Deacetylation of N8-acetylspermidine by subcellular fractions of rat tissue
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
These properties match the tissue distribution, subcellular localization and inhibitor sensitivity of mammalian PDAC.
“These properties match the tissue distribution, subcellular localization and inhibitor sensitivity of mammalian PDAC8910111213.”
From Histone deacetylase 10 structure and molecular function as a polyamine deacetylase (2017) · cites this paper as [8]
Spermidine is acetylated at N8 by an N-acetyltransferase in the nucleus and then exported to the cytosol, where it is deacetylated by a metal-dependent N8-acetylspermidine deacetylase (PDAC).
“Spermidine is acetylated at the N8 position by an N-acetyltransferase in the cell nucleus7 and then exported to the cytosol, where it is deacetylated by a metal-dependent N8-acetylspermidine deacetylase, also known as polyamine deacetylase (PDAC)89.”
From Histone deacetylase 10 structure and molecular function as a polyamine deacetylase (2017) · cites this paper as [8]
Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 315,771 · see citing works
Nuclei from Rat Liver: Isolation Method That Combines Purity with High Yield
Blobel, G., & Potter, V. R. (1966) · Science · doi:10.1126/science.154.3757.1662 · Cited by 1,673 · see citing works
Polyamines in Normal and Neoplastic Growth
O'Connor, P. J. (1976) · British Journal of Cancer · doi:10.1038/bjc.1976.55 · Cited by 548 · see citing works
Function of naturally occurring polyamines
Bachrach, U. (1973) · Cited by 530 · see citing works
Oxidation of spermidine and spermine in rat liver: purification and properties of polyamine oxidase
Hölttä, E. (1977) · Biochemistry · doi:10.1021/bi00620a015 · Cited by 335 · see citing works
Putrescine catabolism in mammalian brain
Seiler, N., & Al‐Therib, M. J. (1974) · Biochemical Journal · doi:10.1042/bj1440029 · Cited by 201 · see citing works
Seiler, N., & Al‐Therib, M. J. (1974) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(74)90007-5 · Cited by 74 · see citing works
Properties of an Acidic Histone-binding Protein Fraction from Cell Nuclei
Vidali, G., Boffa, L. C., & Allfrey, V. G. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44638-3 · Cited by 73 · see citing works
Acetylation of spermidine and spermine by rat liver and kidney chromatin
Blankenship, J., & Walle, T. (1977) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(77)90108-4 · Cited by 69 · see citing works
Self-citationMotohiro, T., Teruo, N., & Sano, I. (1975) · Clinica Chimica Acta · doi:10.1016/0009-8981(75)90024-8 · Cited by 62 · see citing works
Histone deacetylase from calf thymus
Inoue, A., & Fujimoto, D. (1970) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(70)90015-x · Cited by 59 · see citing works
CLARK, J. M. (1964) · Andalas University Repository (Andalas University) · Cited by 59 · see citing works
Analysis of polyamines by thin-layer chromatography
Hammond, J. E., & Herbst, E. J. (1968) · Analytical Biochemistry · doi:10.1016/0003-2697(68)90288-1 · Cited by 55 · see citing works
THE DETERMINATION AND DISTRIBUTION OF POLYAMINES IN MAMMALIAN NERVOUS SYSTEM
Shimizu, H., Kakimoto, Y., & Sano, I. (1964) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)26713-1 · Cited by 53 · see citing works
(1990) · International Journal of Biochemistry · doi:10.1016/0020-711x(90)90148-v · Cited by 41 · see citing works
Activity of histone deacetylase in rat liver and Novikoff hepatoma
Libby, P. R. (1970) · Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis · doi:10.1016/0005-2787(70)90027-4 · Cited by 31 · see citing works
ACETYLSPERMIDINES IN HUMAN URINE
Abdel-Monem, M. M., Ohno, K., Fortuny, I. E., & Theologides, A. (1975) · The Lancet · doi:10.1016/s0140-6736(75)92699-9 · Cited by 28 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Histone deacetylase 10 structure and molecular function as a polyamine deacetylase
Hai, Y., Shinsky, S. A., Porter, N. J., & Christianson, D. W. (2017) · Nature Communications · doi:10.1038/ncomms15368 · Cited by 200 · see citing works
Structure, mechanism, and inhibition of the zinc-dependent histone deacetylases
Porter, N. J., & Christianson, D. W. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.01.004 · Cited by 146 · see citing works
Marchant, P., Dredar, S., Manneh, V., Alshabanah, O., Matthews, H., Fries, D., & Blankenship, J. (1989) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(89)90170-7 · Cited by 23 · see citing works
Self-citationN1-Acetylspermidine is not a substrate for N-acetylspermidine deacetylase
Marchant, P., Manneh, V. A., & Blankenship, J. (1986) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(86)90017-6 · Cited by 13 · see citing works
Self-citationDecroos, C., & Christianson, D. W. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00536 · Cited by 12 · see citing works
- Authors
- Blankenship, J.
- Affiliations
- Medical University of South Carolina (US)
- Corresponding author
- Blankenship, Jim
- Venue
- Archives of Biochemistry and Biophysics
- Publisher
- Elsevier BV
- Published
- 1978-07
- Volume
- 189
- Issue
- 1
- Pages
- 20-27
- ISSN
- 0003-9861 (ISSN-L)
- OpenAlex
- W1996060060
- Cited by
- 47
- References
- 17
- Citations by year
- 2025: 1 · 2024: 1 · 2023: 1 · 2022: 1 · 2021: 1 · 2020: 1 · 2019: 3 · 2018: 1 · 2017: 1 · 2015: 1
- FWCI
- 1.50
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Archives of Biochemistry and Biophysics (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Polyamine Metabolism and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Keywords
- N8-acetylspermidine, deacetylation, deacetylase, polyamines, polyamine metabolism, rat tissues, liver, tissue distribution, subcellular fractions, cytosolic enzyme
- MeSH terms
- Acetylation, Acetyltransferases, Animals, Male, Organ Specificity, Spermidine, Subcellular Fractions, Rats, In Vitro Techniques
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