Cited by 61Protein Interaction Studies and Fluorescence AnalysisProtein Structure and DynamicsDrug Transport and Resistance Mechanisms

Testosterone meets albumin – the molecular mechanism of sex hormone transport by serum albumins

Open access
Czub, Mateusz P., Venkataramany, Barat S., Majorek, Karolina A., Handing, Katarzyna B., Porebski, Przemyslaw J., Beeram, Sandya R., Suh, Kyungah, Woolfork, Ashley G. +3 more·2019·Chemical Science

Abstract

The first albumin structure in complex with testosterone and the hormone's binding affinity measured with two methods.

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.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1039/c8sc04397c

Cites

3 of 3 references verified0 citation errors · 0 not checkable

Statistics

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.

A few free checks a day · papers already verified open instantly · results are public

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?

  • Binding site competition and allosteric coupling can, in conditions such as postprandial and heightened fatty acids and drug usage, result in displacement of testosterone from its binding site, potentially affecting testosterone bioavailability and/or metabolism.

    “Binding site competition and allosteric coupling can in certain conditions, especially postprandial and in circumstances of heightened levels of fatty acids and drug usage, result in displacement of T from its binding site thereby potentially affecting T bioavailability and/or metabolism [25, 26].”

    From Role of sex hormone-binding globulin in the free hormone hypothesis and the relevance of free testosterone in androgen physiology (2022) · cites this paper as [26]

    Split into 2 atoms — 0 confirmed, 2 partially supported, 0 disputed, 0 misattributed, 0 unverifiable. Expand the claim to see per-atom verdicts.

    Experimental — accuracy not yet measured

Self-check

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

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

Cites

Flagged first, then by citations

Research works printed but not linked: 70

  1. Peters T. J., All About Albumin: Biochemistry, Genetics, and Medical Applications, Academic Press, San Diego, CA, USA, 1st edn, 1995.
  2. Handing K. B. Shabalin I. G. Kassaar O. Khazaipoul S. Blindauer C. A. Stewart A. J. Chruszcz M. Minor W. Chem. Sci. 2016 7 6635 6648 28567254 PMC5450522
  3. Merlot A. M. Kalinowski D. S. Richardson D. R. Front. Physiol. 2014 5 299 25161624 PMC4129365
  4. Sudlow G. Birkett D. J. Wade D. N. Mol. Pharmacol. 1976 12 1052 1061 1004490
  5. Sudlow G. Birkett D. J. Wade D. N. Mol. Pharmacol. 1975 11 824 832 1207674
  6. Ghuman J. Zunszain P. A. Petitpas I. Bhattacharya A. A. Otagiri M. Curry S. J. Mol. Biol. 2005 353 38 52 16169013
  7. Wang Z. Ho J. X. Ruble J. R. Rose J. Rüker F. Ellenburg M. Murphy R. Click J. Soistman E. Wilkerson L. Carter D. C. Biochim. Biophys. Acta 2013 1830 5356 5374 23838380
  8. Bhattacharya A. A. Grüne T. Curry S. J. Mol. Biol. 2000 303 721 732 11061971
  9. Curry S. Drug Metab. Pharmacokinet. 2009 24 342 357 19745561
  10. Bern M. Sand K. M. K. Nilsen J. Sandlie I. Andersen J. T. J. Controlled Release 2015 211 144 162 26055641
  11. Handing K. B. Shabalin I. G. Szlachta K. Majorek K. A. Minor W. Mol. Immunol. 2016 71 143 151 26896718 PMC4800003
  12. Petitpas I. Petersen C. E. Ha C. Bhattacharya A. A. Zunszain P. A. Ghuman J. V Bhagavan N. Curry S. Proc. Natl. Acad. Sci. U. S. A. 2003 100 6440 6445 12743361 PMC164465
  13. Rooyackers O. E. Nair K. S. Annu. Rev. Nutr. 1997 17 457 485 9240936
  14. Rifai N., Tietz Textbook of Clinical Chemistry and Molecular Diagnostics, Saunders, St. Louis, MO, USA, 6th edn, 2018.
  15. Melmed S., Polonsky K. S., Larsen P. R. and Kronenberg H. M., Williams Textbook of Endocrinology, Elsevier, Los Angeles, CA, USA, 13th edn, 2016.
  16. Södergård R. Bäckström T. Shanbhag V. Carstensen H. J. Steroid Biochem. 1982 16 801 810 7202083
  17. Zheng X. Bi C. Brooks M. Hage D. S. Anal. Chem. 2015 87 11187 11194 26484387 PMC4986690
  18. Kragh-Hansen U. Minchiotti L. Brennan S. O. Sugita O. Eur. J. Biochem. 1990 193 169 174 2226433
  19. Pearlman W. H. Crépy O. J. Biol. Chem. 1967 242 182 189 6066733
  20. Vermeulen A. Verdonck L. Steroids 1968 11 609 635 4172115
  21. Fischer M. J. Bos O. J. van der Linden R. F. Wilting J. Janssen L. H. Biochem. Pharmacol. 1993 45 2411 2416 8328979
  22. Bertolini J., Goss N. and Curling J., Production of Plasma Proteins for Therapeutic Use, John Wiley & Sons, Inc., Hoboken, NJ, USA, 2013.
  23. Minor W. Cymborowski M. Otwinowski Z. Chruszcz M. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2006 62 859 866 16855301
  24. Otwinowski Z. Minor W. Methods Enzymol. 1997 276 307 326 27754618
  25. Majorek K. A. Porebski P. J. Dayal A. Zimmerman M. D. Jablonska K. Stewart A. J. Chruszcz M. Minor W. Mol. Immunol. 2012 52 174 182 22677715 PMC3401331
  26. Vagin A. Teplyakov A. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2010 66 22 25 20057045
  27. Porebski P. J. Cymborowski M. Pasenkiewicz-Gierula M. Minor W. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2016 72 266 280 PMC4756610 26894674
  28. Murshudov G. N. Skubák P. Lebedev A. A. Pannu N. S. Steiner R. A. Nicholls R. A. Winn M. D. Long F. Vagin A. A. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2011 67 355 367 21460454 PMC3069751
  29. Emsley P. Lohkamp B. Scott W. G. Cowtan K. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2010 66 486 501 20383002 PMC2852313
  30. Winn M. D. Ballard C. C. Cowtan K. D. Dodson E. J. Emsley P. Evans P. R. Keegan R. M. Krissinel E. B. Leslie A. G. W. McCoy A. McNicholas S. J. Murshudov G. N. Pannu N. S. Potterton E. A. Powell H. R. Read R. J. Vagin A. Wilson K. S. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2011 67 235 242 21460441 PMC3069738
  31. Shabalin I. G. Porebski P. J. Minor W. Crystallogr. Rev. 2018 24 236 262 30416256 PMC6219471
  32. Painter J. Merritt E. A. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2006 62 439 450 16552146
  33. Long F. Nicholls R. A. Emsley P. GraGraǽulisulis S. Merkys A. Vaitkus A. Murshudov G. N. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2017 73 112 122 PMC5297914 28177307
  34. Kowiel M. Jaskolski M. Dauter Z. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2014 70 3290 3298 25478846 PMC4257622
  35. Krissinel E. Henrick K. J. Mol. Biol. 2007 372 774 797 17681537
  36. Zimmerman M. D. Grabowski M. Domagalski M. J. Maclean E. M. Chruszcz M. Minor W. Methods Mol. Biol. 2014 1140 1 25 24590705 PMC4086192
  37. Grabowski M. Langner K. M. Cymborowski M. Porebski P. J. Sroka P. Zheng H. Cooper D. R. Zimmerman M. D. Elsliger M. A. Burley S. K. Minor W. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2016 72 1181 1193 PMC5108346 27841751
  38. Ehrenberg M. Cronvall E. Rigler R. FEBS Lett. 1971 18 199 203 11946120
  39. Mallik R. Yoo M. J. Briscoe C. J. Hage D. S. J. Chromatogr. A 2010 1217 2796 2803 20227701 PMC2849903
  40. Zheng X. Li Z. Podariu M. I. Hage D. S. Anal. Chem. 2014 86 6454 6460 24911267 PMC4082384
  41. Holm L. Rosenström P. Nucleic Acids Res. 2010 38 545 549 PMC2896194 20457744
  42. Sekula B. Bujacz A. J. Med. Chem. 2016 59 82 89 26652101
  43. Porebski P. J. Sroka P. Zheng H. Cooper D. R. Minor W. Protein Sci. 2018 27 86 94 28815771 PMC5734276
  44. Curry S. Vox Sang. 2002 83 Suppl. 1 315 319 12617161
  45. Wang Y. Yu H. Shi X. Luo Z. Lin D. Huang M. J. Biol. Chem. 2013 288 15980 15987 23592780 PMC3668753
  46. Batista A. N. L. Batista J. M. Ashton L. Bolzani V. S. Furlan M. Blanch E. W. Chirality 2014 26 497 501 25042763
  47. Majorek K. A. Kuhn M. L. Chruszcz M. Anderson W. F. Minor W. Protein Sci. 2014 23 1359 1368 25044180 PMC4286991
  48. Costello L. C. Franklin R. B. HSOA J. Hum. Endocrinol. 2016 1 1 19 PMC5345696 28286881
  49. Bujacz A. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2012 68 1278 1289 22993082
  50. Zhang Y. Lee P. Liang S. Zhou Z. Wu X. Yang F. Liang H. Chem. Biol. Drug Des. 2015 86 1178 1184 25958880
  51. Curry S. Mandelkow H. Brick P. Franks N. Nat. Struct. Biol. 1998 5 827 835 9731778
  52. Sekula B. Zielinski K. Bujacz A. Int. J. Biol. Macromol. 2013 60 316 324 23769932
  53. Lejon S. Cramer J. F. Nordberg P. Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. 2008 64 64 69 PMC2374170 18259051
  54. Sekula B. Ciesielska A. Rytczak P. Koziołkiewicz M. Bujacz A. Biosci. Rep. 2016 36 e00338 27129297 PMC5293571
  55. Bujacz A. Zielinski K. Sekula B. Proteins 2014 82 2199 2208 24753230
  56. Bhattacharya A. A. Curry S. Franks N. P. J. Biol. Chem. 2000 275 38731 38738 10940303
  57. Rubinstein A. L. Carpenter D. M. Minkoff J. R. Clin. J. Pain 2013 29 840 845 24384986
  58. Bawor M. Bami H. Dennis B. B. Plater C. Worster A. Varenbut M. Daiter J. Marsh D. C. Steiner M. Anglin R. Coote M. Pare G. Thabane L. Samaan Z. Drug Alcohol Depend. 2015 149 1 9 25702934
  59. Schooling C. M. Au Yeung S. L. Freeman G. Cowling B. J. BMC Med. 2013 11 57 23448151 PMC3621815
  60. Anguizola J. Matsuda R. Barnaby O. S. Hoy K. S. Wa C. DeBolt E. Koke M. Hage D. S. Clin. Chim. Acta 2013 425 64 76 23891854 PMC3795802
  61. Ruiz-Cabello F. Erill S. Clin. Pharmacol. Ther. 1984 36 691 695 6488690
  62. Gadgil H. S. Bondarenko P. V. Treuheit M. J. Ren D. Anal. Chem. 2007 79 5991 5999 17571855
  63. Barnaby O. S. Cerny R. L. Clarke W. Hage D. S. Clin. Chim. Acta 2011 412 277 285 21034726 PMC3053033
  64. Liu X. Du Y. Sun W. Kou J. Yu B. Spectrochim. Acta, Part A 2009 74 1189 1196 19857990
  65. Grossmann M. Thomas M. C. Panagiotopoulos S. Sharpe K. MacIsaac R. J. Clarke S. Zajac J. D. Jerums G. J. Clin. Endocrinol. Metab. 2008 93 1834 1840 18319314
  66. Mooradian A. D. Pamplona D. M. Viosca S. P. Korenman S. G. J. Steroid Biochem. 1988 29 369 370 3357342
  67. Watanabe S. Tani T. Watanabe S. Seno M. Lipids 1990 25 633 638 2079869
  68. Manni A. Pardridge W. M. Cefalu W. Nisula B. C. Bardin C. W. Santner S. J. Santen R. J. J. Clin. Endocrinol. Metab. 1985 61 705 710 4040924
  69. Kelly D. M. Nettleship J. E. Akhtar S. Muraleedharan V. Sellers D. J. Brooke J. C. McLaren D. S. Channer K. S. Jones T. H. Life Sci. 2014 109 95 103 24953607
  70. Koutsari C. Ali A. H. Nair K. S. Rizza R. A. O'Brien P. Khosla S. Jensen M. D. J. Clin. Endocrinol. Metab. 2009 94 3414 3423 19567532 PMC2741706

Cited by

Sorted by citations

Authors
Czub, M. P., Venkataramany, B. S., Majorek, K. A., Handing, K. B., Porebski, P. J., Beeram, S. R., Suh, K., Woolfork, A. G., Hage, D. S., Shabalin, I. G., & Minor, W.
Affiliations
  • University of Virginia (US)
  • University of Nebraska–Lincoln (US)
Corresponding author
  • Hage, David S.
  • Shabalin, Ivan G.
  • Minor, Wladek
Venue
Chemical Science
Published
2019
Volume
10
Issue
6
Pages
1607-1618
ISSN
  • 2041-6520 (ISSN-L)
  • 2041-6539
OpenAlex
W2904573435
Cited by
61
References
3
Citations by year
2026: 8 · 2025: 6 · 2024: 8 · 2023: 10 · 2022: 4 · 2021: 12 · 2020: 8 · 2019: 5
FWCI
2.22
Type
journal article
Language
en
Open access
Locations
  • Chemical Science (publishedVersion, cc-by-nc)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
  • OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion, other-oa)
Funders
  • National Institute of General Medical Sciences (R01-GM044391, R01-GM117080, R01-GM117325, R01-GM118619)
  • National Institute of Allergy and Infectious Diseases (HHSN272201200026C, HHSN272201700060C)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
Keywords
testosterone, serum albumin, protein-ligand binding, Sudlow site I, binding sites, human serum albumin, binding constant, tryptophan fluorescence quenching

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