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The literature retrieved here consistently identifies AUP1 as Ancient ubiquitous protein 1 in Homo sapiens, corresponding to UniProt Q9Y679, a ~410 aa protein that localizes to the endoplasmic reticulum (ER) and lipid droplets (LDs) and links LD biology to ubiquitin-dependent ER protein quality control (ERAD). (spandl2011ancientubiquitousprotein pages 3-4, klemm2011dualroleof pages 1-2)
Two frequently used functional descriptors are consistent with the UniProt entry you provided: (i) lipid droplet-regulating protein and (ii) a factor influencing VLDL assembly in liver/hepatocyte models. (zhang2017aup1(ancientubiquitous pages 1-2)
LDs are neutral-lipid storage organelles bounded by a phospholipid monolayer, and many LD membrane proteins are inserted first into the ER and then partition to LDs. AUP1 is a prototypical ER/LD “dual-localized” protein, found in LD proteomes and also associated with ER quality-control machinery. (klemm2011dualroleof pages 1-2, spandl2011ancientubiquitousprotein pages 3-4)
ERAD is a protein quality control pathway in which misfolded or regulated ER proteins are ubiquitinated and then extracted for proteasomal degradation. AUP1 acts as an ERAD accessory factor, coupling substrate handling to the ubiquitination machinery. (klemm2011dualroleof pages 1-1, klemm2011dualroleof pages 11-12)
AUP1 contains two key functional modules:
- CUE domain (“coupling of ubiquitin conjugation to ER degradation”): a ubiquitin-binding domain that mediates interactions with ubiquitinated proteins and ER quality-control components. (klemm2011dualroleof pages 1-1, klemm2011dualroleof pages 4-5)
- G2BR (UBE2G2-binding region): a short C-terminal region that binds and regulates the E2 enzyme UBE2G2 (also called UBC7). (smith2021astructurallyconserved pages 1-2, klemm2011dualroleof pages 11-12)
A schematic of this domain architecture and the LD recruitment concept is shown in the figures retrieved from Spandl et al. (JBC, 2011). (spandl2011ancientubiquitousprotein media 788c5e23, spandl2011ancientubiquitousprotein media ebcd1b79)
AUP1 is enriched on LDs with additional reticular staining consistent with the ER; this has been supported by confocal microscopy, LD flotation, and immunoelectron microscopy. (spandl2011ancientubiquitousprotein pages 3-4)
Mechanistically, AUP1 is an integral membrane protein that inserts via an N-terminal hydrophobic region in a way that leaves both termini cytosolic (hairpin/monotopic insertion), consistent with its role in recruiting cytosolic ubiquitination factors to ER/LD surfaces. (klemm2011dualroleof pages 1-1)
A central, well-supported mechanism is that AUP1 recruits UBE2G2 to ER/LD-associated membranes via its G2BR, enabling efficient ubiquitination during ERAD. (klemm2011dualroleof pages 11-12, klemm2011dualroleof pages 4-5)
High-resolution mechanistic work (structure-function) showed that AUP1’s 27-aa G2BR binds the “backside” of UBE2G2 with low-nanomolar affinity, stabilizes UBE2G2 levels in cells, recruits it to the ER, and allosterically promotes ubiquitination with ERAD E3 ligases. (smith2021astructurallyconserved pages 1-2, smith2021astructurallyconserved pages 15-17)
Klemm et al. (JBC, 2011) provides evidence that AUP1’s CUE domain regulates polyubiquitination and promotes interactions with the HRD1 complex and dislocation substrates; mutation of conserved CUE residues reduces AUP1 association with ERAD/dislocation components such as p97/VCP, SEL1L, OS9, UBXD8, HRD1. (klemm2011dualroleof pages 4-5, klemm2011dualroleof pages 11-12)
AUP1 associates with the HRD1–SEL1L ER quality-control complex; AUP1 depletion impairs degradation of misfolded ER proteins, supporting a direct role in ERAD. (klemm2011dualroleof pages 1-1)
Concurrently, AUP1 localizes to LDs and influences LD abundance/behavior, supporting the concept that ER protein quality control and LD biology are functionally connected. (klemm2011dualroleof pages 1-2, klemm2011dualroleof pages 1-1)
Jo et al. (MBoC, 2013) provides direct functional evidence that AUP1 promotes sterol-induced ubiquitination and ERAD of HMG-CoA reductase, and affects ERAD of Insig-1 and SREBP precursors. Mechanistically, AUP1 facilitates E2 recruitment/binding to E3 ligases including gp78 and Trc8, and localizes this process to LD-associated ER membranes. (jo2013ancientubiquitousprotein1 pages 1-2)
In hepatocyte models, AUP1 is reported to interact with apoB100 and modulate its ubiquitination and proteasomal degradation, with downstream effects on VLDL output and LD size. (zhang2017aup1(ancientubiquitous pages 1-2, zamani2016roleofancienta pages 53-57)
Although much mechanistic AUP1 work predates 2023, recent biomedical literature increasingly frames AUP1 as part of an LD ubiquitination axis relevant to lipophagy and pathogen-driven lipid remodeling (often via the AUP1–UBE2G2 functional relationship). (zhu2024aup1transcriptionallyactivated pages 1-2, wu2024identificationandanalysis pages 1-2)
A 2024 primary study in Cells identified AUP1 as a novel interactor of NKCC2 (ER-resident form) and OS9. AUP1 overexpression decreased NKCC2 protein by enhancing ER retention and ERAD; this effect was fully abolished by ERAD inhibitors MG132 (proteasome) or kifunensine (α-mannosidase inhibitor), and AUP1 knockdown/dominant-negative strongly reduced NKCC2 polyubiquitination while increasing NKCC2 levels. AUP1 also downregulated the related cotransporter NCC, suggesting a broader role as a regulator of sodium-dependent chloride cotransporters. (frachon2024aup1regulatesthe pages 1-2)
This work exemplifies how AUP1’s core ERAD function is being extended into clinically relevant membrane-protein proteostasis (e.g., Bartter syndrome context). (frachon2024aup1regulatesthe pages 1-2)
A 2023 glioma study integrated TCGA multi-omics and experimental validation, reporting that AUP1 is increased in tumor components and associated with tumor grade and inflammatory microenvironment features. The dataset scale was TCGA n=690 with immunohistochemical validation on 78 clinical cases. Functionally, siRNA-mediated downregulation of AUP1 mainly impacted proliferation rather than measurable lipophagy activity in their U87MG assays. (chang2023ancientubiquitousprotein pages 1-2)
A 2024 cervical cancer study proposed a mechanism in which KDM5B transcriptionally activates AUP1, promoting lipid-metabolism reprogramming and malignant behaviors; AUP1 interference reduced malignant phenotypes and lipid-metabolic measures (e.g., LD staining/neutral lipid metrics), and KDM5B overexpression could counteract AUP1 knockdown effects. (zhu2024aup1transcriptionallyactivated pages 1-2)
A 2024 Viruses paper used multiple GEO datasets (bulk RNA-seq and scRNA-seq) and machine-learning feature selection to nominate AUP1 among seven lipophagy-related biomarkers/targets for COVID-19 and reported 47 lipophagy-related differentially expressed genes (DEGs; 27 down, 20 up) under criteria adj. p < 0.05 and log2FC > 0.5. This constitutes computational association rather than direct AUP1 mechanism in infection. (wu2024identificationandanalysis pages 4-7, wu2024identificationandanalysis pages 1-2)
Multiple primary studies converge on the view that AUP1 is a multi-compartment adaptor/accessory factor operating at ER/LD membranes, chiefly by recruiting and regulating ubiquitination machinery (notably UBE2G2) to enable ERAD and regulated degradation events that intersect lipid metabolism. (klemm2011dualroleof pages 1-2, smith2021astructurallyconserved pages 15-17, jo2013ancientubiquitousprotein1 pages 1-2)
A key expert-level mechanistic refinement from structural studies is that AUP1’s G2BR is not merely a tether: it binds UBE2G2 with high specificity/affinity and tunes E2 activity and stability—features that explain why AUP1 can be rate-limiting in specific ERAD branches and why its perturbation can have pronounced effects on membrane protein fate. (smith2021astructurallyconserved pages 15-17)
Importantly, several 2023–2024 disease-focused papers accessible here provide cohort sizes and thresholds but do not expose key numerical effect sizes (e.g., hazard ratios, exact fold-changes of AUP1, or quantified rescue magnitudes) in the snippets available; where absent, this report does not infer them. (frachon2024aup1regulatesthe pages 1-2, chang2023ancientubiquitousprotein pages 1-2)
The following table summarizes core functional annotation and recent (2023–2024) applied contexts.
| Aspect | Key points | Representative evidence (with citation IDs) |
|---|---|---|
| Identity | Human AUP1 corresponds to UniProt Q9Y679; also called Ancient ubiquitous protein 1 and described as a lipid droplet-regulating VLDL assembly factor. It is a broadly expressed, conserved ~410 aa protein linked to ER protein quality control and lipid droplet biology. | (klemm2011dualroleof pages 1-2, spandl2011ancientubiquitousprotein pages 3-4, zhang2017aup1(ancientubiquitous pages 1-2) |
| Domains | Domain architecture includes an N-terminal hydrophobic hairpin/membrane-inserting region, a putative acyltransferase domain containing the conserved HX4D motif, a CUE ubiquitin-binding domain, and a C-terminal G2BR/UBE2G2-binding region. | (klemm2011dualroleof pages 1-1, spandl2011ancientubiquitousprotein pages 3-4, spandl2011ancientubiquitousprotein media 788c5e23) |
| Localization | AUP1 localizes to both the endoplasmic reticulum (ER) and lipid droplets (LDs). Imaging, flotation, and immuno-EM studies show a major LD pool plus reticular ER staining. | (klemm2011dualroleof pages 1-2, spandl2011ancientubiquitousprotein pages 3-4) |
| Membrane topology | AUP1 is inserted in a monotopic hairpin topology, with both N- and C-termini facing the cytosol; this topology is important for ER-to-LD targeting. A transmembrane-converted mutant loses LD localization. | (klemm2011dualroleof pages 1-1, spandl2011ancientubiquitousprotein media 788c5e23) |
| Key interacting partners | Experimentally supported partners include UBE2G2/UBC7, HRD1-SEL1L, p97/VCP, OS9, UBXD8, gp78/AMFR, and Trc8/RNF139. AUP1 also interacts with disease-relevant clients such as apoB100, NKCC2, and NCC in specific contexts. | (klemm2011dualroleof pages 4-5, jo2013ancientubiquitousprotein1 pages 1-2, frachon2024aup1regulatesthe pages 1-2, zamani2016roleofancienta pages 53-57) |
| Core mechanism: CUE domain | The CUE domain mediates ubiquitin/substrate engagement and promotes interaction with ER quality-control/dislocation machinery. CUE mutations reduce AUP1 association with p97, SEL1L, UBXD8, OS9, UBC6e, and HRD1, and impair substrate-related ubiquitination behavior. | (klemm2011dualroleof pages 4-5, klemm2011dualroleof pages 11-12) |
| Core mechanism: G2BR domain | The G2BR directly binds UBE2G2, recruits it to ER membranes, stabilizes cellular UBE2G2, and allosterically activates ERAD ubiquitination. Structural work showed a conserved interface and low-nanomolar affinity for UBE2G2 binding. | (smith2021astructurallyconserved pages 1-2, smith2021astructurallyconserved pages 15-17, klemm2011dualroleof pages 11-12) |
| ERAD role | AUP1 is an ERAD accessory factor in the HRD1-SEL1L complex. It recruits E2 activity, supports ubiquitination of misfolded ER proteins, and is required for efficient degradation of selected ERAD substrates. | (klemm2011dualroleof pages 1-1, klemm2011dualroleof pages 11-12, klemm2011dualroleof pages 3-4) |
| Lipid droplet role | AUP1 links ubiquitination machinery to LDs and can influence LD abundance, clustering, and protein composition. Monoubiquitinated AUP1 promotes LD clustering, and AUP1 expression affects cellular LD levels. | (klemm2011dualroleof pages 1-2, spandl2011ancientubiquitousprotein pages 3-4, klemm2011dualroleof pages 1-1) |
| Sterol/cholesterol pathway | In lipid droplet-associated ER membranes, AUP1 promotes sterol-induced ubiquitination/ERAD of HMG-CoA reductase, Insig-1, and SREBP precursors by helping recruit E2 activity to gp78 and Trc8 complexes. | (jo2013ancientubiquitousprotein1 pages 1-2) |
| ApoB/VLDL pathway | In hepatocytes, AUP1 interacts with apoB100, promotes its ubiquitination/degradation, influences LD size, and thereby regulates VLDL assembly and secretion. Knockdown is associated with more VLDL1-sized apoB100 particles and increased TG in VLDL-sized fractions. | (zhang2017aup1(ancientubiquitous pages 1-2, zamani2016roleofancienta pages 53-57, zamani2016roleofancient pages 53-57) |
| 2023–2024 development: viral lipophagy | Recent work reinforced AUP1’s role in virus-triggered lipophagy, especially with UBE2G2 in flaviviral infection. 2023 work showed UBE2G2 is required for replication organelle biogenesis and virus production in conjunction with AUP1. | (zhu2024aup1transcriptionallyactivated pages 1-2, wu2024identificationandanalysis pages 1-2) |
| 2023–2024 development: renal ERAD | A 2024 Cells study identified AUP1 as a regulator of NKCC2 and NCC ERAD/polyubiquitination in renal cells. AUP1 co-expression lowered NKCC2, while MG132 or kifunensine fully abolished the AUP1 effect. | (frachon2024aup1regulatesthe pages 1-2) |
| 2023–2024 application: glioma biomarker | A 2023 glioma study found AUP1 is a poor-prognosis biomarker associated with tumor grade, TP53 status, tumor mutation burden, proliferation, and inflamed microenvironments. Functional knockdown mainly affected proliferation rather than lipophagy in U87MG cells. | (chang2023ancientubiquitousprotein pages 1-2) |
| 2023–2024 application: cervical cancer | A 2024 study reported that KDM5B transcriptionally activates AUP1, promoting lipid-metabolism reprogramming and malignant progression in cervical cancer; AUP1 knockdown reduced malignant behaviors and lipid metabolic outputs. | (zhu2024aup1transcriptionallyactivated pages 1-2) |
| 2023–2024 application: COVID-19 bioinformatics | AUP1 was identified among seven lipophagy-related biomarker/drug-target candidates in COVID-19 transcriptomic analyses, where lipophagy appeared downregulated and lipid-droplet formation upregulated. This is currently computational rather than direct mechanistic validation for AUP1. | (wu2024identificationandanalysis pages 1-2, wu2024identificationandanalysis pages 4-7) |
| Quantitative data points | Explicit recent numbers available in accessible sources include: glioma study TCGA n=690 plus IHC n=78; COVID-19 study identified 47 lipophagy-related DEGs (27 down, 20 up) and selected 7 feature proteins; cervical cancer methods used 50 nmol/L reagents in 3×10^5 cells/well and viability assays with 2×10^4 cells/well; cervical cancer burden cited 604,000 new cases and 342,000 deaths in 2020. | (zhu2024aup1transcriptionallyactivated pages 1-2, wu2024identificationandanalysis pages 4-7, chang2023ancientubiquitousprotein pages 1-2) |
Table: This table summarizes the verified identity, domains, localization, mechanisms, pathways, and recent 2023–2024 applications of human AUP1 (UniProt Q9Y679). It is useful as a compact evidence map linking classic mechanistic studies with newer disease and biomarker contexts.
References
(spandl2011ancientubiquitousprotein pages 3-4): Johanna Spandl, Daniel Lohmann, Lars Kuerschner, Christine Moessinger, and Christoph Thiele. Ancient ubiquitous protein 1 (aup1) localizes to lipid droplets and binds the e2 ubiquitin conjugase g2 (ube2g2) via its g2 binding region. Journal of Biological Chemistry, 286:5599-5606, Feb 2011. URL: https://doi.org/10.1074/jbc.m110.190785, doi:10.1074/jbc.m110.190785. This article has 154 citations and is from a domain leading peer-reviewed journal.
(klemm2011dualroleof pages 1-2): Elizabeth J. Klemm, Eric Spooner, and Hidde L. Ploegh. Dual role of ancient ubiquitous protein 1 (aup1) in lipid droplet accumulation and endoplasmic reticulum (er) protein quality control. Journal of Biological Chemistry, 286:37602-37614, Oct 2011. URL: https://doi.org/10.1074/jbc.m111.284794, doi:10.1074/jbc.m111.284794. This article has 161 citations and is from a domain leading peer-reviewed journal.
(zhang2017aup1(ancientubiquitous pages 1-2): Jing Zhang, Mostafa Zamani, Christoph Thiele, Jennifer Taher, Mohsen Amir Alipour, Zemin Yao, and Khosrow Adeli. Aup1 (ancient ubiquitous protein 1) is a key determinant of hepatic very-low–density lipoprotein assembly and secretion. Arteriosclerosis, Thrombosis, and Vascular Biology, 37:633–642, Apr 2017. URL: https://doi.org/10.1161/atvbaha.117.309000, doi:10.1161/atvbaha.117.309000. This article has 24 citations and is from a domain leading peer-reviewed journal.
(klemm2011dualroleof pages 1-1): Elizabeth J. Klemm, Eric Spooner, and Hidde L. Ploegh. Dual role of ancient ubiquitous protein 1 (aup1) in lipid droplet accumulation and endoplasmic reticulum (er) protein quality control. Journal of Biological Chemistry, 286:37602-37614, Oct 2011. URL: https://doi.org/10.1074/jbc.m111.284794, doi:10.1074/jbc.m111.284794. This article has 161 citations and is from a domain leading peer-reviewed journal.
(klemm2011dualroleof pages 11-12): Elizabeth J. Klemm, Eric Spooner, and Hidde L. Ploegh. Dual role of ancient ubiquitous protein 1 (aup1) in lipid droplet accumulation and endoplasmic reticulum (er) protein quality control. Journal of Biological Chemistry, 286:37602-37614, Oct 2011. URL: https://doi.org/10.1074/jbc.m111.284794, doi:10.1074/jbc.m111.284794. This article has 161 citations and is from a domain leading peer-reviewed journal.
(klemm2011dualroleof pages 4-5): Elizabeth J. Klemm, Eric Spooner, and Hidde L. Ploegh. Dual role of ancient ubiquitous protein 1 (aup1) in lipid droplet accumulation and endoplasmic reticulum (er) protein quality control. Journal of Biological Chemistry, 286:37602-37614, Oct 2011. URL: https://doi.org/10.1074/jbc.m111.284794, doi:10.1074/jbc.m111.284794. This article has 161 citations and is from a domain leading peer-reviewed journal.
(smith2021astructurallyconserved pages 1-2): Christopher E Smith, Y. Tsai, Yu-He Liang, Domarin Khago, J. Mariano, ID JessLi, S. Tarasov, ID EmmaGergel, B. Tsai, ID MatthewVillaneuva, Michelle E. Clapp, ID ValentinMagidson, R. Chari, ID RAndrewByrd, ID XinhuaJi, ID AllanM.Weissman, and Raquel L. Lieberman. A structurally conserved site in aup1 binds the e2 enzyme ube2g2 and is essential for er-associated degradation. Dec 2021. URL: https://doi.org/10.1371/journal.pbio.3001474, doi:10.1371/journal.pbio.3001474. This article has 23 citations and is from a highest quality peer-reviewed journal.
(spandl2011ancientubiquitousprotein media 788c5e23): Johanna Spandl, Daniel Lohmann, Lars Kuerschner, Christine Moessinger, and Christoph Thiele. Ancient ubiquitous protein 1 (aup1) localizes to lipid droplets and binds the e2 ubiquitin conjugase g2 (ube2g2) via its g2 binding region. Journal of Biological Chemistry, 286:5599-5606, Feb 2011. URL: https://doi.org/10.1074/jbc.m110.190785, doi:10.1074/jbc.m110.190785. This article has 154 citations and is from a domain leading peer-reviewed journal.
(spandl2011ancientubiquitousprotein media ebcd1b79): Johanna Spandl, Daniel Lohmann, Lars Kuerschner, Christine Moessinger, and Christoph Thiele. Ancient ubiquitous protein 1 (aup1) localizes to lipid droplets and binds the e2 ubiquitin conjugase g2 (ube2g2) via its g2 binding region. Journal of Biological Chemistry, 286:5599-5606, Feb 2011. URL: https://doi.org/10.1074/jbc.m110.190785, doi:10.1074/jbc.m110.190785. This article has 154 citations and is from a domain leading peer-reviewed journal.
(smith2021astructurallyconserved pages 15-17): Christopher E Smith, Y. Tsai, Yu-He Liang, Domarin Khago, J. Mariano, ID JessLi, S. Tarasov, ID EmmaGergel, B. Tsai, ID MatthewVillaneuva, Michelle E. Clapp, ID ValentinMagidson, R. Chari, ID RAndrewByrd, ID XinhuaJi, ID AllanM.Weissman, and Raquel L. Lieberman. A structurally conserved site in aup1 binds the e2 enzyme ube2g2 and is essential for er-associated degradation. Dec 2021. URL: https://doi.org/10.1371/journal.pbio.3001474, doi:10.1371/journal.pbio.3001474. This article has 23 citations and is from a highest quality peer-reviewed journal.
(jo2013ancientubiquitousprotein1 pages 1-2): Youngah Jo, Isamu Z. Hartman, and Russell A. DeBose-Boyd. Ancient ubiquitous protein-1 mediates sterol-induced ubiquitination of 3-hydroxy-3-methylglutaryl coa reductase in lipid droplet–associated endoplasmic reticulum membranes. Molecular Biology of the Cell, 24:169-183, Feb 2013. URL: https://doi.org/10.1091/mbc.e12-07-0564, doi:10.1091/mbc.e12-07-0564. This article has 105 citations and is from a domain leading peer-reviewed journal.
(zamani2016roleofancienta pages 53-57): M Zamani. Role of ancient ubiquitous protein 1 in hepatic apob degradation and vldl production. Unknown journal, 2016.
(zhu2024aup1transcriptionallyactivated pages 1-2): Yingping Zhu, Wenjuan Yang, Xinyan Wang, and Mengmeng Chen. Aup1 transcriptionally activated by kdm5b reprograms lipid metabolism to promote the malignant progression of cervical cancer. International Journal of Oncology, Sep 2024. URL: https://doi.org/10.3892/ijo.2024.5695, doi:10.3892/ijo.2024.5695. This article has 6 citations and is from a peer-reviewed journal.
(wu2024identificationandanalysis pages 1-2): Yujia Wu, Zhenlin Wu, Qiying Jin, Jinyuan Liu, and Peiping Xu. Identification and analysis of biomarkers associated with lipophagy and therapeutic agents for covid-19. Viruses, 16:923, Jun 2024. URL: https://doi.org/10.3390/v16060923, doi:10.3390/v16060923. This article has 6 citations.
(frachon2024aup1regulatesthe pages 1-2): Nadia Frachon, Sylvie Demaretz, Elie Seaayfan, Lydia Chelbi, Dalal Bakhos-Douaihy, and Kamel Laghmani. Aup1 regulates the endoplasmic reticulum-associated degradation and polyubiquitination of nkcc2. Cells, 13:389, Feb 2024. URL: https://doi.org/10.3390/cells13050389, doi:10.3390/cells13050389. This article has 7 citations.
(chang2023ancientubiquitousprotein pages 1-2): Pei-Chi Chang, Yu-Chieh Lin, Hui-Ju Yen, Dueng-Yuan Hueng, Shih-Ming Huang, and Yao-Feng Li. Ancient ubiquitous protein 1 (aup1) is a prognostic biomarker connected with tp53 mutation and the inflamed microenvironments in glioma. Cancer Cell International, Apr 2023. URL: https://doi.org/10.1186/s12935-023-02912-y, doi:10.1186/s12935-023-02912-y. This article has 15 citations and is from a peer-reviewed journal.
(wu2024identificationandanalysis pages 4-7): Yujia Wu, Zhenlin Wu, Qiying Jin, Jinyuan Liu, and Peiping Xu. Identification and analysis of biomarkers associated with lipophagy and therapeutic agents for covid-19. Viruses, 16:923, Jun 2024. URL: https://doi.org/10.3390/v16060923, doi:10.3390/v16060923. This article has 6 citations.
(klemm2011dualroleof pages 3-4): Elizabeth J. Klemm, Eric Spooner, and Hidde L. Ploegh. Dual role of ancient ubiquitous protein 1 (aup1) in lipid droplet accumulation and endoplasmic reticulum (er) protein quality control. Journal of Biological Chemistry, 286:37602-37614, Oct 2011. URL: https://doi.org/10.1074/jbc.m111.284794, doi:10.1074/jbc.m111.284794. This article has 161 citations and is from a domain leading peer-reviewed journal.
(zamani2016roleofancient pages 53-57): M Zamani. Role of ancient ubiquitous protein 1 in hepatic apob degradation and vldl production. Unknown journal, 2016.