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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.

Research Report: Human NBR1 (UniProt Q14596) — Functional Annotation and Current Understanding

1) Target verification (gene/protein identity)

The target protein is human NBR1 (Neighbor of BRCA1 gene 1; UniProt Q14596), an evolutionarily conserved selective autophagy receptor (“sequestosome-1–like receptor”, SLR) with a characteristic multi-domain architecture (PB1, ZZ, FW, LIR(s), UBA) and additional membrane-association features (amphipathic helix) described in authoritative reviews focused on NBR1. (rasmussen2022nbr1thearchetypal pages 1-2, rasmussen2022nbr1thearchetypal pages 4-6)

2) Key concepts and definitions (current understanding)

2.1 Selective autophagy and selective autophagy receptors (SARs)

Autophagy sequesters intracellular material in double-membrane autophagosomes that fuse with endolysosomal compartments to form degradative autolysosomes. Selective autophagy differs from bulk autophagy by targeting defined cargo classes (e.g., aggrephagy, xenophagy, pexophagy) and typically involves cargo tagging, frequently ubiquitination, and cargo receptors that bridge cargo to autophagosome membranes. (vargas2023themechanismsand pages 1-6)

In a broad, authoritative synthesis of mammalian selective autophagy, selective cargo specificity is attributed to receptors including p62/SQSTM1, NBR1, OPTN, and NDP52, which possess both LC3-interacting region (LIR) motifs and ubiquitin-binding domains enabling them to bind cargo and recruit autophagic membranes. (vargas2023themechanismsand pages 1-6)

2.2 NBR1 as an archetypal selective autophagy receptor

A dedicated review describes NBR1 as an “archetypal” selective autophagy receptor with deep evolutionary roots and conserved modular architecture. Mechanistically, NBR1’s defining role is as a multivalent adaptor that:
- recognizes ubiquitinated cargo (via UBA),
- binds ATG8-family proteins (LC3/GABARAP) on phagophores/autophagosomes (via LIRs), and
- assembles higher-order receptor/cargo structures through additional interaction modules (PB1/CC/FW) that facilitate receptor cooperation and autophagy initiation. (rasmussen2022nbr1thearchetypal pages 1-2, rasmussen2022nbr1thearchetypal pages 4-6)

3) Molecular architecture, mechanisms, and pathways

3.1 Domain architecture and core molecular interactions

Human NBR1 contains:
- PB1 domain: mediates strong PB1–PB1 electrostatic interaction with p62; metazoan NBR1 PB1 is described as monomeric (loss of the basic binding surface) but remains recruited to p62 assemblies and can act as a chain terminator of p62 polymers, modulating p62 filament length and body formation. (rasmussen2022nbr1thearchetypal pages 6-8)
- ZZ domain (zinc-finger) and coiled-coil (CC) regions contributing to interaction capacity and assembly. (rasmussen2022nbr1thearchetypal pages 4-6, cerdatroncoso2021protumoralfunctionsof pages 7-8)
- FW (four-tryptophan) domain(s): implicated in cargo/adaptor recognition; in human NBR1, FW-domain binding partners include TAX1BP1 and MAP1B, and FW-mediated recruitment of TAX1BP1 to p62 assemblies is proposed as a coupling point to autophagy machinery. (rasmussen2022nbr1thearchetypal pages 2-4, rasmussen2022nbr1thearchetypal pages 6-8)
- Two LIR motifs (LIR1/LIR2): tether NBR1 to LC3/ATG8 proteins; LIR1 is described as dominant in cells. (rasmussen2022nbr1thearchetypal pages 1-2)
- C-terminal UBA domain: binds mono- and poly-ubiquitin, enabling NBR1 recognition of ubiquitinated cargos and (in the p62-body context) enhancing cargo clustering by bringing a high-affinity ubiquitin-binding module into p62 filaments. (rasmussen2022nbr1thearchetypal pages 6-8, cerdatroncoso2021protumoralfunctionsof pages 7-8)
- Amphipathic helix (AH) near UBA: contributes to membrane association; coincident AH+UBA binding targets NBR1 to ubiquitinated peroxisomes during pexophagy. (rasmussen2022nbr1thearchetypal pages 10-11)

The NBR1 domain schematic and associated partners are visually summarized in a JCB review figure (domain map and interaction partners). (rasmussen2022nbr1thearchetypal media 2c6d1299)

3.2 NBR1 within p62 bodies and autophagy initiation

Mechanistic synthesis indicates NBR1 is frequently recruited to p62/ubiquitin-positive bodies, where it can modulate p62 polymer properties and enhance cargo clustering. In this model, NBR1 also recruits TAX1BP1 (via FW) and links to initiation machinery (including FIP200/ULK-related components) to promote efficient selective-autophagy flux. (rasmussen2022nbr1thearchetypal pages 6-8)

A further development (reported as 2024 work in a 2024-05 preprint posting) argues that the NBR1 LIR region is a protein-interaction hub in which ATG8-family proteins, FIP200, and TAX1BP1 bind overlapping but distinct determinants within a short linear motif, and that phosphorylation can differentially tune binding (enhancing FIP200/ATG8 binding but not TAX1BP1 binding in the peptide-array framework). (north2025thelc3interactingregion pages 1-4)

3.3 Subcellular localization (where NBR1 acts)

Evidence from reviews and primary studies supports a predominantly cytoplasmic role for NBR1 as a receptor that localizes to:
- p62 bodies / ubiquitin-positive aggregates (cytosolic condensates),
- autophagosomal membranes via LC3/ATG8 binding,
- peroxisomes during selective removal (pexophagy) through combined AH+UBA targeting to ubiquitinated peroxisomes. (rasmussen2022nbr1thearchetypal pages 6-8, rasmussen2022nbr1thearchetypal pages 10-11)

In human nucleus pulposus cells, immunofluorescence evidence indicates NBR1 is predominantly cytoplasmic and its interaction with the cargo protein SRBD1 occurs primarily in the cytoplasm. (song2024selectiveautophagyreceptor pages 8-10)

4) Recent developments (prioritizing 2023–2024)

4.1 2024: NBR1 in intervertebral disc degeneration via selective clearance of SRBD1 (human cells; disease mechanism)

A 2024 study in International Journal of Biological Sciences investigated NBR1 in intervertebral disc degeneration (IDD) and nucleus pulposus cell (NPC) senescence, reporting:
- Proteomics after NBR1 knockdown identified 1,082 differentially expressed proteins (819 upregulated, 263 downregulated), indicating broad proteostasis remodeling when NBR1-mediated selective degradation is reduced. (song2024selectiveautophagyreceptor pages 8-10)
- Integration of IP–MS and proteomics identified SRBD1 as a candidate direct NBR1-associated substrate; SRBD1 was reported as ~50.6-fold upregulated after NBR1 knockdown at the protein level while SRBD1 mRNA did not change, consistent with NBR1 regulating SRBD1 protein stability. (song2024selectiveautophagyreceptor pages 8-10)
- Pharmacologic interrogation supported lysosomal/autophagic routing: Baf-A1 (lysosomal inhibition) significantly mitigated SRBD1 degradation, while MG132 (proteasome inhibitor) had minimal influence, supporting an autophagic-lysosomal degradation route for SRBD1. (song2024selectiveautophagyreceptor pages 8-10)
- Mechanistic downstream pathways were linked to SRBD1 accumulation: NBR1 knockdown → SRBD1 accumulation → senescence signaling via AKT1/p53 and RB/p16 pathways and pro-SASP signaling via NF-κB. (song2024selectiveautophagyreceptor pages 1-2)
- Ubiquitin-recognition was functionally required: overexpression of wild-type NBR1 (but not NBR1-ΔUBA) accelerated SRBD1 degradation, supporting a model where NBR1 uses its ubiquitin-binding capacity to drive selective cargo clearance. (song2024selectiveautophagyreceptor pages 8-10)
- Human tissue-level association: NBR1 was described as reduced in IDD, including a statistically significant reduction in NBR1-positive cells in normal (n=11) vs degenerated (n=34) human samples (P<0.01, Mann–Whitney U test). (song2024selectiveautophagyreceptor pages 5-8)

These results extend NBR1 functional annotation beyond canonical “aggregate receptor” roles to a specific, disease-relevant selective cargo–substrate relationship (NBR1→SRBD1) with defined signaling consequences. (song2024selectiveautophagyreceptor pages 1-2, song2024selectiveautophagyreceptor pages 8-10)

4.2 2024: NBR1 turnover during HSV-1 infection (xenophagy-linked antiviral defense)

A 2024 primary study in Cells assessed the dynamics of xenophagy-associated receptors during productive HSV-1 infection in human cells and reported:
- HSV-1 infection in H4 human neuroglioma cells reduced total ubiquitin conjugates and significantly decreased NBR1 protein levels starting from 8 hours post-infection (hpi) (densitometry normalized to β-actin; n=3 biological replicates for NBR1). (pinobelmar2024anintrinsichost pages 6-8)
- Viral load dependence: only high HSV-1 doses (approximately MOI 5–10) produced a notable reduction in receptor levels including NBR1 at 8 hpi. (pinobelmar2024anintrinsichost pages 6-8)
- In HaCaT keratinocytes, NBR1 levels significantly decreased from 4 hpi onward, and the authors highlight NBR1 and NDP52 as among the most impacted receptors. (pinobelmar2024anintrinsichost pages 8-10)
- The report also noted that NBR1 mRNA increased at late time points despite protein loss, consistent with compensatory transcriptional responses amid post-translational depletion. (pinobelmar2024anintrinsichost pages 8-10)

Functionally, this positions NBR1 within a host-defense framework where xenophagy engages receptor turnover during infection and intersects with viral strategies that modulate ubiquitin-dependent pathways. (pinobelmar2024anintrinsichost pages 1-2, pinobelmar2024anintrinsichost pages 8-10)

4.3 2023: Updated framing of receptor-based selectivity in mammalian selective autophagy

The 2023 Nature Reviews Molecular Cell Biology synthesis emphasizes that selective autophagy targets (including xenophagy and aggrephagy) rely on receptors (including NBR1) that bridge cargo to lipidated LC3 via LIR motifs and ubiquitin-binding domains, and highlights the disease relevance of selective-autophagy insufficiency for neurodegeneration and infection. (vargas2023themechanismsand pages 1-6)

5) Current applications and real-world implementations

5.1 Cancer and immune evasion (MHC-I degradation)

An NBR1-focused review summarizes evidence that in pancreatic ductal adenocarcinoma (PDAC) cells, MHC class I molecules can be degraded by NBR1-mediated selective autophagy, and that NBR1 knockdown increases total and surface MHC-I levels, linking NBR1 activity to tumor immune evasion phenotypes (antigen presentation). (rasmussen2022nbr1thearchetypal pages 11-12)

Additional cancer-related literature notes NBR1’s participation in focal adhesion turnover via selective autophagy of ubiquitylated focal adhesion components, influencing migration and metastatic phenotypes in model systems. (cerdatroncoso2021protumoralfunctionsof pages 6-7)

5.2 Degenerative disease biology (IDD) and selective-autophagy targeting

The 2024 IDD/NPC senescence study proposes a selective-autophagy-based intervention logic: rather than globally modulating autophagy, enhancing NBR1-dependent clearance of detrimental substrates (e.g., SRBD1) could be a targeted approach for degenerative disc pathology. (song2024selectiveautophagyreceptor pages 1-2)

5.3 Infection biology and host defense

The 2024 HSV-1 study provides a tractable experimental system where NBR1 and other receptors are monitored as infection progresses, offering an implementation pathway for testing antiviral xenophagy modulation (e.g., receptor turnover, ubiquitin conjugate dynamics, MOI/time dependence). (pinobelmar2024anintrinsichost pages 6-8, pinobelmar2024anintrinsichost pages 8-10)

6) Expert opinions and analysis (authoritative sources)

6.1 “Archetypal receptor” framing and cooperation with p62

Expert synthesis argues that mammalian NBR1 frequently operates in a cooperative network with p62/SQSTM1, often colocalizing with p62 and ubiquitin in pathological inclusions, and that NBR1’s recruitment to p62 bodies plus its high-affinity UBA may enhance the efficiency of ubiquitin-positive cargo clustering and selective-autophagy progression. The same synthesis cautions that because NBR1 and p62 often act together, NBR1-specific effects can be difficult to disentangle experimentally without careful genetic and biochemical designs. (rasmussen2022nbr1thearchetypal pages 11-12, rasmussen2022nbr1thearchetypal pages 6-8)

6.2 Receptor redundancy and context dependence

A 2023 study in mouse ESCs and ESC-derived neurons reported that p62 and NBR1 can be dispensable for aggrephagy in those contexts, implying redundancy across cargo receptors and/or alternative proteostasis pathways that can compensate for loss of canonical SLR functions in certain cell types. This is a key interpretive point for functional annotation: NBR1’s necessity can be cell-type and context dependent, even if its molecular capabilities as an SLR are well supported. (trapannone2023p62andnbr1 pages 7-9)

7) Statistics and data highlights (recent studies)

• IDD/NPC senescence (2024, Song et al.): 1,082 differentially expressed proteins after NBR1 knockdown (819 up; 263 down) (proteomics); SRBD1 upregulated ~50.6-fold at protein level after NBR1 knockdown; reduced NBR1-positive cells in normal vs degenerated human samples (n=11 vs n=34; P<0.01). (song2024selectiveautophagyreceptor pages 8-10, song2024selectiveautophagyreceptor pages 5-8)
• HSV-1 infection (2024, Pino-Belmar et al.): significant NBR1 protein reduction during infection in H4 and HaCaT cells; MOI dependence (notable reduction at MOI ~5–10); densitometric quantification normalized to β-actin with NBR1 biological replicates (n=3 in H4; NBR1 quantified also with replicate counts described in figure captions). (pinobelmar2024anintrinsichost pages 6-8, pinobelmar2024anintrinsichost pages 8-10)

8) Disease associations from a target–disease knowledgebase (Open Targets)

Open Targets lists disease associations for NBR1 (ENSG00000188554; “NBR1 autophagy cargo receptor”) including categories such as neoplasm, neurodegenerative disease, and specific cancers (e.g., gastric and ovarian cancer) with scored evidence and linked literature identifiers. These associations are useful for prioritization but should be interpreted as aggregated evidence rather than direct mechanistic proof. (OpenTargets Search: -NBR1)

9) Visual evidence (domain architecture and functional schematic)

The JCB review provides clear visuals of (i) NBR1 domain architecture and binding partners, (ii) NBR1-centered selective autophagy processes across cargo types, and (iii) NBR1’s mechanistic placement within p62 bodies and initiation machinery. (rasmussen2022nbr1thearchetypal media 2c6d1299, rasmussen2022nbr1thearchetypal media 47b06603, rasmussen2022nbr1thearchetypal media 07b5ca64)

10) Summary functional annotation (human NBR1 / UniProt Q14596)

Primary function: NBR1 is a multivalent selective autophagy cargo receptor that binds ubiquitinated cargo (UBA) and recruits autophagic membranes via ATG8/LC3 binding (LIRs), while coordinating receptor assembly and autophagy initiation through additional interaction modules (PB1/CC/FW; TAX1BP1/FIP200 connections). (rasmussen2022nbr1thearchetypal pages 1-2, rasmussen2022nbr1thearchetypal pages 6-8, north2025thelc3interactingregion pages 1-4)

Where it acts: predominantly cytoplasmic, enriched at p62/ubiquitin-positive condensates, forming autophagosomal membranes, and ubiquitinated peroxisomes during pexophagy; specific cytoplasmic cargo interactions (e.g., SRBD1) are reported in human cells. (rasmussen2022nbr1thearchetypal pages 10-11, song2024selectiveautophagyreceptor pages 8-10)

Pathways/biological processes: aggrephagy, xenophagy/antiviral defense, pexophagy, focal adhesion turnover/migration, and tumor immune evasion phenotypes (MHC-I degradation) depending on context. (rasmussen2022nbr1thearchetypal pages 10-11, rasmussen2022nbr1thearchetypal pages 11-12, cerdatroncoso2021protumoralfunctionsof pages 6-7)

Domain/interactions quick reference

Table: This table summarizes the validated domain architecture of human NBR1 (UniProt Q14596) and its best-supported molecular interactions and selective-autophagy functions. It is useful as a compact functional annotation reference grounded only in the provided source contexts.

References

1. (rasmussen2022nbr1thearchetypal pages 1-2): Nikoline Lander Rasmussen, Athanasios Kournoutis, Trond Lamark, and Terje Johansen. Nbr1: the archetypal selective autophagy receptor. The Journal of Cell Biology, Oct 2022. URL: https://doi.org/10.1083/jcb.202208092, doi:10.1083/jcb.202208092. This article has 110 citations.

2. (rasmussen2022nbr1thearchetypal pages 4-6): Nikoline Lander Rasmussen, Athanasios Kournoutis, Trond Lamark, and Terje Johansen. Nbr1: the archetypal selective autophagy receptor. The Journal of Cell Biology, Oct 2022. URL: https://doi.org/10.1083/jcb.202208092, doi:10.1083/jcb.202208092. This article has 110 citations.

3. (vargas2023themechanismsand pages 1-6): Jose Norberto S. Vargas, Maho Hamasaki, Tsuyoshi Kawabata, Richard J. Youle, and Tamotsu Yoshimori. The mechanisms and roles of selective autophagy in mammals. Nature Reviews Molecular Cell Biology, 24:167-185, Oct 2023. URL: https://doi.org/10.1038/s41580-022-00542-2, doi:10.1038/s41580-022-00542-2. This article has 1079 citations and is from a domain leading peer-reviewed journal.

4. (rasmussen2022nbr1thearchetypal pages 6-8): Nikoline Lander Rasmussen, Athanasios Kournoutis, Trond Lamark, and Terje Johansen. Nbr1: the archetypal selective autophagy receptor. The Journal of Cell Biology, Oct 2022. URL: https://doi.org/10.1083/jcb.202208092, doi:10.1083/jcb.202208092. This article has 110 citations.

5. (cerdatroncoso2021protumoralfunctionsof pages 7-8): Cristóbal Cerda-Troncoso, Manuel Varas-Godoy, and Patricia V. Burgos. Pro-tumoral functions of autophagy receptors in the modulation of cancer progression. Frontiers in Oncology, Feb 2021. URL: https://doi.org/10.3389/fonc.2020.619727, doi:10.3389/fonc.2020.619727. This article has 19 citations.

6. (rasmussen2022nbr1thearchetypal pages 2-4): Nikoline Lander Rasmussen, Athanasios Kournoutis, Trond Lamark, and Terje Johansen. Nbr1: the archetypal selective autophagy receptor. The Journal of Cell Biology, Oct 2022. URL: https://doi.org/10.1083/jcb.202208092, doi:10.1083/jcb.202208092. This article has 110 citations.

7. (rasmussen2022nbr1thearchetypal pages 10-11): Nikoline Lander Rasmussen, Athanasios Kournoutis, Trond Lamark, and Terje Johansen. Nbr1: the archetypal selective autophagy receptor. The Journal of Cell Biology, Oct 2022. URL: https://doi.org/10.1083/jcb.202208092, doi:10.1083/jcb.202208092. This article has 110 citations.

8. (rasmussen2022nbr1thearchetypal media 2c6d1299): Nikoline Lander Rasmussen, Athanasios Kournoutis, Trond Lamark, and Terje Johansen. Nbr1: the archetypal selective autophagy receptor. The Journal of Cell Biology, Oct 2022. URL: https://doi.org/10.1083/jcb.202208092, doi:10.1083/jcb.202208092. This article has 110 citations.

9. (north2025thelc3interactingregion pages 1-4): Brian J North, Amelia E Ohnstad, Michael J Ragusa, and Christopher J Shoemaker. The lc3-interacting region of nbr1 is a protein interaction hub enabling optimal flux. bioRxiv, May 2025. URL: https://doi.org/10.1101/2024.05.09.593318, doi:10.1101/2024.05.09.593318. This article has 9 citations.

10. (song2024selectiveautophagyreceptor pages 8-10): Honghai Song, Yutao Zhu, Chuan Hu, Qianyu Liu, Yang Jin, Pan Tang, Jiechao Xia, Dingqi Xie, Sicheng Jiang, Geliang Yao, Zhili Liu, and Zhijun Hu. Selective autophagy receptor nbr1 retards nucleus pulposus cell senescence by directing the clearance of srbd1. International Journal of Biological Sciences, 20:701-717, Jan 2024. URL: https://doi.org/10.7150/ijbs.90186, doi:10.7150/ijbs.90186. This article has 17 citations and is from a peer-reviewed journal.

11. (song2024selectiveautophagyreceptor pages 1-2): Honghai Song, Yutao Zhu, Chuan Hu, Qianyu Liu, Yang Jin, Pan Tang, Jiechao Xia, Dingqi Xie, Sicheng Jiang, Geliang Yao, Zhili Liu, and Zhijun Hu. Selective autophagy receptor nbr1 retards nucleus pulposus cell senescence by directing the clearance of srbd1. International Journal of Biological Sciences, 20:701-717, Jan 2024. URL: https://doi.org/10.7150/ijbs.90186, doi:10.7150/ijbs.90186. This article has 17 citations and is from a peer-reviewed journal.

12. (song2024selectiveautophagyreceptor pages 5-8): Honghai Song, Yutao Zhu, Chuan Hu, Qianyu Liu, Yang Jin, Pan Tang, Jiechao Xia, Dingqi Xie, Sicheng Jiang, Geliang Yao, Zhili Liu, and Zhijun Hu. Selective autophagy receptor nbr1 retards nucleus pulposus cell senescence by directing the clearance of srbd1. International Journal of Biological Sciences, 20:701-717, Jan 2024. URL: https://doi.org/10.7150/ijbs.90186, doi:10.7150/ijbs.90186. This article has 17 citations and is from a peer-reviewed journal.

13. (pinobelmar2024anintrinsichost pages 6-8): Camila Pino-Belmar, Rayén Aguilar, Guillermo E. Valenzuela-Nieto, Viviana A. Cavieres, Cristóbal Cerda-Troncoso, Valentina C. Navarrete, Paula Salazar, Patricia V. Burgos, Carola Otth, and Hianara A. Bustamante. An intrinsic host defense against hsv-1 relies on the activation of xenophagy with the active clearance of autophagic receptors. Cells, 13:1256, Jul 2024. URL: https://doi.org/10.3390/cells13151256, doi:10.3390/cells13151256. This article has 12 citations.

14. (pinobelmar2024anintrinsichost pages 8-10): Camila Pino-Belmar, Rayén Aguilar, Guillermo E. Valenzuela-Nieto, Viviana A. Cavieres, Cristóbal Cerda-Troncoso, Valentina C. Navarrete, Paula Salazar, Patricia V. Burgos, Carola Otth, and Hianara A. Bustamante. An intrinsic host defense against hsv-1 relies on the activation of xenophagy with the active clearance of autophagic receptors. Cells, 13:1256, Jul 2024. URL: https://doi.org/10.3390/cells13151256, doi:10.3390/cells13151256. This article has 12 citations.

15. (pinobelmar2024anintrinsichost pages 1-2): Camila Pino-Belmar, Rayén Aguilar, Guillermo E. Valenzuela-Nieto, Viviana A. Cavieres, Cristóbal Cerda-Troncoso, Valentina C. Navarrete, Paula Salazar, Patricia V. Burgos, Carola Otth, and Hianara A. Bustamante. An intrinsic host defense against hsv-1 relies on the activation of xenophagy with the active clearance of autophagic receptors. Cells, 13:1256, Jul 2024. URL: https://doi.org/10.3390/cells13151256, doi:10.3390/cells13151256. This article has 12 citations.

16. (rasmussen2022nbr1thearchetypal pages 11-12): Nikoline Lander Rasmussen, Athanasios Kournoutis, Trond Lamark, and Terje Johansen. Nbr1: the archetypal selective autophagy receptor. The Journal of Cell Biology, Oct 2022. URL: https://doi.org/10.1083/jcb.202208092, doi:10.1083/jcb.202208092. This article has 110 citations.

17. (cerdatroncoso2021protumoralfunctionsof pages 6-7): Cristóbal Cerda-Troncoso, Manuel Varas-Godoy, and Patricia V. Burgos. Pro-tumoral functions of autophagy receptors in the modulation of cancer progression. Frontiers in Oncology, Feb 2021. URL: https://doi.org/10.3389/fonc.2020.619727, doi:10.3389/fonc.2020.619727. This article has 19 citations.

18. (trapannone2023p62andnbr1 pages 7-9): Riccardo Trapannone, Julia Romanov, and Sascha Martens. P62 and nbr1 functions are dispensable for aggrephagy in mouse escs and esc-derived neurons. Life Science Alliance, 6:e202301936, Aug 2023. URL: https://doi.org/10.26508/lsa.202301936, doi:10.26508/lsa.202301936. This article has 6 citations and is from a peer-reviewed journal.

19. (OpenTargets Search: -NBR1): Open Targets Query (-NBR1, 13 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.

20. (rasmussen2022nbr1thearchetypal media 47b06603): Nikoline Lander Rasmussen, Athanasios Kournoutis, Trond Lamark, and Terje Johansen. Nbr1: the archetypal selective autophagy receptor. The Journal of Cell Biology, Oct 2022. URL: https://doi.org/10.1083/jcb.202208092, doi:10.1083/jcb.202208092. This article has 110 citations.

21. (rasmussen2022nbr1thearchetypal media 07b5ca64): Nikoline Lander Rasmussen, Athanasios Kournoutis, Trond Lamark, and Terje Johansen. Nbr1: the archetypal selective autophagy receptor. The Journal of Cell Biology, Oct 2022. URL: https://doi.org/10.1083/jcb.202208092, doi:10.1083/jcb.202208092. This article has 110 citations.

22. (trapannone2023p62andnbr1 pages 9-12): Riccardo Trapannone, Julia Romanov, and Sascha Martens. P62 and nbr1 functions are dispensable for aggrephagy in mouse escs and esc-derived neurons. Life Science Alliance, 6:e202301936, Aug 2023. URL: https://doi.org/10.26508/lsa.202301936, doi:10.26508/lsa.202301936. This article has 6 citations and is from a peer-reviewed journal.

23. (pinobelmar2024anintrinsichost pages 2-3): Camila Pino-Belmar, Rayén Aguilar, Guillermo E. Valenzuela-Nieto, Viviana A. Cavieres, Cristóbal Cerda-Troncoso, Valentina C. Navarrete, Paula Salazar, Patricia V. Burgos, Carola Otth, and Hianara A. Bustamante. An intrinsic host defense against hsv-1 relies on the activation of xenophagy with the active clearance of autophagic receptors. Cells, 13:1256, Jul 2024. URL: https://doi.org/10.3390/cells13151256, doi:10.3390/cells13151256. This article has 12 citations.

24. (rasmussen2022nbr1thearchetypal pages 8-10): Nikoline Lander Rasmussen, Athanasios Kournoutis, Trond Lamark, and Terje Johansen. Nbr1: the archetypal selective autophagy receptor. The Journal of Cell Biology, Oct 2022. URL: https://doi.org/10.1083/jcb.202208092, doi:10.1083/jcb.202208092. This article has 110 citations.

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Citations

1. vargas2023themechanismsand pages 1-6
2. song2024selectiveautophagyreceptor pages 8-10
3. song2024selectiveautophagyreceptor pages 1-2
4. song2024selectiveautophagyreceptor pages 5-8
5. pinobelmar2024anintrinsichost pages 6-8
6. pinobelmar2024anintrinsichost pages 8-10
7. cerdatroncoso2021protumoralfunctionsof pages 6-7
8. cerdatroncoso2021protumoralfunctionsof pages 7-8
9. pinobelmar2024anintrinsichost pages 1-2
10. pinobelmar2024anintrinsichost pages 2-3
11. https://doi.org/10.1083/jcb.202208092
12. https://doi.org/10.3389/fonc.2020.619727
13. https://doi.org/10.1101/2024.05.09.593318
14. https://doi.org/10.1038/s41580-022-00542-2
15. https://doi.org/10.26508/lsa.202301936
16. https://doi.org/10.3390/cells13151256
17. https://doi.org/10.7150/ijbs.90186
18. https://doi.org/10.1083/jcb.202208092,
19. https://doi.org/10.1038/s41580-022-00542-2,
20. https://doi.org/10.3389/fonc.2020.619727,
21. https://doi.org/10.1101/2024.05.09.593318,
22. https://doi.org/10.7150/ijbs.90186,
23. https://doi.org/10.3390/cells13151256,
24. https://doi.org/10.26508/lsa.202301936,