CoChat
Sign Up
Cited by 10

Conformational stability as a quality attribute for the cell therapy raw material human serum albumin

Wynendaele, Evelien, Ma, Gamaliel Junren, Xu, Xiaolong, Cho, Nam-Joon, De Spiegeleer, Bart·2021·RSC Advances
DOI 10.1039/d1ra01064fPMC PMC8698240
Open this paper in CoChat — free account

Abstract

An overall attribute for the consistency in pharmaceutical quality of human serum albumin encompasses a global measure of conformational stability, as measured by CD, DLS, QCM-D or LSPR.

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/d1ra01064f

Cites

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?

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

No references could be resolved yet.

Research works printed but not linked: 55

  1. Akbarzadehlaleh P. Mirzaei M. Mashahdi-Keshtiban M. Shamsasenjan K. Heydari H. Adv. Pharm. Bull. 2016 6 309 10.15171/apb.2016.043 27766215 PMC5071794 · DOI
  2. Dockal M. Carter D. C. Rüker F. J. Biol. Chem. 2000 275 3042 10.1074/jbc.275.5.3042 10652284 · DOI
  3. Chatterjee T. Pal A. Dey S. Chatterjee B. K. Chakrabarti P. PLoS One 2012 7 e37468 10.1371/journal.pone.0037468 22649528 PMC3359307 · DOI
  4. He X. M. Carter D. C. Nature 1992 358 209 10.1038/358209a0 1630489 · DOI
  5. Curry S. Mandelkow H. Brick P. Franks N. Nat. Struct. Biol. 1998 5 827 10.1038/1869 9731778 · DOI
  6. Bujacz A. Acta Crystallogr. 2012 D68 1278 10.1107/S0907444912027047 22993082 · DOI
  7. Kawaa A. Chuang V. T. G. Kouno Y. Yamasaki K. Miyamoto S. Anraku M. Otagiri M. Biochim. Biophys. Acta, Proteins Proteomics 2017 1865 979 10.1016/j.bbapap.2017.04.004 28473296 · DOI
  8. Yamasaki K. Chuang V. T. G. Maruyama T. Otagiri M. Biochim. Biophys. Acta, Gen. Subj. 2013 1830 5435 10.1016/j.bbagen.2013.05.005 23665585 · DOI
  9. Peters T., All about albumin: biochemistry, genetics, and medical applications, Academic Press, 1995
  10. Simard J. Zunszain P. Ha C.-E. Yang J. Bhagavan N. Petitpas I. Curry S. Hamilton J. Proc. Natl. Acad. Sci. 2005 102 17958 10.1073/pnas.0506440102 16330771 PMC1312385 · DOI
  11. Fanali G. Di Masi A. Trezza V. Marino M. Fasano M. Ascenzi P. Mol. Aspects Med. 2012 33 209 10.1016/j.mam.2011.12.002 22230555 · DOI
  12. Francis G. L. Cytotechnology 2010 62 1 10.1007/s10616-010-9263-3 20373019 PMC2860567 · DOI · Paper page
  13. Tekkatte C. Gunasingh G. P. Cherian K. Sankaranarayanan K. Stem Cells Int. 2011 2011 504723 21603148 PMC3096451
  14. Roche M. Rondeau P. Singh N. R. Tarnus E. Bourdon E. FEBS Lett. 2008 582 1783 10.1016/j.febslet.2008.04.057 18474236 · DOI · Paper page
  15. De Castro M. Orive G. Gascon A. Hernandez R. Pedraz J. Int. J. Pharm. 2006 310 8 10.1016/j.ijpharm.2005.10.028 16434155 · DOI
  16. Horváthy D. B. Simon M. Schwarz C. M. Masteling M. Vácz G. Hornyák I. Lacza Z. BioFactors 2017 43 315 10.1002/biof.1337 27859738 · DOI
  17. Zoellner H. Hofler M. Beckmann R. Hufnagl P. Vanyek E. Bielek E. Wojta J. Fabry A. Lockie S. Binder B. R. J. Cell Sci. 1996 109 2571 10.1242/jcs.109.10.2571 8923218 · DOI
  18. Larsen M. T. Kuhlmann M. Hvam M. L. Howard K. A. Mol Cell Ther. 2016 4 3 10.1186/s40591-016-0048-8 26925240 PMC4769556 · DOI
  19. Merlot A. M. Kalinowski D. S. Richardson D. R. Front. Physiol. 2014 5 299 25161624 PMC4129365
  20. Keenan J. Pearson D. Clynes M. Cytotechnology 2006 50 49 10.1007/s10616-006-9002-y 19003070 PMC3476004 · DOI
  21. Guerrini M. Beccati D. Shriver Z. Naggi A. Viswanathan K. Bisio A. Capila I. Lansing J. C. Guglieri S. Fraser B. Nat. Biotechnol. 2008 26 669 10.1038/nbt1407 18437154 PMC3491566 · DOI
  22. Yao H. Wynendaele E. De Spiegeleer B. Drug Test. Anal. 2019 12 67 10.1002/dta.2691 31471998 · DOI
  23. Yao H. Wynendaele E. Xu X. Kosgei A. De Spiegeleer B. J. Pharm. Biomed. Anal. 2018 147 50 10.1016/j.jpba.2017.08.031 28870607 · DOI
  24. Greenfield N. J. Nat. Protoc. 2006 1 2527 10.1038/nprot.2006.204 17406506 PMC2752288 · DOI
  25. Park J. H. Sut T. N. Jackman J. A. Ferhan A. R. Yoon B. K. Cho N.-J. Phys. Chem. Chem. Phys. 2017 19 8854 10.1039/C7CP01310H 28294278 · DOI
  26. Park J. H. Jackman J. A. Ferhan A. R. Ma G. J. Yoon B. K. Cho N.-J. ACS Appl. Mater. Interfaces 2018 10 32047 10.1021/acsami.8b13749 30178663 · DOI
  27. Park J. H. Ferhan A. R. Jackman J. A. Cho N.-J. Colloids Surf., B 2019 180 306 10.1016/j.colsurfb.2019.04.017 31071570 · DOI
  28. Tan J. Y. B. Yoon B. K. Ma G. J. Sut T. N. Cho N.-J. Jackman J. A. Langmuir 2020 36 9215 10.1021/acs.langmuir.0c01478 32654494 · DOI
  29. Bleustein C. B. Sennett M. Kung R. T. V. Felsen D. Poppas D. P. Stewart R. B. Lasers Surg. Med. 2000 27 465 10.1002/1096-9101(2000)27:5<465::AID-LSM1007>3.0.CO;2-S 11126440 · DOI
  30. Gorobets M. G. Wasserman L. A. Bychkova A. V. Rosenfeld M. A. Chem. Phys. 2019 523 34 10.1016/j.chemphys.2019.03.018 · DOI
  31. Jiang L. Wang Z. Li Y. Meng X. Sui X. Qi B. Zhou L. Int. J. Food Prop. 2015 18 1059 10.1080/10942912.2013.865057 · DOI
  32. Whitmore L. Wallace B. A. Biopolymers 2008 89 392 10.1002/bip.20853 17896349 · DOI
  33. Whitmore L. Wallace B. A. Nucleic Acids Res. 2004 32 W668 10.1093/nar/gkh371 15215473 PMC441509 · DOI
  34. Greenfield N. J. Nat. Protoc. 2007 1 2876 10.1038/nprot.2006.202 17406547 PMC2728378 · DOI
  35. Greenfield N. J. Nat. Protoc. 2006 1 2527 10.1038/nprot.2006.204 17406506 PMC2752288 · DOI
  36. Verma S. Mehta R. K. Maiti P. Rohm K. H. Sonawane A. Biochim. Biophys. Acta 2014 1844 1219 10.1016/j.bbapap.2014.03.013 24721562 · DOI
  37. Benjwal S. Verma S. Rohm K. H. Gursky O. Protein Sci. 2006 15 635 10.1110/ps.051917406 16452626 PMC2249783 · DOI
  38. Facchinetti de Castro Girao L. Goncalves da Rocha S. L. Sobral R. S. Dinis Ano Bom A. P. Franco Sampaio A. L. Godinho da Silva Jr J. Ferrara M. A. Pinto da Silva Bon E. Perales J. Protein Expression Purif. 2016 120 118 10.1016/j.pep.2015.12.012 26714301 · DOI
  39. Cho N.-J. Frank C. W. Kasemo B. Höök F. Nat. Protoc. 2010 5 1096 10.1038/nprot.2010.65 20539285 · DOI
  40. Jackman J. A. Zhdanov V. P. Cho N.-J. Langmuir 2014 30 9494 10.1021/la502431x 25035920 · DOI
  41. Ioannou J. Donald A. M. Tromp R. Food Hydrocolloids 2015 46 216 10.1016/j.foodhyd.2014.12.027 · DOI
  42. Liu Y. Lee J. Mansfield K. M. Ko J. H. Sallam S. Wesdemiotis C. Maynard H. D. Bioconjugate Chem. 2017 28 836 10.1021/acs.bioconjchem.6b00659 28044441 PMC5352466 · DOI
  43. Borrok M. J. Mody N. Lu X. Kuhn M. L. Wu H. Dall'Acqua W. F. Tsui P. J. Pharm. Sci. 2017 106 1008 10.1016/j.xphs.2016.12.023 28057542 · DOI
  44. Xie Y. An J. Yang G. Wu G. Zhang Y. Cui L. Feng Y. J. Biol. Chem. 2014 289 7994 10.1074/jbc.M113.536045 24448805 PMC3953309 · DOI
  45. Mai X. t. Huang J. Tan J. Huang Y. Chen Y. J. Pept. Sci. 2015 21 561 10.1002/psc.2767 25826179 · DOI
  46. Chiu W. A. Axelrad D. A. Dalaijamts C. Dockins C. Shao K. Shapiro A. J. Paoli G. Environ. Health Perspect. 2018 126 067009 10.1289/EHP3368 29968566 PMC6084844 · DOI
  47. Van Vooren L. Krikilion G. Rosier J. De Spiegeleer B. Drug Dev. Ind. Pharm. 2001 27 885 10.1081/DDC-100107254 11699842 · DOI
  48. Lang B. E. Cole K. D. Biotechnol. Prog. 2015 31 62 10.1002/btpr.1996 25270911 · DOI
  49. Michnik A. Therm J. Anal. Calorim. 2003 71 509 10.1023/A:1022851809481 · DOI
  50. Ma G. J. Ferhan A. R. Sut T. N. Jackman J. A. Cho N.-J. Colloids Surf., B 2020 194 111194 10.1016/j.colsurfb.2020.111194 32585535 · DOI
  51. Ma G. J. Ferhan A. R. Jackman J. A. Cho N.-J. Communications Materials 2020 1 1 10.1038/s43246-020-0047-9 · DOI
  52. Ma G. J. Ferhan A. R. Jackman J. A. Cho N.-J. Langmuir 2020 36 10606 10.1021/acs.langmuir.0c02048 32787011 · DOI
  53. Jackman J. A. Ferhan A. R. Yoon B. K. Park J. H. Zhdanov V. P. Cho N.-J. Anal. Chem. 2017 89 12976 10.1021/acs.analchem.7b03921 29111680 · DOI
  54. Ferhan A. R. Jackman J. A. Sut T. N. Cho N.-J. Sensors 2018 18 1283 10.3390/s18041283 29690554 PMC5948918 · DOI
  55. Park H. Ma G. J. Yoon B. K. Cho N.-J. Jackman J. A. Langmuir 2021 37 1306 10.1021/acs.langmuir.0c03396 33444030 · DOI

Cited by

Sorted by citations

Authors
Wynendaele, E., Ma, G. J., Xu, X., Cho, N.-J., & De Spiegeleer, B.
Affiliations
  • Faculty of Pharmaceutical Sciences
  • School of Materials Science and Engineering
ORCID
Venue
RSC Advances
Publisher
Royal Society of Chemistry (RSC)
Published
2021
Volume
11
Issue
25
Pages
15332-15339
ISSN
2046-2069
DOI
10.1039/d1ra01064f
PMC
PMC8698240
Cited by
10
References
0
Language
en
Licence
creativecommons.org/licenses/by-nc/3.0/ (vor, 112 d)
Funders
China Scholarship Council (Xiaolong Xu)

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