb, consistent with functional divergence after duplication. (rossen2025zebrafishasa pages 3-4)
Experimental confirmation of gene product. In a zebrafish CRISPR study generating null alleles for the three α‑crystallin genes (cryaa, cryaba, cryabb), adult lens proteomics (parallel reaction monitoring) detected an αBa‑crystallin peptide in wild type lenses that was absent in cryaba−/− lenses, confirming that zebrafish cryaba encodes an αB‑like crystallin protein in vivo. (posner2021effectsofαcrystallin pages 15-18)
sHSPs are ATP‑independent molecular chaperones that primarily act as “holdases”: they bind partially unfolded or destabilized proteins to inhibit aggregation, maintaining proteostasis under basal conditions and especially during stress. In vertebrates, α‑crystallins (αA and αB) are members of this sHSP class, and in zebrafish the αB class is represented by cryaba (αBa) and cryabb (αBb). (posner2021effectsofαcrystallin pages 1-3, zou2015aconservedrole pages 1-2, rossen2025zebrafishasa pages 3-4)
A zebrafish crystallin review summarizes αB‑crystallin proteins as having a conserved crystallin domain and variable N‑ and C‑terminal regions; they form large, dynamic oligomers, and phosphorylation can remodel oligomer size and client binding kinetics. This provides the conceptual basis for why zebrafish αB paralogs may have low basal activity yet become more functional under stress and/or after post‑translational regulation. (rossen2025zebrafishasa pages 2-3, rossen2025zebrafishasa pages 3-4)
Zebrafish lens work directly frames α‑crystallins as chaperones that bind thermodynamically destabilized proteins and inhibit aggregation. In vivo, morpholino knockdown of cryaba (αBa) leads to lens abnormalities and opacity phenotypes that can be partially rescued by expressing an exogenous αA‑crystallin, supporting that the phenotype relates to loss of α‑crystallin chaperone capacity rather than an unrelated function. (zou2015aconservedrole pages 1-2, zou2015aconservedrole pages 4-6)
A zebrafish crystallin review reports cryaba (αBa) exhibits lower chaperone activity than cryabb (αBb). This implies that, for annotation purposes, cryaba is still a bona fide sHSP chaperone, but its activity is likely more conditional (stress‑induced or modification‑dependent) compared with its paralog. (rossen2025zebrafishasa pages 3-4)
A 2025 zebrafish crystallin review synthesizes evidence that αB‑crystallins participate in regulation of lysosomal activities needed for organelle degradation during lens fiber differentiation, describing that in hsf4−/− zebrafish lenses, cryaba expression decreases and lysosomal pH increases. The review further summarizes mechanistic data (zebrafish plus complementary mammalian experiments) in which αB‑crystallin binds and stabilizes an ATP6V1A–mTORC1 complex, preventing degradation and maintaining lysosomal acidity and signaling. This connects cryaba function to lysosome‑linked proteostasis, not solely cytosolic holdase activity. (rossen2025zebrafishasa pages 4-5)
Expression statements vary by developmental stage and assay, but several consistent themes emerge:
Park et al. (2023, Frontiers in Molecular Biosciences; publication date July 2023, URL https://doi.org/10.3389/fmolb.2023.1185704) provide figure‑level evidence showing relative mRNA levels of cryaba and cryabb in tissues including lens and heart, plus representative images and quantitative penetrance plots for lens defects and heart edema phenotypes in relevant genotypes. (park2023interplaybetweennrf2 media 77804744, park2023interplaybetweennrf2 media f49f3e8a, park2023interplaybetweennrf2 media adcb316d)
Direct zebrafish cryaba subcellular localization evidence is limited in the retrieved excerpts. The strongest mechanistic localization implication is association with lysosome‑proximal mTORC1/V‑ATPase machinery in lens proteostasis as summarized in the zebrafish crystallin review. (rossen2025zebrafishasa pages 4-5)
Zebrafish cryaba phenotypes depend strongly on genetic method and background:
Interpretation: for functional annotation, the direction of effect (cryaba contributes to lens proteostasis/transparency) is well supported, but penetrance estimates are not stable across methodologies (morpholino vs stable knockout) and likely depend on strain/background and stress context. (posner2021effectsofαcrystallin pages 10-12, rossen2025zebrafishasa pages 4-5)
Park et al. (2023) report that cryaba loss‑of‑function contributes to stress‑induced heart edema, and that compromised nrf2 function increases penetrance of the cardiac phenotype (including in cryaba−/−; nrf2 double mutants). While the excerpt does not provide explicit numeric penetrance values, the paper includes phenotype images and quantitative heart measurements in figures. (park2023interplaybetweennrf2 pages 10-11, park2023interplaybetweennrf2 media adcb316d)
A key recent zebrafish‑focused development is the explicit mapping of oxidative stress response (Nrf2) to αB‑crystallin biology. Park et al. used zebrafish lines with compromised nrf2 and/or αB paralogs and found tissue‑specific and phenotype‑level interactions affecting lens and heart. In the lens, combined loss of nrf2 and cryaba was associated with altered expression programs including upregulation of cholesterol biosynthesis, with pharmacological cholesterol lowering (atorvastatin/lovastatin) modulating lens defect penetrance. (park2023interplaybetweennrf2 pages 1-2, park2023interplaybetweennrf2 pages 9-10)
A zebrafish crystallin review summarizes that in hsf4−/− zebrafish lenses, cryaba expression decreases and lysosomal pH is increased, consistent with cryaba acting downstream of lens stress/proteostasis regulation to maintain lysosomal function required for organelle degradation in differentiating fibers. (rossen2025zebrafishasa pages 4-5)
Zebrafish cryaba is used as part of genetic frameworks to model lens proteostasis failure, congenital cataract mechanisms, and modifier pathways (e.g., sterol metabolism and oxidative stress response). A zebrafish crystallin review positions cryaba/cryabb as central to these modeling efforts and highlights the utility of zebrafish for real‑time visualization and genetic manipulation. (rossen2025zebrafishasa pages 4-5)
The zebrafish crystallin review describes that expressing a pathogenic human‑like R120G CRYAB variant in zebrafish can produce mild lens defects that worsen in cryaba/cryabb null backgrounds, supporting zebrafish as a platform for interpreting disease alleles and genetic buffering in vivo. (rossen2025zebrafishasa pages 4-5)
Across zebrafish experimental work and synthesis reviews, cryaba is consistently described as an sHSP chaperone contributing to proteostasis, rather than a refractive “structural” β/γ‑crystallin. It is implicated in lens clarity, and (under stress/genetic sensitization) heart homeostasis. (zou2015aconservedrole pages 1-2, park2023interplaybetweennrf2 pages 9-10, rossen2025zebrafishasa pages 4-5)
The CRISPR null study argues that minimal early phenotypes in some settings may reflect low cryaba/cryabb expression in early lens epithelial/fiber cells, and that background or experimental context influences penetrance. The duplication (cryaba/cryabb) and potential pathway compensation further complicate interpreting single‑gene loss. (posner2021effectsofαcrystallin pages 10-12, posner2021effectsofαcrystallin pages 1-3, rossen2025zebrafishasa pages 3-4)
Zebrafish‑specific (2023): Park et al. (July 2023) explicitly connect Nrf2‑mediated oxidative stress response with αB‑crystallin paralogs in lens and heart, identifying cholesterol biosynthesis and extracellular/cardiomyopathy‑linked gene programs as candidate mediators and providing quantitative tissue expression and phenotype figures. URL: https://doi.org/10.3389/fmolb.2023.1185704. (park2023interplaybetweennrf2 pages 1-2, park2023interplaybetweennrf2 pages 9-10, park2023interplaybetweennrf2 media 77804744, park2023interplaybetweennrf2 media adcb316d)
Zebrafish methods/implementation (2024): Peng et al. (January 2024) summarize zebrafish crystallin gene duplication (one cryaa; two cryab paralogs) and provide a lens‑genetics tool (lens‑specific Cre) relevant for future conditional interrogation of lens genes including cryaba. URL: https://doi.org/10.63500/mv_v30_123. (peng2024thegenerationand pages 2-3)
Mechanistic/structural context (non‑zebrafish; interpretive only): Recent human CRYAB work reinforces the view of αB‑crystallin as a dynamic oligomeric chaperone whose assembly features control activity; this supports conservative orthology‑based mechanistic hypotheses for zebrafish cryaba but is not direct zebrafish evidence. (rossen2025zebrafishasa pages 2-3)
Gene/protein: cryaba (UniProt Q9PUR2), αBa‑crystallin; small heat shock protein (α‑crystallin/Hsp20 family). (rossen2025zebrafishasa pages 3-4, posner2021effectsofαcrystallin pages 15-18)
Primary molecular function: ATP‑independent molecular chaperone/holdase that limits protein aggregation; contributes to lens proteostasis and transparency, and under stress interacts with broader proteostasis/oxidative pathways. (zou2015aconservedrole pages 1-2, rossen2025zebrafishasa pages 3-4, park2023interplaybetweennrf2 pages 9-10)
Likely cellular sites of action: primarily intracellular; lens‑relevant mechanism includes lysosome‑associated V‑ATPase/mTORC1 machinery affecting lysosomal acidity (as reviewed), consistent with roles in organelle degradation during fiber cell differentiation; direct zebrafish subcellular localization remains incompletely mapped. (rossen2025zebrafishasa pages 4-5)
Pathways: proteostasis network intersection with oxidative stress response (Nrf2) and lens stress regulation (Hsf4), with downstream modulation of cholesterol biosynthesis and lysosomal physiology affecting phenotype penetrance. (rossen2025zebrafishasa pages 4-5, park2023interplaybetweennrf2 pages 9-10)
Phenotypes: variable lens defect penetrance across methods; morpholino (~50% defective embryos) vs some CRISPR null lines (mild early phenotypes). Evidence also supports adult age‑related cataract in cryaba−/− (~50% by 2 years in one study summary) and stress‑dependent heart edema that is enhanced by nrf2 deficiency. (zou2015aconservedrole pages 4-6, posner2021effectsofαcrystallin pages 10-12, rossen2025zebrafishasa pages 4-5, park2023interplaybetweennrf2 pages 10-11)
| Category | Zebrafish-specific findings (include quantitative numbers when available) | Key source(s) with year and URL | Notes/limitations |
|---|---|---|---|
| Identity/Family | UniProt Q9PUR2 corresponds to zebrafish cryaba, one of two teleost αB-crystallin paralogs (cryaba/cryabb) generated by genome duplication. cryaba encodes an ~168 aa small heat shock protein with ~61% homology to human CRYAB; zebrafish αB-crystallins retain canonical α-crystallin/sHSP architecture and chaperone function. CRISPR null lines plus adult lens mass spectrometry detected αBa peptide(s) in wild type and loss in cryaba−/−, confirming gene-protein identity. | Rossen et al., 2025, Front Cell Dev Biol, https://doi.org/10.3389/fcell.2025.1552988; Posner et al., 2021, bioRxiv, https://doi.org/10.1101/2021.12.22.473921; Elicker & Hutson, 2007, Gene, https://doi.org/10.1016/j.gene.2007.08.003 | Strong identity evidence, but some details come from review synthesis and preprint support; domain architecture is inferred at family level rather than from a zebrafish cryaba-specific structure (rossen2025zebrafishasa pages 3-4, posner2021effectsofαcrystallin pages 15-18, posner2021effectsofαcrystallin pages 1-3, rossen2025zebrafishasa pages 2-3, elicker2007genomewideanalysisand pages 10-10). |
| Molecular function | cryaba/αBa functions as an ATP-independent small heat shock “holdase” chaperone that binds destabilized proteins and limits aggregation. Compared with cryabb, cryaba shows lower baseline chaperone activity and may require stress-linked post-translational activation. In zebrafish lens biology, αB-crystallin also contributes to lysosomal homeostasis, with evidence that αB-crystallin stabilizes the ATP6V1A–mTORC1 complex to maintain lysosomal acidity. | Zou et al., 2015, Exp Eye Res, https://doi.org/10.1016/j.exer.2015.07.001; Rossen et al., 2025, Front Cell Dev Biol, https://doi.org/10.3389/fcell.2025.1552988 | Client specificity for zebrafish cryaba is not well resolved; much mechanistic detail on lysosomal complex stabilization is summarized through review of zebrafish plus complementary mammalian work rather than a purified zebrafish cryaba biochemical assay (rossen2025zebrafishasa pages 4-5, zou2015aconservedrole pages 1-2, rossen2025zebrafishasa pages 3-4). |
| Key pathways/regulation | A recent zebrafish study links cryaba to proteostatic/oxidative stress crosstalk with Nrf2. Combined loss of nrf2 and cryaba in lens upregulated the cholesterol biosynthesis pathway, and pharmacologic lowering of cholesterol (atorvastatin/lovastatin) increased lens-defect penetrance, implicating sterol homeostasis in phenotype modification. Separately, hsf4−/− lenses show reduced cryaba expression and increased lysosomal pH, placing cryaba downstream of Hsf4 in lens proteostasis. | Park et al., 2023, Front Mol Biosci, https://doi.org/10.3389/fmolb.2023.1185704; Rossen et al., 2025, Front Cell Dev Biol, https://doi.org/10.3389/fcell.2025.1552988 | RNA-seq sample sizes in the Nrf2/cryab study were limited, and exact fold changes are not provided in the available evidence excerpts; pathway-level inference is stronger than single direct molecular-cascade proof for every step (rossen2025zebrafishasa pages 4-5, park2023interplaybetweennrf2 pages 1-2, park2023interplaybetweennrf2 pages 9-10, park2023interplaybetweennrf2 media 77804744). |
| Expression & localization | During early development, cryaba is reported as predominantly non-ocular relative to cryaa, with expression noted across brain, heart, skeletal muscle, liver and some lens cell contexts in single-cell analyses; other recent summaries state cryaba becomes more lens-restricted with maturation. RT-PCR detected cryaba transcription from about 24 hpf. Figure evidence from Park et al. shows tissue-level cryaba/cryabb mRNA measurements in lens and heart. | Rossen et al., 2025, Front Cell Dev Biol, https://doi.org/10.3389/fcell.2025.1552988; Peng et al., 2024, Mol Vis, https://doi.org/10.63500/mv_v30_123; Park et al., 2023, Front Mol Biosci, https://doi.org/10.3389/fmolb.2023.1185704; Zou et al., 2015, Exp Eye Res, https://doi.org/10.1016/j.exer.2015.07.001 | Expression literature is somewhat inconsistent because developmental stage, assay type, and paralog separation differ across studies; explicit subcellular localization of zebrafish Cryaba remains limited in the provided evidence (rossen2025zebrafishasa pages 3-4, park2023interplaybetweennrf2 pages 9-10, peng2024thegenerationand pages 2-3, zou2015aconservedrole pages 4-6, park2023interplaybetweennrf2 media 77804744). |
| Phenotypes/knockout | Phenotypes are context- and method-dependent. CRISPR null studies reported no significant early lens defects in cryaba−/− larvae at 72–96 hpf, whereas morpholino knockdown caused lens abnormalities in about ~50% of embryos and could be partially rescued by rat Cryaa transgene expression. A later summary reports ~50% of cryaba−/− adults developed age-related cataract by 2 years versus ~25% in wild type/cryaa−/−. Double mutants (cryaba−/−; cryabb−/− or cryaa−/−; cryaba−/−) showed 75–95% lens abnormality frequencies in one study. cryaba loss also contributes to stress-induced heart edema, worsened by nrf2 deficiency. | Posner et al., 2021, bioRxiv, https://doi.org/10.1101/2021.12.22.473921; Zou et al., 2015, Exp Eye Res, https://doi.org/10.1016/j.exer.2015.07.001; Park et al., 2023, Front Mol Biosci, https://doi.org/10.3389/fmolb.2023.1185704; Rossen et al., 2025, Front Cell Dev Biol, https://doi.org/10.3389/fcell.2025.1552988 | This is the most conflicted area: morpholino, CRISPR, and background-dependent studies disagree on penetrance; heart-edema results are supported, but exact percentages were not available in the excerpts (rossen2025zebrafishasa pages 4-5, zou2015aconservedrole pages 4-6, posner2021effectsofαcrystallin pages 10-12, park2023interplaybetweennrf2 pages 10-11, posner2021effectsofαcrystallin pages 1-3, park2023interplaybetweennrf2 media f49f3e8a). |
| Applications/implementations | Zebrafish cryaba biology is being used to model congenital/age-related cataract, proteostasis failure, and cardiac stress susceptibility. Human disease alleles such as CRYAB R120G have been expressed/knocked in within zebrafish lens systems, producing mild lens defects that worsen on cryaba/cryabb-null backgrounds, supporting use of zebrafish for variant interpretation and modifier studies. | Wu et al., 2018, PLoS ONE, https://doi.org/10.1371/journal.pone.0207540; Park et al., 2023, Front Mol Biosci, https://doi.org/10.3389/fmolb.2023.1185704; Rossen et al., 2025, Front Cell Dev Biol, https://doi.org/10.3389/fcell.2025.1552988 | Most translational implementations involve zebrafish as a disease model rather than direct therapeutic targeting of endogenous cryaba; some cited studies are reviews or transgenic paradigms rather than native cryaba functional assays alone (rossen2025zebrafishasa pages 4-5, park2023interplaybetweennrf2 pages 10-11). |
| Recent structural/biomedical context | Although zebrafish cryaba itself lacks a 2023–2024 structure in the provided context, current CRYAB/HSPB5 research reinforces interpretation of cryaba as a dynamic oligomeric sHSP chaperone whose activity depends on α-crystallin-domain assembly, NT-IXI interactions, and oligomer remodeling. Recent human/vertebrate work also highlights CRYAB roles in mitochondrial protection, anti-apoptosis, aggregation disease, and tissue repair, providing a mechanistic framework relevant to zebrafish ortholog annotation. | McFarland et al., 2024, Nat Commun, https://doi.org/10.1038/s41467-024-54647-7; Wang et al., 2023, Int J Mol Sci, https://doi.org/10.3390/ijms25010471; Wang et al., 2024, JCI Insight, https://doi.org/10.1172/jci.insight.182209 | These biomedical/structural data are largely non-zebrafish and should be used for cautious orthology-based inference only, not as direct evidence for unique zebrafish cryaba localization or substrate repertoire (rossen2025zebrafishasa pages 2-3). |
Table: This table summarizes zebrafish cryaba (UniProt Q9PUR2) functional annotation evidence across identity, molecular function, regulation, expression, phenotypes, and translational context. It highlights zebrafish-specific findings where available and notes where conclusions rely on review synthesis or orthology-based inference.
References
(rossen2025zebrafishasa pages 3-4): Jennifer L. Rossen, Antionette L. Williams, and Brenda L. Bohnsack. Zebrafish as a model for crystallin-associated congenital cataracts in humans. Frontiers in Cell and Developmental Biology, Mar 2025. URL: https://doi.org/10.3389/fcell.2025.1552988, doi:10.3389/fcell.2025.1552988. This article has 5 citations.
(posner2021effectsofαcrystallin pages 1-3): Mason Posner, Kelly L. Murray, Brandon Andrew, Stuart Brdicka, Alexis Roberts, Kirstan Franklin, Adil Hussen, Taylor Kaye, Emmaline Kepp, Mathew S. McDonald, Tyler Snodgrass, Keith Zientek, and Larry L. David. Effects of α-crystallin gene knockout on zebrafish lens development. bioRxiv, Dec 2021. URL: https://doi.org/10.1101/2021.12.22.473921, doi:10.1101/2021.12.22.473921. This article has 0 citations.
(park2023interplaybetweennrf2 pages 1-2): Jinhee Park, Samantha MacGavin, Laurie Niederbrach, and Hassane S. Mchaourab. Interplay between nrf2 and αb-crystallin in the lens and heart of zebrafish under proteostatic stress. Frontiers in Molecular Biosciences, Jul 2023. URL: https://doi.org/10.3389/fmolb.2023.1185704, doi:10.3389/fmolb.2023.1185704. This article has 4 citations.
(posner2021effectsofαcrystallin pages 15-18): Mason Posner, Kelly L. Murray, Brandon Andrew, Stuart Brdicka, Alexis Roberts, Kirstan Franklin, Adil Hussen, Taylor Kaye, Emmaline Kepp, Mathew S. McDonald, Tyler Snodgrass, Keith Zientek, and Larry L. David. Effects of α-crystallin gene knockout on zebrafish lens development. bioRxiv, Dec 2021. URL: https://doi.org/10.1101/2021.12.22.473921, doi:10.1101/2021.12.22.473921. This article has 0 citations.
(zou2015aconservedrole pages 1-2): Ping Zou, Shu-Yu Wu, Hanane A. Koteiche, Sanjay Mishra, Daniel S. Levic, Ela Knapik, Wenbiao Chen, and Hassane S. Mchaourab. A conserved role of αa-crystallin in the development of the zebrafish embryonic lens. Experimental eye research, 138:104-13, Sep 2015. URL: https://doi.org/10.1016/j.exer.2015.07.001, doi:10.1016/j.exer.2015.07.001. This article has 38 citations and is from a peer-reviewed journal.
(rossen2025zebrafishasa pages 2-3): Jennifer L. Rossen, Antionette L. Williams, and Brenda L. Bohnsack. Zebrafish as a model for crystallin-associated congenital cataracts in humans. Frontiers in Cell and Developmental Biology, Mar 2025. URL: https://doi.org/10.3389/fcell.2025.1552988, doi:10.3389/fcell.2025.1552988. This article has 5 citations.
(zou2015aconservedrole pages 4-6): Ping Zou, Shu-Yu Wu, Hanane A. Koteiche, Sanjay Mishra, Daniel S. Levic, Ela Knapik, Wenbiao Chen, and Hassane S. Mchaourab. A conserved role of αa-crystallin in the development of the zebrafish embryonic lens. Experimental eye research, 138:104-13, Sep 2015. URL: https://doi.org/10.1016/j.exer.2015.07.001, doi:10.1016/j.exer.2015.07.001. This article has 38 citations and is from a peer-reviewed journal.
(rossen2025zebrafishasa pages 4-5): Jennifer L. Rossen, Antionette L. Williams, and Brenda L. Bohnsack. Zebrafish as a model for crystallin-associated congenital cataracts in humans. Frontiers in Cell and Developmental Biology, Mar 2025. URL: https://doi.org/10.3389/fcell.2025.1552988, doi:10.3389/fcell.2025.1552988. This article has 5 citations.
(peng2024thegenerationand pages 2-3): Xuyan Peng, Xiaolin Jia, Guohui Shang, Mengjiao Xue, Mingjun Jiang, Dandan Chen, Fengyan Zhang, and Yanzhong Hu. The generation and characterization of a transgenic zebrafish line with lens-specific cre expression. Molecular Vision, 30:123-136, Jan 2024. URL: https://doi.org/10.63500/mv_v30_123, doi:10.63500/mv_v30_123. This article has 2 citations and is from a peer-reviewed journal.
(park2023interplaybetweennrf2 media 77804744): Jinhee Park, Samantha MacGavin, Laurie Niederbrach, and Hassane S. Mchaourab. Interplay between nrf2 and αb-crystallin in the lens and heart of zebrafish under proteostatic stress. Frontiers in Molecular Biosciences, Jul 2023. URL: https://doi.org/10.3389/fmolb.2023.1185704, doi:10.3389/fmolb.2023.1185704. This article has 4 citations.
(park2023interplaybetweennrf2 media f49f3e8a): Jinhee Park, Samantha MacGavin, Laurie Niederbrach, and Hassane S. Mchaourab. Interplay between nrf2 and αb-crystallin in the lens and heart of zebrafish under proteostatic stress. Frontiers in Molecular Biosciences, Jul 2023. URL: https://doi.org/10.3389/fmolb.2023.1185704, doi:10.3389/fmolb.2023.1185704. This article has 4 citations.
(park2023interplaybetweennrf2 media adcb316d): Jinhee Park, Samantha MacGavin, Laurie Niederbrach, and Hassane S. Mchaourab. Interplay between nrf2 and αb-crystallin in the lens and heart of zebrafish under proteostatic stress. Frontiers in Molecular Biosciences, Jul 2023. URL: https://doi.org/10.3389/fmolb.2023.1185704, doi:10.3389/fmolb.2023.1185704. This article has 4 citations.
(posner2021effectsofαcrystallin pages 10-12): Mason Posner, Kelly L. Murray, Brandon Andrew, Stuart Brdicka, Alexis Roberts, Kirstan Franklin, Adil Hussen, Taylor Kaye, Emmaline Kepp, Mathew S. McDonald, Tyler Snodgrass, Keith Zientek, and Larry L. David. Effects of α-crystallin gene knockout on zebrafish lens development. bioRxiv, Dec 2021. URL: https://doi.org/10.1101/2021.12.22.473921, doi:10.1101/2021.12.22.473921. This article has 0 citations.
(park2023interplaybetweennrf2 pages 10-11): Jinhee Park, Samantha MacGavin, Laurie Niederbrach, and Hassane S. Mchaourab. Interplay between nrf2 and αb-crystallin in the lens and heart of zebrafish under proteostatic stress. Frontiers in Molecular Biosciences, Jul 2023. URL: https://doi.org/10.3389/fmolb.2023.1185704, doi:10.3389/fmolb.2023.1185704. This article has 4 citations.
(park2023interplaybetweennrf2 pages 9-10): Jinhee Park, Samantha MacGavin, Laurie Niederbrach, and Hassane S. Mchaourab. Interplay between nrf2 and αb-crystallin in the lens and heart of zebrafish under proteostatic stress. Frontiers in Molecular Biosciences, Jul 2023. URL: https://doi.org/10.3389/fmolb.2023.1185704, doi:10.3389/fmolb.2023.1185704. This article has 4 citations.
(elicker2007genomewideanalysisand pages 10-10): Kimberly S. Elicker and Lara D. Hutson. Genome-wide analysis and expression profiling of the small heat shock proteins in zebrafish. Gene, 403 1-2:60-9, Nov 2007. URL: https://doi.org/10.1016/j.gene.2007.08.003, doi:10.1016/j.gene.2007.08.003. This article has 101 citations and is from a peer-reviewed journal.