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.

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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

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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 TMF1 (UniProt P82094) / TMF-1 / ARA160 (TATA element modulatory factor)

1) Gene/protein identity verification and nomenclature

Human TMF1 encodes a ~160 kDa, ~1,093 amino-acid protein historically identified under multiple names, including TATA element modulatory factor (TMF) and androgen receptor-associated protein of 160 kDa (ARA160). ARA160 was cloned as an androgen receptor (AR) N-terminal–associated protein and was reported to be identical in sequence to TMF (a factor previously described in the context of TATA element modulation), thereby linking the gene symbol TMF1 to the protein described in UniProt accession P82094 (Hsiao & Chang, 1999; publication date Aug 1999; https://doi.org/10.1074/jbc.274.32.22373) (hsiao1999isolationandcharacterization pages 1-1).

2) Key concepts/definitions and current understanding of TMF1 function

2.1 TMF1 as a Golgi-associated golgin and Rab6 effector

A major validated concept is that TMF1/ARA160 is a Golgi-associated coiled-coil “golgin” that binds Rab6 family GTPases and contributes to Golgi organization. Fridmann-Sirkis et al. (May 2004; https://doi.org/10.1186/1471-2121-5-18) localized TMF to the Golgi by immunofluorescence and biochemical fractionation, and showed that a C-terminal fragment of TMF localizes to the Golgi and binds Rab6, consistent with the notion that Rab6 recruits this golgin (fridmannsirkis2004tmfisa pages 5-7). Functionally, partial TMF depletion by RNAi correlated with Golgi dispersal, supporting an architectural role in maintaining compact Golgi organization (fridmannsirkis2004tmfisa pages 5-7).

Yamane et al. (Oct 2007; https://doi.org/10.1016/j.yexcr.2007.07.010) extended this to trafficking function: TMF localized around Rab6-positive Golgi structures and, by immuno-EM, concentrated near budding structures of Golgi cisternae. TMF knockdown (and Rab6 perturbation) disrupted Rab6-dependent retrograde traffic, including endosome→TGN transport of Shiga toxin and aspects of Golgi→ER recycling, and affected Golgi retention of specific resident enzymes such as GalNAc-T2 (yamane2007functionalinvolvementof pages 1-2).

Definition (functional): In mammalian cells, TMF1 is best supported as a Golgi tether/scaffold (golgin) and Rab6 effector that contributes to Golgi ribbon morphology and to specific retrograde trafficking pathways (fridmannsirkis2004tmfisa pages 5-7, yamane2007functionalinvolvementof pages 1-2).

2.2 TMF1 as a nuclear receptor coactivator (ARA160)

TMF1/ARA160 was originally cloned as the first reported AR N-terminal–associated coactivator in prostate cells. Hsiao & Chang (Aug 1999; https://doi.org/10.1074/jbc.274.32.22373) demonstrated direct AR–ARA160 binding using far-Western, pull-down, co-immunoprecipitation, and mammalian two-hybrid assays, and showed functional coactivation in androgen-dependent reporter systems (hsiao1999isolationandcharacterization pages 1-1, hsiao1999isolationandcharacterization pages 3-3). Interaction mapping supported engagement with the AR N-terminal/AF-1 region and an internal ARA160 region (e.g., ARA160 aa 410–888 used in binding assays) (hsiao1999isolationandcharacterization pages 1-3, hsiao1999isolationandcharacterization pages 3-3). ARA160 enhanced AR transactivation and could synergize with another AR coactivator (ARA70), consistent with coactivator network behavior (hsiao1999isolationandcharacterization pages 4-5).

Definition (functional): TMF1 can function as an AR coactivator in transcriptional reporter contexts, with ligand-enhanced AR–TMF/ARA160 interaction and mapped preference for AR AF-1 (hsiao1999isolationandcharacterization pages 4-5, hsiao1999isolationandcharacterization pages 3-3).

2.3 TMF1 as a BC-box protein coupling signaling to proteasomal degradation

Another central concept is that TMF1/ARA160 contains a BC-box motif capable of binding elongin C (an adaptor module often used in Cullin-based ubiquitin ligase complexes), enabling TMF1 to promote ubiquitination and proteasomal turnover of select targets.

Perry et al. (Nov 2004; https://doi.org/10.1038/sj.onc.1208149) described TMF/ARA160 as a Golgi-confined coiled-coil protein that can redistribute into the cytoplasm under serum starvation, associate with the non-receptor tyrosine kinase Fer and transcription factor STAT3, and promote STAT3 ubiquitination and proteasomal degradation in a BC-box–dependent manner (perry2004tmfara160isa pages 1-2, perry2004tmfara160isa pages 8-9). Proteasome inhibition (MG132) blocked TMF-induced STAT3/Fer loss, supporting a proteasome-dependent mechanism (perry2004tmfara160isa pages 8-9).

Abrham et al. (Jul 2009; https://doi.org/10.1002/ijc.24277) further linked TMF to stress-conditional proteostasis control in cancer models: in PC3 xenografts, TMF expression correlated with lower abundance of NF-κB p65/RelA and downregulation of proangiogenic cytokines (e.g., IL-8, IL-1β), consistent with TMF-mediated suppression of NF-κB–dependent proangiogenic programs under metabolic constraints (abrham2009tmfara160downregulatesproangiogenic pages 1-2, abrham2009tmfara160downregulatesproangiogenic pages 7-8).

Definition (functional): TMF1 can act as a BC-box–dependent regulator of protein stability, linking signaling/stress states to selective ubiquitin-proteasome control of factors such as STAT3 and (in stressed tumor settings) NF-κB p65/RelA (perry2004tmfara160isa pages 8-9, abrham2009tmfara160downregulatesproangiogenic pages 7-8).

2.4 TMF1 in nuclear receptor tyrosine kinase (RTK) trafficking and chromatin remodeling

A modern mechanistic axis connecting TMF1 to nuclear signaling is the PDGFRβ–Fer–TMF-1–Brg-1 pathway.

Papadopoulos et al. (May 2018; https://doi.org/10.1083/jcb.201706118) showed that PDGF-BB stimulation causes a fraction of full-length PDGFRβ to accumulate in the nucleus (chromatin and nuclear matrix), where it forms ligand-inducible complexes with Fer and TMF-1 (papadopoulos2018pdgfrβtranslocatesto pages 1-2, papadopoulos2018pdgfrβtranslocatesto pages 9-11). PDGF-BB stimulation decreased TMF-1 association with Brg-1 and released Brg-1 from the SWI–SNF chromatin remodeling complex, linking RTK nuclear trafficking to chromatin remodeling (papadopoulos2018pdgfrβtranslocatesto pages 1-2). TMF-1 knockdown reduced PDGFRβ nuclear translocation and increased expression of the cell cycle inhibitor CDKN1A (p21), while immediate-early PDGFRβ responses were largely unaffected—supporting a selective chromatin-mediated proliferation control route (papadopoulos2018pdgfrβtranslocatesto pages 1-2, papadopoulos2018pdgfrβtranslocatesto pages 7-8).

A 2024 review on RTK signaling in neurodegenerative contexts explicitly cites this mechanism—“PDGFRβ translocates to the nucleus and regulates chromatin remodeling via TATA element–modifying factor 1”—placing TMF1 within an ongoing shift in RTK biology toward nuclear functions and chromatin regulation (Feb 2024; https://doi.org/10.37349/en.2024.00033) (sengupta2024connectingtheends pages 21-23).

Definition (functional): TMF1 functions as a cofactor/trafficking-linked regulator of nuclear PDGFRβ signaling, impacting SWI–SNF chromatin remodeling (via Brg-1) and cell-cycle control genes such as p21 (papadopoulos2018pdgfrβtranslocatesto pages 1-2, papadopoulos2018pdgfrβtranslocatesto pages 7-8, sengupta2024connectingtheends pages 21-23).

3) Domain architecture and subcellular localization

Subcellular localization is context-dependent, with strong evidence for Golgi association but also documented nuclear/cytoplasmic roles.

• Golgi localization: TMF localizes to Golgi membranes by immunofluorescence and Golgi fractionation and exhibits a characteristic Golgi “ring” pattern; a C-terminal fragment is sufficient for Golgi localization and Rab6-dependent recruitment (fridmannsirkis2004tmfisa pages 5-7). TMF also surrounds Rab6-positive Golgi structures and is observed at budding regions by immuno-EM (yamane2007functionalinvolvementof pages 1-2).
• Cytoplasmic redistribution under stress: In serum-starved myoblasts, TMF redistributes from Golgi to the cytoplasm and associates with Fer/STAT3 in a proteasome-regulated complex (perry2004tmfara160isa pages 8-9).
• Nuclear functions/associations: TMF-1 is found in nuclear complexes with PDGFRβ/Fer and is implicated in chromatin remodeling via Brg-1 (papadopoulos2018pdgfrβtranslocatesto pages 1-2, papadopoulos2018pdgfrβtranslocatesto pages 9-11).

Structural motifs (functionally inferred/validated):
* Coiled-coil architecture: TMF is described as a coiled-coil rich protein consistent with golgin family features (perry2004tmfara160isa pages 1-2, fridmannsirkis2004tmfisa pages 5-7).
* C-terminal Rab6-binding region: Experiments localize Rab6 interaction/Golgi targeting to the C-terminal region (fridmannsirkis2004tmfisa pages 5-7).
* BC-box motif: Required for elongin C binding and for STAT3 degradation activity (perry2004tmfara160isa pages 1-2, perry2004tmfara160isa pages 8-9).
* Microtubule-interacting domain (MIT) (shown in mouse TMF): A C-terminal MIT domain plus coiled-coil regions are required for stable Golgi association and microtubule binding in spermatogenic contexts, supporting cytoskeletal coupling of Golgi behavior (elkis2015tmfara160governsthe pages 11-13, elkis2015tmfara160governsthe pages 15-17).

4) Biological roles and pathways (experimentally supported)

4.1 Golgi organization and retrograde membrane traffic (Rab6 pathway)

TMF1 is implicated in maintaining compact Golgi organization and in Rab6-dependent retrograde trafficking. In NRK cells, TMF RNAi correlated with loss of a compact Golgi ribbon: 58% of cells with normal TMF levels exhibited a compact Golgi versus 8% of TMF-depleted cells (Fridmann-Sirkis et al., 2004; Fig. 4C image evidence) (fridmannsirkis2004tmfisa pages 5-7, fridmannsirkis2004tmfisa media a620ef8a). TMF knockdown also disrupted Shiga toxin retrograde routing to the TGN and altered retention of select Golgi enzymes (GalNAc-T2) (yamane2007functionalinvolvementof pages 1-2).

4.2 AR transcriptional coactivation (steroid receptor signaling)

ARA160/TMF interacts with AR (ligand enhanced) and augments AR transcriptional output in prostate cell reporter assays, with stronger enhancement of AR AF-1 activity than AF-2 in mapping experiments. Reporter outcomes include DHT-induced transactivation increased from approximately 5-fold to ~17-fold with ARA160 coexpression in one assay configuration (hsiao1999isolationandcharacterization pages 3-3). These data support a role for TMF1 as a transcriptional cofactor in steroid receptor signaling contexts (hsiao1999isolationandcharacterization pages 4-5, hsiao1999isolationandcharacterization pages 3-3).

4.3 Proteostasis control of STAT3 and NF-κB under growth arrest/metabolic stress

Under serum deprivation, TMF associates with Fer and STAT3 and promotes STAT3 ubiquitination and proteasomal degradation in a BC-box–dependent manner; MG132 blocks this loss (perry2004tmfara160isa pages 8-9). In tumor contexts where metabolic stress is expected, TMF expression correlated with reduced NF-κB p65/RelA (~2-fold in xenograft tumors) and downregulation of NF-κB–regulated proangiogenic cytokines (IL-8, IL-1β) (abrham2009tmfara160downregulatesproangiogenic pages 5-7, abrham2009tmfara160downregulatesproangiogenic pages 7-8).

4.4 Nuclear PDGFRβ signaling to chromatin remodeling and cell-cycle control

Papadopoulos et al. provide direct quantification of PDGFRβ nuclear trafficking: nuclear PDGFRβ increased from ~7% of total receptor (basal) to a peak of ~26% at 30 minutes after PDGF-BB stimulation (papadopoulos2018pdgfrβtranslocatesto pages 2-4). They also quantified plasma-membrane–derived (biotinylated) PDGFRβ clusters colocalizing with TMF-1 in Golgi and nucleus (e.g., ~13 Golgi clusters and ~14 nuclear clusters per cell; n=29; and ~2.5 vs ~2.4 triple-positive dots per cell using a Pearson cutoff) (papadopoulos2018pdgfrβtranslocatesto pages 4-5). Functionally, Fer/TMF-1/Brg-1 depletion increased the fraction of p21-positive cells (control 6.5% vs 21% Fer KD, 25% TMF-1 KD, 50% Brg-1 KD), and impaired PDGF-driven proliferation (papadopoulos2018pdgfrβtranslocatesto pages 7-8). These findings support an expert-level mechanistic model in which TMF-1-positive trafficking routes contribute to nuclear receptor delivery and to chromatin remodeling events that modulate p53/p21-linked proliferation control (papadopoulos2018pdgfrβtranslocatesto pages 1-2, papadopoulos2018pdgfrβtranslocatesto pages 7-8).

4.5 Spermiogenesis and Golgi orientation (in vivo developmental cell biology)

In TMF knockout mice, TMF is required for correct Golgi spatial orientation in developing spermatids and for pro-acrosomal vesicle targeting to the nucleus during acrosome formation. TMF displays dynamic localization across Golgi regions during spermiogenesis. The work supports TMF as a Golgi- and microtubule-associated factor: TMF co-immunoprecipitates with tubulin and associates with polymerized microtubules; disrupting microtubules (colchicine) disrupts Golgi association of TMF constructs. A C-terminal MIT domain and coiled-coil regions are required for stable TMF association with Golgi in NIH3T3 mapping experiments (Dec 2015; https://doi.org/10.1371/journal.pone.0145277) (elkis2015tmfara160governsthe pages 11-13, elkis2015tmfara160governsthe pages 15-17).

4.6 Mucus secretion, mucus barrier function, microbiota composition, and colitis susceptibility

In the colon, TMF is linked to regulated secretion of the major gel-forming mucin MUC2, and to downstream ecological effects on microbiota. Bel et al. (Mar 2014; https://doi.org/10.1073/pnas.1319114111) showed that TMF−/− goblet cells display altered secretory granule behavior by TEM (granules “do not fuse before mucus secretion” and are discharged late), consistent with a vesicle fusion/tethering defect affecting mucus granule exocytosis (bel2014reprogrammedandtransmissible pages 4-5). TMF colocalized with MUC2 in human colonic goblet cells by immunofluorescence (bel2014reprogrammedandtransmissible pages 2-3). Biochemically, mucus from TMF−/− mice contained highly oligomerized MUC2 that resisted natural degradation: under nonreducing conditions WT MUC2 appeared as a smear (degraded) whereas TMF−/− MUC2 appeared as an undegraded high–molecular-weight species (bel2014reprogrammedandtransmissible pages 2-3).

Phenotypically, TMF−/− mice had altered microbiota (higher diversity; shifts toward Firmicutes taxa described as beneficial) and showed reduced susceptibility to DSS-induced colitis; the protective microbiota was transmissible to WT mice by cohousing, and DSS outcomes (weight loss, fecal/histopathology scoring, cytokine mRNAs) showed significant differences (p<0.05; n=5 in reported DSS experiments) (bel2014reprogrammedandtransmissible pages 4-5, bel2014reprogrammedandtransmissible pages 4-4).

5) Disease relevance, real-world applications, and implementations

5.1 Cancer biology: antiangiogenic activity in prostate xenografts

In vivo, ectopic TMF expression in PC3 xenografts attenuated tumor progression, associated with reduced angiogenesis and increased apoptotic markers (activated caspase-3, TUNEL), while proliferation markers (PCNA) were not changed—supporting a model where TMF influences tumor microenvironment (angiogenesis) and stress-driven survival rather than baseline proliferation (Jul 2009; https://doi.org/10.1002/ijc.24277) (abrham2009tmfara160downregulatesproangiogenic pages 5-7). Vessel mass reduction was supported by CD31 staining with reported significance (p<0.04, n=6) (abrham2009tmfara160downregulatesproangiogenic pages 5-7). This suggests TMF1-related pathways may be relevant for interpreting tumor stress responses and angiogenic transcription programs involving NF-κB/STAT3, though clinical translation remains investigational in the cited record.

5.2 Reproductive health and infertility associations

Mechanistic mouse studies demonstrate TMF’s necessity for normal spermiogenesis and acrosome formation (elkis2015tmfara160governsthe pages 9-11, elkis2015tmfara160governsthe pages 11-13). Consistent with this biology, Open Targets lists TMF1 disease associations enriched in male infertility-related phenotypes (e.g., azoospermia and spermatogenic failure terms) with multiple literature evidence links (evidence count=5 in the returned Open Targets results for each listed disease) (OpenTargets Search: -TMF1). These database associations should be interpreted as curated linkage signals rather than mechanistic proof, but they align with in vivo functional roles in male germ cell development.

5.3 Systems/cell biology implementations

TMF1 is used in real-world research implementations as:
* A Golgi scaffold/tether perturbation target (RNAi/siRNA or knockout) to assay Golgi ribbon morphology and retrograde traffic pathways (fridmannsirkis2004tmfisa pages 5-7, yamane2007functionalinvolvementof pages 1-2).
* A component in nuclear RTK trafficking studies leveraging surface biotinylation, colocalization pipelines, and chromatin fractionation (papadopoulos2018pdgfrβtranslocatesto pages 4-5, papadopoulos2018pdgfrβtranslocatesto pages 2-4).
* A regulator of mucus barrier biology and microbiome transmissibility studies using cohousing paradigms and DSS colitis induction (bel2014reprogrammedandtransmissible pages 4-4).

6) Expert synthesis and analysis (integrating the evidence)

The literature supports TMF1 as a multifunctional, localization-flexible scaffold that links membrane trafficking architecture to signal-dependent transcriptional control.

1. Primary/most reproducible cellular role: The Golgi/tethering axis is supported by multiple cell biological methods (Golgi localization, Rab6-binding, trafficking defects, Golgi morphology quantification). These findings converge on TMF1 acting as a Rab6 effector/golgin mediating aspects of retrograde trafficking and maintaining Golgi compactness (fridmannsirkis2004tmfisa pages 5-7, yamane2007functionalinvolvementof pages 1-2).

2. Conditional regulatory role in proteostasis: TMF1’s BC-box-dependent proteasome coupling appears to become prominent under growth arrest or metabolic stress, consistent with its cytoplasmic redistribution under serum starvation and xenograft-specific effects absent in standard culture (perry2004tmfara160isa pages 8-9, abrham2009tmfara160downregulatesproangiogenic pages 8-10). This conditionality is important for functional annotation: TMF1 is not a constitutive E3 ligase, but rather an adaptor-like factor whose activity depends on cellular state.

3. Emerging nuclear signaling integration: The PDGFRβ nuclear trafficking/chromatin axis provides a mechanistic bridge between TMF1’s trafficking identity and transcriptional outcomes, and has been highlighted in recent (2024) synthesis of RTK nuclear functions (papadopoulos2018pdgfrβtranslocatesto pages 4-5, papadopoulos2018pdgfrβtranslocatesto pages 7-8, sengupta2024connectingtheends pages 21-23).

4. Physiological specialization: TMF1’s roles in spermiogenesis and in goblet cell mucin secretion indicate it contributes to specialized secretory processes requiring oriented Golgi dynamics and regulated granule fusion (elkis2015tmfara160governsthe pages 9-11, bel2014reprogrammedandtransmissible pages 4-5).

7) Quantitative highlights (selected)

• Golgi morphology: compact Golgi in 58% of TMF-normal cells vs 8% of TMF-reduced cells after RNAi (Fridmann-Sirkis et al., 2004; Fig. 4C) (fridmannsirkis2004tmfisa media a620ef8a).
• Nuclear PDGFRβ: ~7% basal → ~26% at 30 min after PDGF-BB (Papadopoulos et al., 2018) (papadopoulos2018pdgfrβtranslocatesto pages 2-4).
• Nuclear PDGFRβ/TMF-1 trafficking quantification: ~13 Golgi and 14 nuclear biotinylated PDGFRβ clusters per cell; ~2.5 (Golgi) and 2.4 (nucleus) triple-positive dots per cell (Pearson >0.2; n=29) (papadopoulos2018pdgfrβtranslocatesto pages 4-5).
• p21-positive cells after knockdown: control 6.5% vs 21% (Fer KD), 25% (TMF-1 KD), 50% (Brg-1 KD) (Papadopoulos et al., 2018) (papadopoulos2018pdgfrβtranslocatesto pages 7-8).
• PC3 xenografts: group size n=8 per group; reduced CD31 vessel mass with p<0.04 (n=6); IL-8 and IL-1β reduced across three independent xenografts (Abrham et al., 2009) (abrham2009tmfara160downregulatesproangiogenic pages 5-7, abrham2009tmfara160downregulatesproangiogenic pages 3-5).
• DSS colitis: 3% DSS, with significant outcomes (p<0.05) and n=5 in reported experiments; transmissible microbiota protective effect after 4 weeks cohousing (Bel et al., 2014) (bel2014reprogrammedandtransmissible pages 4-4).

8) Summary table (evidence-grounded)

The following table consolidates the validated functional areas, partners, evidence types, quantitative highlights, and DOI links.

Table: This table summarizes experimentally validated functions of human TMF1/P82094 across trafficking, nuclear signaling, proteostasis, reproduction, mucosal biology, and cancer. It highlights key partners, assay types, quantitative findings, and the primary supporting papers with DOI links.

9) Notes on evidence gaps and 2023–2024 coverage

Within the retrieved corpus, TMF1-specific mechanistic advances in 2023–2024 were limited; however, a 2024 review explicitly positions TMF1 in the contemporary framework of nuclear RTK signaling/chromatin remodeling (sengupta2024connectingtheends pages 21-23). Most definitive mechanistic and in vivo functional studies currently available here span 1999–2018 (AR coactivation; Rab6/golgin trafficking; BC-box proteostasis; PDGFRβ nuclear chromatin axis) plus strong in vivo phenotypes in 2014–2015 (mucus secretion/microbiome; spermiogenesis) (hsiao1999isolationandcharacterization pages 3-3, yamane2007functionalinvolvementof pages 1-2, perry2004tmfara160isa pages 8-9, papadopoulos2018pdgfrβtranslocatesto pages 1-2, bel2014reprogrammedandtransmissible pages 2-3, elkis2015tmfara160governsthe pages 11-13).

References

1. (hsiao1999isolationandcharacterization pages 1-1): Pei-Wen Hsiao and Chawnshang Chang. Isolation and characterization of ara160 as the first androgen receptor n-terminal-associated coactivator in human prostate cells*. The Journal of Biological Chemistry, 274:22373-22379, Aug 1999. URL: https://doi.org/10.1074/jbc.274.32.22373, doi:10.1074/jbc.274.32.22373. This article has 180 citations.

2. (fridmannsirkis2004tmfisa pages 5-7): Yael Fridmann-Sirkis, Symeon Siniossoglou, and Hugh RB Pelham. Tmf is a golgin that binds rab6 and influences golgi morphology. BMC Cell Biology, 5:18-18, May 2004. URL: https://doi.org/10.1186/1471-2121-5-18, doi:10.1186/1471-2121-5-18. This article has 119 citations.

3. (yamane2007functionalinvolvementof pages 1-2): Junko Yamane, Akiharu Kubo, Kazuhisa Nakayama, Akiko Yuba-Kubo, Tatsuya Katsuno, Shoichiro Tsukita, and Sachiko Tsukita. Functional involvement of tmf/ara160 in rab6-dependent retrograde membrane traffic. Experimental cell research, 313 16:3472-85, Oct 2007. URL: https://doi.org/10.1016/j.yexcr.2007.07.010, doi:10.1016/j.yexcr.2007.07.010. This article has 79 citations and is from a peer-reviewed journal.

4. (hsiao1999isolationandcharacterization pages 3-3): Pei-Wen Hsiao and Chawnshang Chang. Isolation and characterization of ara160 as the first androgen receptor n-terminal-associated coactivator in human prostate cells*. The Journal of Biological Chemistry, 274:22373-22379, Aug 1999. URL: https://doi.org/10.1074/jbc.274.32.22373, doi:10.1074/jbc.274.32.22373. This article has 180 citations.

5. (hsiao1999isolationandcharacterization pages 1-3): Pei-Wen Hsiao and Chawnshang Chang. Isolation and characterization of ara160 as the first androgen receptor n-terminal-associated coactivator in human prostate cells*. The Journal of Biological Chemistry, 274:22373-22379, Aug 1999. URL: https://doi.org/10.1074/jbc.274.32.22373, doi:10.1074/jbc.274.32.22373. This article has 180 citations.

6. (hsiao1999isolationandcharacterization pages 4-5): Pei-Wen Hsiao and Chawnshang Chang. Isolation and characterization of ara160 as the first androgen receptor n-terminal-associated coactivator in human prostate cells*. The Journal of Biological Chemistry, 274:22373-22379, Aug 1999. URL: https://doi.org/10.1074/jbc.274.32.22373, doi:10.1074/jbc.274.32.22373. This article has 180 citations.

7. (perry2004tmfara160isa pages 1-2): Erez Perry, Rachel Tsruya, Pavel Levitsky, Oz Pomp, Michal Taller, Shira Weisberg, Wendy Parris, Sarang Kulkarni, Hana Malovani, Tony Pawson, Sally Shpungin, and Uri Nir. Tmf/ara160 is a bc-box-containing protein that mediates the degradation of stat3. Oncogene, 23:8908-8919, Nov 2004. URL: https://doi.org/10.1038/sj.onc.1208149, doi:10.1038/sj.onc.1208149. This article has 70 citations and is from a domain leading peer-reviewed journal.

8. (perry2004tmfara160isa pages 8-9): Erez Perry, Rachel Tsruya, Pavel Levitsky, Oz Pomp, Michal Taller, Shira Weisberg, Wendy Parris, Sarang Kulkarni, Hana Malovani, Tony Pawson, Sally Shpungin, and Uri Nir. Tmf/ara160 is a bc-box-containing protein that mediates the degradation of stat3. Oncogene, 23:8908-8919, Nov 2004. URL: https://doi.org/10.1038/sj.onc.1208149, doi:10.1038/sj.onc.1208149. This article has 70 citations and is from a domain leading peer-reviewed journal.

9. (abrham2009tmfara160downregulatesproangiogenic pages 1-2): Galya Abrham, Marina Volpe, Sally Shpungin, and Uri Nir. Tmf/ara160 downregulates proangiogenic genes and attenuates the progression of pc3 xenografts. International Journal of Cancer, 125:43-53, Jul 2009. URL: https://doi.org/10.1002/ijc.24277, doi:10.1002/ijc.24277. This article has 24 citations and is from a domain leading peer-reviewed journal.

10. (abrham2009tmfara160downregulatesproangiogenic pages 7-8): Galya Abrham, Marina Volpe, Sally Shpungin, and Uri Nir. Tmf/ara160 downregulates proangiogenic genes and attenuates the progression of pc3 xenografts. International Journal of Cancer, 125:43-53, Jul 2009. URL: https://doi.org/10.1002/ijc.24277, doi:10.1002/ijc.24277. This article has 24 citations and is from a domain leading peer-reviewed journal.

11. (papadopoulos2018pdgfrβtranslocatesto pages 1-2): Natalia Papadopoulos, Johan Lennartsson, and Carl-Henrik Heldin. Pdgfrβ translocates to the nucleus and regulates chromatin remodeling via tata element–modifying factor 1. The Journal of Cell Biology, 217:1701-1717, May 2018. URL: https://doi.org/10.1083/jcb.201706118, doi:10.1083/jcb.201706118. This article has 35 citations.

12. (papadopoulos2018pdgfrβtranslocatesto pages 9-11): Natalia Papadopoulos, Johan Lennartsson, and Carl-Henrik Heldin. Pdgfrβ translocates to the nucleus and regulates chromatin remodeling via tata element–modifying factor 1. The Journal of Cell Biology, 217:1701-1717, May 2018. URL: https://doi.org/10.1083/jcb.201706118, doi:10.1083/jcb.201706118. This article has 35 citations.

13. (papadopoulos2018pdgfrβtranslocatesto pages 7-8): Natalia Papadopoulos, Johan Lennartsson, and Carl-Henrik Heldin. Pdgfrβ translocates to the nucleus and regulates chromatin remodeling via tata element–modifying factor 1. The Journal of Cell Biology, 217:1701-1717, May 2018. URL: https://doi.org/10.1083/jcb.201706118, doi:10.1083/jcb.201706118. This article has 35 citations.

14. (sengupta2024connectingtheends pages 21-23): Priyanka Sengupta, Russa Das, Piyali Majumder, and Debashis Mukhopadhyay. Connecting the ends: signaling via receptor tyrosine kinases and cytoskeletal degradation in neurodegeneration. Exploration of Neuroscience, 3:1-26, Feb 2024. URL: https://doi.org/10.37349/en.2024.00033, doi:10.37349/en.2024.00033. This article has 18 citations.

15. (elkis2015tmfara160governsthe pages 11-13): Yoav Elkis, Shai Bel, Roni Rahimi, Tali Lerer-Goldstein, Smadar Levin-Zaidman, Tatiana Babushkin, Sally Shpungin, and Uri Nir. Tmf/ara160 governs the dynamic spatial orientation of the golgi apparatus during sperm development. PLoS ONE, 10:e0145277, Dec 2015. URL: https://doi.org/10.1371/journal.pone.0145277, doi:10.1371/journal.pone.0145277. This article has 29 citations and is from a peer-reviewed journal.

16. (elkis2015tmfara160governsthe pages 15-17): Yoav Elkis, Shai Bel, Roni Rahimi, Tali Lerer-Goldstein, Smadar Levin-Zaidman, Tatiana Babushkin, Sally Shpungin, and Uri Nir. Tmf/ara160 governs the dynamic spatial orientation of the golgi apparatus during sperm development. PLoS ONE, 10:e0145277, Dec 2015. URL: https://doi.org/10.1371/journal.pone.0145277, doi:10.1371/journal.pone.0145277. This article has 29 citations and is from a peer-reviewed journal.

17. (fridmannsirkis2004tmfisa media a620ef8a): Yael Fridmann-Sirkis, Symeon Siniossoglou, and Hugh RB Pelham. Tmf is a golgin that binds rab6 and influences golgi morphology. BMC Cell Biology, 5:18-18, May 2004. URL: https://doi.org/10.1186/1471-2121-5-18, doi:10.1186/1471-2121-5-18. This article has 119 citations.

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31. (papadopoulos2018pdgfrβtranslocatesto pages 8-9): Natalia Papadopoulos, Johan Lennartsson, and Carl-Henrik Heldin. Pdgfrβ translocates to the nucleus and regulates chromatin remodeling via tata element–modifying factor 1. The Journal of Cell Biology, 217:1701-1717, May 2018. URL: https://doi.org/10.1083/jcb.201706118, doi:10.1083/jcb.201706118. This article has 35 citations.

32. (elkis2015tmfara160governsthe pages 17-18): Yoav Elkis, Shai Bel, Roni Rahimi, Tali Lerer-Goldstein, Smadar Levin-Zaidman, Tatiana Babushkin, Sally Shpungin, and Uri Nir. Tmf/ara160 governs the dynamic spatial orientation of the golgi apparatus during sperm development. PLoS ONE, 10:e0145277, Dec 2015. URL: https://doi.org/10.1371/journal.pone.0145277, doi:10.1371/journal.pone.0145277. This article has 29 citations and is from a peer-reviewed journal.

33. (bel2014reprogrammedandtransmissible pages 1-2): Shai Bel, Yoav Elkis, Hila Elifantz, Omry Koren, Rotem Ben-Hamo, Tal Lerer-Goldshtein, Roni Rahimi, Shomron Ben Horin, Abraham Nyska, Sally Shpungin, and Uri Nir. Reprogrammed and transmissible intestinal microbiota confer diminished susceptibility to induced colitis in tmf−/− mice. Proceedings of the National Academy of Sciences, 111:4964-4969, Mar 2014. URL: https://doi.org/10.1073/pnas.1319114111, doi:10.1073/pnas.1319114111. This article has 64 citations and is from a highest quality peer-reviewed journal.

34. (bel2014reprogrammedandtransmissible pages 3-4): Shai Bel, Yoav Elkis, Hila Elifantz, Omry Koren, Rotem Ben-Hamo, Tal Lerer-Goldshtein, Roni Rahimi, Shomron Ben Horin, Abraham Nyska, Sally Shpungin, and Uri Nir. Reprogrammed and transmissible intestinal microbiota confer diminished susceptibility to induced colitis in tmf−/− mice. Proceedings of the National Academy of Sciences, 111:4964-4969, Mar 2014. URL: https://doi.org/10.1073/pnas.1319114111, doi:10.1073/pnas.1319114111. This article has 64 citations and is from a highest quality peer-reviewed journal.

35. (bel2014reprogrammedandtransmissible pages 5-6): Shai Bel, Yoav Elkis, Hila Elifantz, Omry Koren, Rotem Ben-Hamo, Tal Lerer-Goldshtein, Roni Rahimi, Shomron Ben Horin, Abraham Nyska, Sally Shpungin, and Uri Nir. Reprogrammed and transmissible intestinal microbiota confer diminished susceptibility to induced colitis in tmf−/− mice. Proceedings of the National Academy of Sciences, 111:4964-4969, Mar 2014. URL: https://doi.org/10.1073/pnas.1319114111, doi:10.1073/pnas.1319114111. This article has 64 citations and is from a highest quality peer-reviewed journal.

36. (abrham2009tmfara160downregulatesproangiogenic pages 10-11): Galya Abrham, Marina Volpe, Sally Shpungin, and Uri Nir. Tmf/ara160 downregulates proangiogenic genes and attenuates the progression of pc3 xenografts. International Journal of Cancer, 125:43-53, Jul 2009. URL: https://doi.org/10.1002/ijc.24277, doi:10.1002/ijc.24277. This article has 24 citations and is from a domain leading peer-reviewed journal.

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