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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
Human CTDSP2 encodes carboxy-terminal-domain RNA polymerase II polypeptide A small phosphatase 2, commonly called SCP2, OS4, or NIF2. The supplied identity is correct: UniProt O14595 corresponds to human CTDSP2/SCP2, an FCP/SCP-family, HAD-like phosphoserine/threonine phosphatase, and not to the related genes CTDSP1, CTDSPL, CTDSPL2, or CTDNEP1. A curated phosphatase classification independently associates human CTDSP2/SCP2 with O14595 and chromosome 12q13–q15. (cohen2010phosphatasefamiliesdephosphorylating pages 14-15, rallabandi2020targetingthecterminal pages 3-5)
The best-supported molecular functions are: (1) Mg²⁺-dependent hydrolysis of phosphoserine-containing protein substrates through the conserved FCP-homology DXDX(T/V) catalytic machinery; (2) in-vitro dephosphorylation of the RNA polymerase II C-terminal domain (CTD), with SCP-family preference for pSer5 over pSer2; and (3) direct removal of activating C-terminal phosphate groups from Smad1, thereby terminating nuclear BMP signaling. Endogenous CTDSP2 is predominantly nuclear in the experimentally examined osteosarcoma cells. (cossa2021proteinphosphatasesin pages 6-7, knockaert2006uniqueplayersin pages 3-4, knockaert2006uniqueplayersin pages 4-5)
No substantive CTDSP2-specific mechanistic publication from 2023–2024 was identified in the searches. Consequently, the strongest annotation still rests on foundational primary studies from 2006 and 2015 and a 2021 authoritative review. A 2023 paper found during searching concerned CTDNEP1, a different phosphatase, and was excluded rather than transferred to CTDSP2.
| Topic | Best-supported conclusion | Evidence type/model | Confidence/caveat | Key source/date/DOI |
|---|---|---|---|---|
| Identity and aliases | Human CTDSP2 encodes small C-terminal-domain phosphatase 2 (SCP2), UniProt O14595; aliases include OS4 and NIF2. It is distinct from CTDSP1, CTDSPL/SCP3, CTDSPL2, and CTDNEP1. | Curated phosphatase classification plus human CTDSP2 literature | High. The CTDSPL2 nuclear-interactome study concerns a different paralog and is not transferable. | Cohen, Jan 2010, DOI; Rallabandi et al., May 2020, DOI (cohen2010phosphatasefamiliesdephosphorylating pages 14-15, rallabandi2020targetingthecterminal pages 3-5) |
| Family, domains, and structure | CTDSP2 is an FCP/SCP phosphoserine/threonine phosphatase in the HAD-like superfamily, characterized by the Mg²⁺-dependent DXDX(T/V) catalytic motif. Its experimental apo structure is PDB 2Q5E; CTDSP2 has a roughly 10-residue N-terminal insertion adjacent to the active site. | Family biochemistry, sequence/structure comparison, crystallographic entry | High for classification and PDB assignment; catalytic chemistry is strongly inferred from the conserved family mechanism rather than uniquely quantified for CTDSP2. CTDSP1, CTDSP2, and CTDSPL are highly conserved near the active site, complicating selective inhibitor design. | Rallabandi et al., May 2020, DOI (rallabandi2020targetingthecterminal pages 3-5) |
| RNAPII CTD substrate specificity | Purified human SCP-family enzymes dephosphorylate the RNA polymerase II CTD in vitro and prefer phospho-Ser5 over phospho-Ser2 within the heptad repeat. | In-vitro SCP-family assays summarized in an authoritative transcription review | Moderate for CTDSP2 specifically. The preference is reported for the SCP group—CTDSP1, CTDSP2, CTDSPL, and CTDSPL2—rather than established by modern CTDSP2-selective kinetics. SCP loss-of-function data do not support a major global transcription-cycle role. | Cossa et al., Apr 2021, DOI (cossa2021proteinphosphatasesin pages 6-7) |
| Smad1 substrate and BMP attenuation | CTDSP2/SCP2 binds Smad1 and removes its activating C-terminal phosphorylation, attenuating BMP–Smad1 signaling. Human SCP2 expression reduced endogenous phospho-Smad1 and BMP-responsive transcription in embryos; combined SCP1/SCP2 depletion increased the magnitude and duration of BMP-induced phospho-Smad1 in human cells. | Recombinant phosphatase assay; co-immunoprecipitation; Xenopus gain-of-function; siRNA loss-of-function in HaCaT, U2OS, and OsA-CL cells | High that CTDSP2 contributes, but some loss-of-function experiments depleted SCP1 and SCP2 together. Smad1 was strongly preferred over Smad2; this study addresses the Smad1 C-terminal SSXS region, not linker dephosphorylation. | Knockaert et al., Aug 8, 2006, DOI (knockaert2006uniqueplayersin pages 1-2, knockaert2006uniqueplayersin pages 2-3, knockaert2006uniqueplayersin pages 3-4, knockaert2006uniqueplayersin pages 4-5) |
| Nuclear localization and site of action | Endogenous CTDSP2 is localized mainly in the nucleus. Following BMP stimulation, CTDSP2 and Smad1 colocalize there; CTDSP2 does not prevent Smad1 nuclear import, supporting nuclear signal termination as its operative BMP role. | CTDSP2-specific antibody, immunoblotting, and immunofluorescence in OsA-CL osteosarcoma cells; siRNA loss of staining as specificity control | High in the tested cell model. Localization may vary with context, but plasma-membrane palmitoylation findings reported for CTDSP1 must not be assigned to CTDSP2. | Knockaert et al., Aug 8, 2006, DOI (knockaert2006uniqueplayersin pages 4-5, rallabandi2020targetingthecterminal pages 3-5) |
| Quantitative BMP evidence | SCP1/SCP2 siRNAs reduced their respective transcripts by at least 80% in HaCaT and osteosarcoma cells. Control-cell phospho-Smad1 returned almost to baseline within 1 hour after BMP4 removal, whereas SCP1/SCP2- or CTDSP2-depleted cells retained elevated phospho-Smad1 longer; CTDSP2 knockdown in OsA-CL cells reached about 90%. | qRT-PCR and phospho-Smad1 time-course immunoblotting | Moderate–high. Strong functional evidence, although exact kinetic constants and CTDSP2-only effect sizes were not reported. | Knockaert et al., Aug 8, 2006, DOI (knockaert2006uniqueplayersin pages 3-4, knockaert2006uniqueplayersin pages 4-5) |
| FOXO transcriptional regulation | CTDSP2 is a direct transcriptional target of FOXO1, FOXO3, and FOXO4, linking PI3K–Akt growth-factor signaling to CTDSP2 expression. FOXO binding near the transcription start site and activation of a 479-bp CTDSP2 promoter/5′-UTR reporter were experimentally demonstrated. | Cross-dataset transcriptomics, inhibitor studies, ChIP–qPCR/ChIP-seq support, promoter mutagenesis, and luciferase assays in human cell lines | High. Three biological replicates were used for quantitative reporter experiments, with reported significance thresholds of P<0.05 and P<0.005. | Kloet et al., Jul 2015, DOI (kloet2015foxotargetgene pages 3-4, kloet2015foxotargetgene pages 4-6) |
| Ras–ERK–p21 and cell-cycle effects | Catalytically active CTDSP2 increased Ras-GTP, ERK and Akt phosphorylation, induced p21^Cip1/Waf1, reduced cyclin–CDK activity, and decreased S-phase entry. S-phase reductions were 46.8±11.4% in U2OS cells, 40.0±6.7% in wild-type mouse fibroblasts, and 29.2±12.4% in Rb-family-triple-knockout fibroblasts. CTDSP2 altered p21 (1.64-fold up), cyclin E2 (1.77-fold down), E2F1 (1.74-fold down), and E2F7 (1.88-fold up). | Doxycycline-controlled wild-type versus D98E/D101N phosphatase-dead CTDSP2; BrdU, microarray/qPCR, Ras pull-down, kinase assays, RNAi, and inhibitor experiments | Moderate–high for the cell models. Rb dephosphorylation was not required for arrest; p21 depletion partially rescued the phenotype. Both overexpression and depletion reduced proliferation in some contexts, indicating network-level, dose-dependent behavior rather than a simple linear tumor-suppressor mechanism. | Kloet et al., Jul 2015, DOI (kloet2015foxotargetgene pages 1-2, kloet2015foxotargetgene pages 8-9, kloet2015foxotargetgene pages 4-6, kloet2015foxotargetgene pages 6-8) |
| Translational status and recent developments | CTDSP2 is currently a research target, not a validated clinical biomarker or therapeutic target. Potential applications include probing nuclear BMP termination, FOXO–growth-factor feedback, and phosphatase-selective inhibitor design; no approved CTDSP2-directed drug, clinical implementation, or substantive 2023–2024 CTDSP2-specific mechanistic advance was identified. | Literature landscape and structural comparison | Low translational maturity. Active-site conservation with CTDSP1 and CTDSPL creates a major selectivity barrier. A 2023 review found during searching concerns CTDNEP1, a different protein, and cannot be used as a CTDSP2 advance. | Cossa et al., Apr 2021, DOI; Rallabandi et al., May 2020, DOI (cossa2021proteinphosphatasesin pages 6-7, rallabandi2020targetingthecterminal pages 3-5) |
Table: Evidence matrix distinguishing direct human CTDSP2 findings from SCP-family or shared-paralog evidence. It summarizes molecular function, localization, pathways, quantitative results, caveats, and the limited current translational status.
The requested gene–protein pairing is internally and externally consistent:
CTDSP2 must not be confused with CTDSPL2, despite the similar symbol. The retrieved CTDSPL2 nuclear-interactome paper investigates another protein and even reports context-dependent behavior toward CTD substrates; none of those results was used as direct CTDSP2 evidence. CTDNEP1/Dullard is likewise a separate enzyme with different established biology. (kang2016asystematicstudy pages 1-2)
CTDSP2 belongs to the small CTD phosphatase branch of the FCP/SCP phosphatase family and the broader haloacid-dehalogenase-like, or HAD-like, phosphohydrolase superfamily. This agrees with the supplied InterPro annotations—Dullard phosphatase, FCP1 domain, HAD-like superfamily, and RNA polymerase CTD phosphatase—and with literature placing CTDSP2 among FCP-related nuclear phosphatases. (cohen2010phosphatasefamiliesdephosphorylating pages 14-15, cossa2021proteinphosphatasesin pages 6-7)
The catalytic center contains the conserved DXDX(T/V) signature characteristic of FCP-homology phosphatases. In the accepted HAD-like mechanism, the first aspartate acts as a catalytic nucleophile, forming a transient phosphoaspartyl intermediate; a divalent cation, generally Mg²⁺ in biochemical descriptions of this family, coordinates the phosphate and supports catalysis. This precise chemical mechanism is strongly supported at the family and structural level, although modern CTDSP2-specific pre-steady-state kinetics were not found.
Human CTDSP2 has an experimentally deposited apo structure, PDB 2Q5E. Structural comparisons indicate substantial similarity among CTDSP1, CTDSP2, and CTDSPL, particularly around the catalytic pocket. CTDSP2 has an approximately ten-residue N-terminal insertion adjacent to the active site, which may contribute to binding-partner discrimination despite active-site conservation. The three proteins are reported to have approximately 40% conservation across their full sequences and much higher conservation around the catalytic center. (rallabandi2020targetingthecterminal pages 3-5)
This conservation has an important practical consequence: an active-site inhibitor developed without extensive selectivity profiling could inhibit several SCP paralogs. Authoritative analysis therefore treats paralog selectivity—potentially through peripheral or N-terminal interaction surfaces—as a central drug-development challenge. (rallabandi2020targetingthecterminal pages 3-5)
CTDSP2 catalyzes the hydrolysis of a phosphoserine residue in a protein or peptide substrate:
protein–O–PO₃²⁻ + H₂O → protein–OH + inorganic phosphate.
It is therefore a protein serine/threonine phosphatase in biochemical classification, although its established physiological substrates and sequence-context preferences are considerably narrower than that broad EC designation implies.
The RNA polymerase II largest subunit contains tandem heptad repeats with the consensus YSPTSPS. Human SCP-family enzymes—including CTDSP2—were identified through homology to FCP1 and display CTD phosphatase activity in vitro, preferentially removing phosphate from Ser5 rather than Ser2. Ser5 phosphorylation is associated especially with promoter escape and early transcription, whereas FCP1 has stronger pSer2-directed activity and a major role in polymerase recycling. (kim2017emergingrolesof pages 1-3, cossa2021proteinphosphatasesin pages 6-7)
The crucial annotation caveat is that the pSer5 preference was established and reviewed largely at the SCP-family level, not through comprehensive CTDSP2-selective kinetic measurements against all CTD phospho-isoforms. Moreover, loss-of-function work has not established the SCPs as dominant global transcription-cycle phosphatases. Current expert synthesis instead suggests that they may act locally, including in transcriptional-repressor contexts, rather than controlling bulk RNAPII phosphorylation throughout the genome. (cossa2021proteinphosphatasesin pages 6-7)
Thus, RNAPII CTD pSer5 is a credible biochemical substrate, but describing global RNAPII transcriptional resetting as CTDSP2’s sole or definitively primary physiological function would overstate the evidence.
The most compelling substrate-level evidence concerns Smad1, a receptor-regulated transcription factor in the BMP pathway. BMP receptors phosphorylate the Smad1 C-terminal SSXS region, promoting nuclear accumulation and transcriptional activity. Knockaert and colleagues showed that Xenopus SCP2/Os4 directly removed this C-terminal phosphorylation in vitro and strongly preferred phospho-Smad1 over phospho-Smad2. At high enzyme concentration a small, reproducible effect on Smad2 was observed, indicating preference rather than absolute specificity. (knockaert2006uniqueplayersin pages 1-2, knockaert2006uniqueplayersin pages 3-4)
Human SCP2/CTDSP2 expressed in embryos decreased endogenous phospho-Smad1 and BMP-responsive transcription. In HEK293 cells, human SCP1–3 bound Smad1 efficiently but Smad2 only weakly; catalytically inactive substrate-trapping forms retained Smad1 binding. These results support direct recognition rather than an indirect effect caused simply by global transcriptional repression. (knockaert2006uniqueplayersin pages 2-3, knockaert2006uniqueplayersin pages 3-4)
Importantly, this study demonstrates removal of the receptor-generated C-terminal Smad1 phosphate, not dephosphorylation of its interdomain linker. Statements in some secondary literature that broadly group CTDSP proteins as “R-SMAD phosphatases” should therefore not erase the experimentally resolved site specificity. (knockaert2006uniqueplayersin pages 2-3, knockaert2006uniqueplayersin pages 3-4)
Endogenous CTDSP2 was detected mainly in the nucleus of OsA-CL osteosarcoma cells using a CTDSP2-reactive antibody. The nuclear immunofluorescence signal was substantially depleted by CTDSP2-targeting siRNA, supporting antibody specificity. Following BMP treatment, Smad1 and CTDSP2 colocalized in the nucleus; CTDSP2 did not block Smad1 nuclear import. These observations place CTDSP2 downstream of receptor activation and translocation, where it terminates or limits nuclear Smad1 signaling. (knockaert2006uniqueplayersin pages 4-5)
This localization also fits access to RNAPII CTD and proposed transcriptional-repressor complexes. It should not be inferred that CTDSP2 shares every localization mechanism of CTDSP1: for example, reported palmitoylation-dependent plasma-membrane targeting applies to CTDSP1 and was not demonstrated for CTDSP2. (rallabandi2020targetingthecterminal pages 3-5)
CTDSP2 is a negative regulator of canonical BMP signaling. In Xenopus embryos, SCP2/Os4 expression reduced epidermal BMP-response markers, induced neural markers, inhibited a BMP-responsive reporter, and could induce a partial secondary dorsal axis. A catalytic Asp mutant lacked these effects, connecting the developmental phenotype to phosphatase activity. (knockaert2006uniqueplayersin pages 1-2, knockaert2006uniqueplayersin pages 2-3)
Loss-of-function experiments in human cells strengthened the physiological case. SCP1- and SCP2-directed siRNAs reduced their respective transcripts by at least 80% in HaCaT cells and increased BMP4-induced phospho-Smad1 accumulation, while TGF-β-induced phospho-Smad2 remained unchanged. After BMP4 removal, phospho-Smad1 returned almost to baseline within one hour in control cells but remained significantly elevated after SCP1/SCP2 depletion. (knockaert2006uniqueplayersin pages 3-4, knockaert2006uniqueplayersin pages 4-5)
In OsA-CL cells, CTDSP2 knockdown approached 90% and prolonged phospho-Smad1 persistence after BMP withdrawal. Combined biochemical, gain-of-function, rescue, localization, and RNAi results therefore support CTDSP2 as a prominent nuclear Smad1 C-terminal phosphatase, while also indicating partial redundancy with CTDSP1 and possibly other phosphatases. (knockaert2006uniqueplayersin pages 3-4, knockaert2006uniqueplayersin pages 4-5)
CTDSP2 is itself controlled by growth-factor signaling. Kloet and colleagues identified it as a direct transcriptional target of FOXO1, FOXO3, and FOXO4. PI3K or Akt activation decreased CTDSP2 expression, whereas FOXO activation or PI3K/Akt inhibition increased it across several human and mouse cell lines. Rapid induction persisted in the presence of cycloheximide, supporting direct rather than newly synthesized intermediary-dependent regulation. (kloet2015foxotargetgene pages 1-2, kloet2015foxotargetgene pages 3-4)
ChIP experiments showed FOXO occupancy near the CTDSP2 transcriptional start site. FOXO3 activated a 479-bp CTDSP2 promoter/5′-UTR reporter, and mutation of the FOXO-binding sites reduced activation. Reporter data used three biological replicates with reported thresholds of P<0.05 and P<0.005. (kloet2015foxotargetgene pages 3-4, kloet2015foxotargetgene pages 4-6)
Ectopic wild-type CTDSP2, but not a phosphatase-dead D98E/D101N mutant, reduced BrdU incorporation and S-phase entry. The reduction was 46.8±11.4% in U2OS cells, 40.0±6.7% in wild-type mouse embryonic fibroblasts, and 29.2±12.4% in fibroblasts lacking all three Rb-family pocket proteins. The persistence of arrest in Rb-triple-knockout cells showed that Rb dephosphorylation is not required, challenging earlier interpretations that placed Rb at the center of the phenotype. (kloet2015foxotargetgene pages 1-2, kloet2015foxotargetgene pages 4-6)
CTDSP2 expression altered several cell-cycle regulators: p21^Cip1/Waf1 increased 1.64-fold, E2F7 increased 1.88-fold, cyclin E2 decreased 1.77-fold, and E2F1 decreased 1.74-fold. p21 depletion attenuated the arrest and restored cyclin-E-bound CDK2 activity, whereas E2F7 depletion did not significantly rescue it. (kloet2015foxotargetgene pages 4-6, kloet2015foxotargetgene pages 6-8)
Mechanistically, CTDSP2 increased Ras-GTP loading and phosphorylation of ERK and Akt. MEK inhibition reduced CTDSP2-induced p21 expression, and p53 perturbation also impaired p21 induction. CTDSP2 depletion reduced basal and FOXO-induced ERK/Akt phosphorylation. The proposed signaling chain is therefore FOXO → CTDSP2 phosphatase activity → Ras–Raf–MEK–ERK and p53-dependent p21 induction → reduced cyclin–CDK activity and S-phase entry. The immediate CTDSP2 substrate that initiates Ras activation remains unidentified. (kloet2015foxotargetgene pages 8-9, kloet2015foxotargetgene pages 6-8)
An important systems-level qualification is that both overexpression and depletion reduced proliferation in some experimental settings. CTDSP2 therefore appears to participate in a feedback-regulated signaling network with expression-level and context dependence, not a simple monotonic “more CTDSP2 equals less growth” relationship. (kloet2015foxotargetgene pages 6-8)
Secondary sources associate CTDSP2 with PML and Rb and describe tumor-suppressive functions shared with CTDSPL and CTDSP1. However, these claims are less mechanistically resolved than the Smad1 work and are frequently presented jointly across paralogs. The Rb-triple-knockout experiments specifically demonstrate that Rb is dispensable for CTDSP2-induced arrest, even though Rb hypophosphorylation accompanies CTDSP2 expression. (rallabandi2020targetingthecterminal pages 3-5, kloet2015foxotargetgene pages 4-6)
Likewise, the association of SCPs with neuronal-gene silencing is well supported for the family, especially CTDSP1-centered REST studies, but the retrieved evidence does not establish a unique CTDSP2-specific molecular role with the same precision as its Smad1 activity. Expert reviews note that SCP expression in non-neuronal lineages may help maintain local RNAPII hypophosphorylation at neuronal genes, while emphasizing that SCPs do not appear to be major global transcription phosphatases. (cossa2021proteinphosphatasesin pages 6-7)
CTDSP2 currently has research applications, rather than an established clinical implementation:
No approved CTDSP2-directed drug, validated clinical diagnostic, or real-world therapeutic implementation was identified. Claims that CTDSP2 is presently an actionable cancer target should therefore be considered hypothesis-generating. The most defensible translational strategy would first require selective chemical probes, direct substrate mapping, pharmacodynamic biomarkers, and genetic validation in relevant disease models.
The evidence hierarchy supports the following conclusions:
Priority experiments include CTDSP2-selective quantitative phosphoproteomics; kinetic comparison of RNAPII pSer2, pSer5, pSer7, and Smad phosphopeptides; endogenous catalytic-site editing rather than overexpression; identification of the substrate linking CTDSP2 to Ras activation; tissue-resolved localization and expression; and development of paralog-selective probes exploiting surfaces outside the conserved catalytic pocket.
References
(cohen2010phosphatasefamiliesdephosphorylating pages 14-15): Patricia T.W. Cohen. Phosphatase families dephosphorylating serine and threonine residues in proteins. ArXiv, pages 659-675, Jan 2010. URL: https://doi.org/10.1016/b978-0-12-374145-5.00085-1, doi:10.1016/b978-0-12-374145-5.00085-1. This article has 19 citations.
(rallabandi2020targetingthecterminal pages 3-5): Harikrishna Reddy Rallabandi, Palanivel Ganesan, and Young Jun Kim. Targeting the c-terminal domain small phosphatase 1. May 2020. URL: https://doi.org/10.3390/life10050057, doi:10.3390/life10050057. This article has 17 citations.
(cossa2021proteinphosphatasesin pages 6-7): Giacomo Cossa, Pabitra K. Parua, Martin Eilers, and Robert P. Fisher. Protein phosphatases in the rnapii transcription cycle: erasers, sculptors, gatekeepers, and potential drug targets. Genes & Development, 35:658-676, Apr 2021. URL: https://doi.org/10.1101/gad.348315.121, doi:10.1101/gad.348315.121. This article has 75 citations and is from a highest quality peer-reviewed journal.
(knockaert2006uniqueplayersin pages 3-4): Marie Knockaert, Gopal Sapkota, Claudio Alarcón, Joan Massagué, and Ali H. Brivanlou. Unique players in the bmp pathway: small c-terminal domain phosphatases dephosphorylate smad1 to attenuate bmp signaling. Proceedings of the National Academy of Sciences, 103:11940-11945, Aug 2006. URL: https://doi.org/10.1073/pnas.0605133103, doi:10.1073/pnas.0605133103. This article has 177 citations and is from a highest quality peer-reviewed journal.
(knockaert2006uniqueplayersin pages 4-5): Marie Knockaert, Gopal Sapkota, Claudio Alarcón, Joan Massagué, and Ali H. Brivanlou. Unique players in the bmp pathway: small c-terminal domain phosphatases dephosphorylate smad1 to attenuate bmp signaling. Proceedings of the National Academy of Sciences, 103:11940-11945, Aug 2006. URL: https://doi.org/10.1073/pnas.0605133103, doi:10.1073/pnas.0605133103. This article has 177 citations and is from a highest quality peer-reviewed journal.
(knockaert2006uniqueplayersin pages 1-2): Marie Knockaert, Gopal Sapkota, Claudio Alarcón, Joan Massagué, and Ali H. Brivanlou. Unique players in the bmp pathway: small c-terminal domain phosphatases dephosphorylate smad1 to attenuate bmp signaling. Proceedings of the National Academy of Sciences, 103:11940-11945, Aug 2006. URL: https://doi.org/10.1073/pnas.0605133103, doi:10.1073/pnas.0605133103. This article has 177 citations and is from a highest quality peer-reviewed journal.
(knockaert2006uniqueplayersin pages 2-3): Marie Knockaert, Gopal Sapkota, Claudio Alarcón, Joan Massagué, and Ali H. Brivanlou. Unique players in the bmp pathway: small c-terminal domain phosphatases dephosphorylate smad1 to attenuate bmp signaling. Proceedings of the National Academy of Sciences, 103:11940-11945, Aug 2006. URL: https://doi.org/10.1073/pnas.0605133103, doi:10.1073/pnas.0605133103. This article has 177 citations and is from a highest quality peer-reviewed journal.
(kloet2015foxotargetgene pages 3-4): David E.A. Kloet, Paulien E. Polderman, Astrid Eijkelenboom, Lydia M. Smits, Miranda H. van Triest, Maaike C.W. van den Berg, Marian J. Groot Koerkamp, Dik van Leenen, Philip Lijnzaad, Frank C. Holstege, and Boudewijn M.T. Burgering. Foxo target gene ctdsp2 regulates cell cycle progression through ras and p21cip1/waf1. Jul 2015. URL: https://doi.org/10.1042/bj20140831, doi:10.1042/bj20140831. This article has 44 citations and is from a domain leading peer-reviewed journal.
(kloet2015foxotargetgene pages 4-6): David E.A. Kloet, Paulien E. Polderman, Astrid Eijkelenboom, Lydia M. Smits, Miranda H. van Triest, Maaike C.W. van den Berg, Marian J. Groot Koerkamp, Dik van Leenen, Philip Lijnzaad, Frank C. Holstege, and Boudewijn M.T. Burgering. Foxo target gene ctdsp2 regulates cell cycle progression through ras and p21cip1/waf1. Jul 2015. URL: https://doi.org/10.1042/bj20140831, doi:10.1042/bj20140831. This article has 44 citations and is from a domain leading peer-reviewed journal.
(kloet2015foxotargetgene pages 1-2): David E.A. Kloet, Paulien E. Polderman, Astrid Eijkelenboom, Lydia M. Smits, Miranda H. van Triest, Maaike C.W. van den Berg, Marian J. Groot Koerkamp, Dik van Leenen, Philip Lijnzaad, Frank C. Holstege, and Boudewijn M.T. Burgering. Foxo target gene ctdsp2 regulates cell cycle progression through ras and p21cip1/waf1. Jul 2015. URL: https://doi.org/10.1042/bj20140831, doi:10.1042/bj20140831. This article has 44 citations and is from a domain leading peer-reviewed journal.
(kloet2015foxotargetgene pages 8-9): David E.A. Kloet, Paulien E. Polderman, Astrid Eijkelenboom, Lydia M. Smits, Miranda H. van Triest, Maaike C.W. van den Berg, Marian J. Groot Koerkamp, Dik van Leenen, Philip Lijnzaad, Frank C. Holstege, and Boudewijn M.T. Burgering. Foxo target gene ctdsp2 regulates cell cycle progression through ras and p21cip1/waf1. Jul 2015. URL: https://doi.org/10.1042/bj20140831, doi:10.1042/bj20140831. This article has 44 citations and is from a domain leading peer-reviewed journal.
(kloet2015foxotargetgene pages 6-8): David E.A. Kloet, Paulien E. Polderman, Astrid Eijkelenboom, Lydia M. Smits, Miranda H. van Triest, Maaike C.W. van den Berg, Marian J. Groot Koerkamp, Dik van Leenen, Philip Lijnzaad, Frank C. Holstege, and Boudewijn M.T. Burgering. Foxo target gene ctdsp2 regulates cell cycle progression through ras and p21cip1/waf1. Jul 2015. URL: https://doi.org/10.1042/bj20140831, doi:10.1042/bj20140831. This article has 44 citations and is from a domain leading peer-reviewed journal.
(kang2016asystematicstudy pages 1-2): NaNa Kang, JaeHyung Koo, Sen Wang, Sun Jin Hur, and Young Yil Bahk. A systematic study of nuclear interactome of c-terminal domain small phosphatase-like 2 using inducible expression system and shotgun proteomics. BMB Reports, 49:319-324, Jun 2016. URL: https://doi.org/10.5483/bmbrep.2016.49.6.240, doi:10.5483/bmbrep.2016.49.6.240. This article has 9 citations and is from a peer-reviewed journal.
(kim2017emergingrolesof pages 1-3): Youngjun Kim. Emerging roles of ctd phosphatases. ArXiv, 27:370-381, Mar 2017. URL: https://doi.org/10.5352/jls.2017.27.3.370, doi:10.5352/jls.2017.27.3.370. This article has 1 citations.