Cited by 111Sirtuins and Resveratrol in MedicineHistone Deacetylase Inhibitors ResearchNuclear Structure and Function

The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.

The seven faces of SIRT7

Open access

Blank, Maximilian F., Grummt, Ingrid·2017·Transcription

DOI 10.1080/21541264.2016.1276658PMC PMC5423475

Open this paper in CoChat — free account

Abstract

-dependent protein deacetylases, is a key mediator of many cellular activities. SIRT7 expression is linked to cell proliferation and oncogenic activity, connecting SIRT7-dependent regulation of ribosome biogenesis with checkpoints controlling cell cycle progression, metabolic homeostasis, stress resistance, aging and tumorigenesis. Despite this important functional link, the enzymatic activity, the molecular targets and physiological functions of SIRT7 are poorly defined. Here, we review recent progress in SIRT7 research and elaborate the main pathways in which SIRT7 participates.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1080/21541264.2016.1276658

Cites

44 of 44 references verified0 citation errors · 0 not checkable

Statistics

Figure 1. The sirtuin family of NAD+-dependent deacetylases. The seven mammalian sirtuins (SIRT1–7) share a conserved catalytic core domain (HDAC domain) with varying N- and C-terminal sequences. They localize to different cellular compartments, use NAD+ as a co-factor and serve functions in multiple cellular processes.CC BY-NC-ND · PubMed Central

Figure 2. Reversible acetylation of PAF53 and U3–55k regulates pre-rRNA synthesis and processing. In normal growth conditions, SIRT7 keeps the Pol I-associated factor PAF53 hypoacetylated, which is required for rDNA transcription. Deacetylation of the U3–55k protein by SIRT7 facilitates the interaction of U3–55k with U3 snoRNA, thus promoting pre-rRNA cleavage. Nucleolar release of SIRT7 in response to environmental or metabolic stress enhances acetylation of PAF53 and U3–55k, which impairs Pol I transcription and pre-rRNA processing and attenuates ribosome biogenesis.CC BY-NC-ND · PubMed Central

Figure 3. The seven faces of SIRT7. The cartoon depicts the main pathways in which SIRT7 is involved. The proteins that are targeted by SIRT7 or mediate SIRT7 function are highlighted.CC BY-NC-ND · PubMed Central

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

1 retracted

RETRACTED ARTICLE: Sirt7 promotes gastric cancer growth and inhibits apoptosis by epigenetically inhibiting miR-34a
Zhang, S., Chen, P., Huang, Z., Hu, X., Chen, M., Hu, S., Hu, Y. J., & Cai, T. (2015) · Scientific Reports · doi:10.1038/srep09787 · Cited by 111
Retracted
Mitochondria: In Sickness and in Health
Nunnari, J., & Suomalainen, A. (2012) · Cell · doi:10.1016/j.cell.2012.02.035 · Cited by 3,479
Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins
Michishita, E., Park, J. Y., Burneskis, J. M., Barrett, J. C., & Horikawa, I. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-01-0033 · Cited by 1,364
Nucleolar proteome dynamics
Andersen, J., Lam, Y. W., Leung, A. K. L., Ong, S., Lyon, C. E., Lamond, A. I., & Mann, M. (2005) · Nature · doi:10.1038/nature03207 · Cited by 1,173
The nucleolus under stress
Boulon, S., Westman, B. J., Hutten, S., Boisvert, F.-M., & Lamond, A. I. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.024 · Cited by 1,103
Sirt7 Increases Stress Resistance of Cardiomyocytes and Prevents Apoptosis and Inflammatory Cardiomyopathy in Mice
Vakhrusheva, O., Smolka, C., Gajawada, P., Sawa Kostin, D., Boettger, T., Kubin, T., Braun, T. W., & Bober, E. (2008) · Circulation Research · doi:10.1161/circresaha.107.164558 · Cited by 646
SIRT7 links H3K18 deacetylation to maintenance of oncogenic transformation
Barber, M. F., Michishita-Kioi, E., Xi, Y., Tasselli, L., Kioi, M., Moqtaderi, Z., Tennen, R. I., Paredes, S., Young, N. L., Chen, K., et al. (2012) · Nature · doi:10.1038/nature11043 · Cited by 635
Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription
Ford, E., Voit, R., Liszt, G., Magin, C., Grummt, I., & Guarente, L. (2006) · Genes & Development · doi:10.1101/gad.1399706 · Cited by 629
Self-citation
Global Levels of Histone Modifications Predict Prognosis in Different Cancers
Seligson, D. B., Horvath, S., McBrian, M. A., Mah, V. H., Yu, H., Tze, S., Wang, Q., Chia, D., Goodglick, L., & Kurdistani, S. K. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.080874 · Cited by 524
The box C/D and H/ACA snoRNPs: key players in the modification, processing and the dynamic folding of ribosomal RNA
Watkins, N. J., & Bohnsack, M. T. (2011) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.117 · Cited by 520
The multifaceted functions of sirtuins in cancer
Chalkiadaki, A., & Guarente, L. (2015) · Nature reviews. Cancer · doi:10.1038/nrc3985 · Cited by 513
The Complexity of Human Ribosome Biogenesis Revealed by Systematic Nucleolar Screening of Pre-rRNA Processing Factors
Tafforeau, L., Zorbas, C., Langhendries, J.-L., Mullineux, S.-T., Stamatopoulou, V., Mullier, R., Wacheul, L., & Lafontaine, D. L. J. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.08.011 · Cited by 492
A mitochondrial UPR-mediated metabolic checkpoint regulates hematopoietic stem cell aging
Mohrin, M., Shin, J., Liu, Y., Brown, K., Luo, H., Xi, Y., Haynes, C. M., & Chen, D. (2015) · Science · doi:10.1126/science.aaa2361 · Cited by 490
SIRT7 is a histone desuccinylase that functionally links to chromatin compaction and genome stability
Li, L., Shi, L., Yang, S., Yan, R., Zhang, D., Yang, J., He, L., Li, W., Yi, X., Sun, L., et al. (2016) · Nature Communications · doi:10.1038/ncomms12235 · Cited by 400
Sirtuin7 oncogenic potential in human hepatocellular carcinoma and its regulation by the tumor suppressors MiR-125a-5p and MiR-125b
Kim, J. K., Noh, J. H., Jung, K. H., Eun, J. W., Bae, H. J., Kim, M. G., Chang, Y. G., Shen, Q., Park, W. S., Lee, J. Y., et al. (2012) · Hepatology · doi:10.1002/hep.26101 · Cited by 323
Histone acetylation by CBP and p300 at double-strand break sites facilitates SWI/SNF chromatin remodeling and the recruitment of non-homologous end joining factors
Ogiwara, H., Ui, A., Otsuka, A., Satoh, H., Yokomi, I., Nakajima, S., Yasui, A., Yokota, J., & Kohno, T. (2011) · Oncogene · doi:10.1038/onc.2010.592 · Cited by 320
Yeast Pre-rRNA Processing and Modification Occur Cotranscriptionally
Koš, M., & Tollervey, D. W. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.02.024 · Cited by 310
SIRT7 represses Myc activity to suppress ER stress and prevent fatty liver disease
Shin, J., He, M., Liu, Y., Paredes, S., Villanova, L., Brown, K., Qiu, X., Nabavi, N., Mohrin, M., Wojnoonski, K., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.10.007 · Cited by 287
SIRT7 promotes genome integrity and modulates non‐homologous end joining DNA repair
Vázquez, B. N., Thackray, J. K., Simonet, N. G., Kane‐Goldsmith, N., Martínez‐Redondo, P., Nguyen, T. T. T., Bunting, S. F., Vaquero, A., Tischfield, J. A., & Serrano, L. (2016) · The EMBO Journal · doi:10.15252/embj.201593499 · Cited by 276
A SIRT7-Dependent Acetylation Switch of GABPβ1 Controls Mitochondrial Function
Ryu, D., Jo, Y. S., Sasso, G. L., Stein, S., Zhang, H., Perino, A., Lee, J. U., Zeviani, M., Romand, R., Hottiger, M. O., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.08.001 · Cited by 267
The opposing roles of Wnt-5a in cancer
McDonald, S. L., & Silver, A. R. (2009) · British Journal of Cancer · doi:10.1038/sj.bjc.6605174 · Cited by 260
Repression of RNA Polymerase I upon Stress Is Caused by Inhibition of RNA-Dependent Deacetylation of PAF53 by SIRT7
Chen, S., Seiler, J., Santiago-Reichelt, M., Felbel, K., Grummt, I., & Voit, R. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.10.010 · Cited by 229
SIRT7 Controls Hepatic Lipid Metabolism by Regulating the Ubiquitin-Proteasome Pathway
Yoshizawa, T., Karim, M. F., Sato, Y., Senokuchi, T., Miyata, K., Fukuda, T., Go, C., Tasaki, M., Uchimura, K., Kadomatsu, T., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.03.006 · Cited by 218
Functional Proteomics Establishes the Interaction of SIRT7 with Chromatin Remodeling Complexes and Expands Its Role in Regulation of RNA Polymerase I Transcription
Tsai, Y.-C., Greco, T. M., Boonmee, A., Miteva, Y., & Cristea, I. M. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.a111.015156 · Cited by 201
FOXOs and Sirtuins in Vascular Growth, Maintenance, and Aging
Oellerich, M. F., & Potente, M. (2012) · Circulation Research · doi:10.1161/circresaha.111.246488 · Cited by 161
Recruitment of factors linking transcription and processing of pre-rRNA to NOR chromatin is UBF-dependent and occurs independent of transcription in human cellsPreprint
Prieto, J.-L., & McStay, B. (2007) · Genes & Development · doi:10.1101/gad.436707 · Cited by 156
Involvement of SIRT7 in resumption of rDNA transcription at the exit from mitosis
Grob, A., Roussel, P., Wright, J. E., McStay, B., Hernandez‐Verdun, D., & Sirri, V. (2009) · Journal of Cell Science · doi:10.1242/jcs.042382 · Cited by 155
Sirtuin-7 Inhibits the Activity of Hypoxia-inducible Factors
Hubbi, M. E., Hu, H., Gupta, K., Gilkes, D. M., & Semenza, G. L. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.476903 · Cited by 154
Biological and Potential Therapeutic Roles of Sirtuin Deacetylases
Taylor, D. M., Maxwell, M. M., Luthi‐Carter, R., & Kazantsev, A. G. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8357-y · Cited by 146
The Role of Sirtuins in the Control of Metabolic Homeostasis
Yu, J., & Auwerx, J. (2009) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.04952.x · Cited by 145
Quantitative Proteomics and Dynamic Imaging of the Nucleolus Reveal Distinct Responses to UV and Ionizing Radiation
Moore, H. M., Bai, B., Boisvert, F., Latonen, L., Rantanen, V., Simpson, J. C., Pepperkok, R., Lamond, A. I., & Laiho, M. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.009241 · Cited by 138
SIRT7-dependent deacetylation of the U3-55k protein controls pre-rRNA processing
Chen, S., Blank, M. F., Iyer-Bierhoff, A., Huang, B., Wang, L., Grummt, I., & Voit, R. (2016) · Nature Communications · doi:10.1038/ncomms10734 · Cited by 129
Intracellular distribution of human SIRT 7 and mapping of the nuclear/nucleolar localization signal
Kiran, S., Chatterjee, N., Singh, S., Kaul, S. C., Wadhwa, R., & Ramakrishna, G. (2013) · FEBS Journal · doi:10.1111/febs.12346 · Cited by 125
Sirtuin 7 Plays a Role in Ribosome Biogenesis and Protein Synthesis
Tsai, Y.-C., Greco, T. M., & Cristea, I. M. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.031377 · Cited by 125
SIRT7 inactivation reverses metastatic phenotypes in epithelial and mesenchymal tumors
Malik, S., Villanova, L., Tanaka, S., Aonuma, M., Roy, N., Berber, E., Pollack, J. R., Michishita-Kioi, E., & Chua, K. F. (2015) · Scientific Reports · doi:10.1038/srep09841 · Cited by 120
Comparative interactomes of SIRT 6 and SIRT 7: Implication of functional links to aging
Lee, N., Kim, D., Kim, E., Park, S. J., Kwon, J., Shin, J., Park, S., Moon, Y. H., Wang, H.-J., Gho, Y. S., et al. (2014) · PROTEOMICS · doi:10.1002/pmic.201400001 · Cited by 86
SIRT7 Is Activated by DNA and Deacetylates Histone H3 in the Chromatin Context
Tong, Z., Wang, Y., Zhang, X., Kim, D. D., Sadhukhan, S., Hao, Q., & Lin, H. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.5b01084 · Cited by 75
Regulation of energy homeostasis by the ubiquitin-independent REGγ proteasome
Sun, L., Fan, G., Shan, P., Qiu, X., Dong, S., Liao, L., Yu, C., Wang, T., Gu, X., Li, Q., et al. (2016) · Nature Communications · doi:10.1038/ncomms12497 · Cited by 72
MicroRNA-3666-induced suppression of SIRT7 inhibits the growth of non-small cell lung cancer cells
Shi, H., Ji, Y., Zhang, D., Liu, Y., & Fang, P. (2016) · Oncology Reports · doi:10.3892/or.2016.5063 · Cited by 65
SIRT7 Exhibits Oncogenic Potential in Human Ovarian Cancer Cells
Wang, H.-L., Lu, R.-Q., Xie, S.-H., Zheng, H., Wen, X.-M., Gao, X., & Guo, L. (2015) · Asian Pacific Journal of Cancer Prevention · doi:10.7314/apjcp.2015.16.8.3573 · Cited by 61
p53‐Dependent subcellular proteome localization following DNA damage
Boisvert, F., & Lamond, A. I. (2010) · PROTEOMICS · doi:10.1002/pmic.201000213 · Cited by 59
Isolation of U3 snoRNP from CHO cells: a novel 55 kDa protein binds to the central part of U3 snoRNA
Lübben, B., Marshallsay, C., Rottmann, N., & Lührmann, R. (1993) · Nucleic Acids Research · doi:10.1093/nar/21.23.5377 · Cited by 59
Altered Sirtuin 7 Expression is Associated with Early Stage Breast Cancer
Aljada, A., Saleh, A., Alkathiri, M. A., Shamsa, H. B., Al-Bawab, A., & Nasr, A. (2015) · Breast Cancer Basic and Clinical Research · doi:10.4137/bcbcr.s23156 · Cited by 42
Wnt5a Signals through DVL1 to Repress Ribosomal DNA Transcription by RNA Polymerase I
Dass, R. A., Sarshad, A. A., Carson, B. B., Feenstra, J. M., Kaur, A., Obrdlík, A., Parks, M., Prakash, V., Love, D. K., Pietras, K., et al. (2016) · PLoS Genetics · doi:10.1371/journal.pgen.1006217 · Cited by 26

Research works printed but not linked: 1

10.1074/mcp.A111.01515 · DOI

Sorted by citations

NAD+ metabolism, stemness, the immune response, and cancer
Navas, L. E., & Carnero, A. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00354-w · Cited by 551
Nuclear sirtuins and inflammatory signaling pathways
Mendes, K. L., Lelis, D. D. F., & Santos, S. H. S. (2017) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2017.11.001 · Cited by 239
Dual Tumor Suppressor and Tumor Promoter Action of Sirtuins in Determining Malignant Phenotype
Carafa, V., Altucci, L., & Nebbioso, A. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00038 · Cited by 186
The Roles of Sirtuin Family Proteins in Cancer Progression
Zhao, E., Hou, J., Ke, X., Abbas, M. N., Kausar, S., Zhang, L., & Cui, H. (2019) · Cancers · doi:10.3390/cancers11121949 · Cited by 125
Sirtuins' control of autophagy and mitophagy in cancer
Aventaggiato, M., Vernucci, E., Barreca, F., Russo, M. A., & Tafani, M. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107748 · Cited by 103

See all 111

Authors: Blank, M. F., & Grummt, I.
Affiliations: German Cancer Research Center (DE)
Corresponding author: Grummt, Ingrid
ORCID: Blank, Maximilian F.
Grummt, Ingrid
Venue: Transcription
Publisher: Informa UK Limited
Published: 2017-01-23
Volume: 8
Issue: 2
Pages: 67-74
ISSN: 2154-1264 (ISSN-L)
2154-1272
DOI: 10.1080/21541264.2016.1276658
PMC: PMC5423475
OpenAlex: W2571520146
Cited by: 111
References: 44
Citations by year: 2026: 5 · 2025: 8 · 2024: 9 · 2023: 14 · 2022: 21 · 2021: 12 · 2020: 15 · 2019: 13 · 2018: 9 · 2017: 5
FWCI: 1.31
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc-nd
creativecommons.org/licenses/by-nc-nd/4.0/ (vor)
Locations: Transcription (publishedVersion, cc-by-nc-nd)
Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-nd)
PubMed Central (publishedVersion, cc-by-nc-nd)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
Keywords: SIRT7, ribosome biogenesis, cell cycle checkpoints, metabolic homeostasis, stress tolerance, aging, carcinogenesis, cell proliferation, molecular targets
MeSH terms: Animals, Cell Transformation, Neoplastic, Energy Metabolism, Humans, Ribosomes, DNA-Directed RNA Polymerases, Stress, Physiological, Transcription, Genetic, Sirtuins, Genomic Instability, Cell Cycle Checkpoints

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

The seven faces of SIRT7

Abstract

Overview

Integrity signals

Figures

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks