CoChat
Sign Up
Cited by 63Amyloidosis: Diagnosis, Treatment, OutcomesMass Spectrometry Techniques and ApplicationsAlzheimer's disease research and treatments

The DOI matches its Crossref record.

Characterization of Transthyretin Variants in Familial Transthyretin Amyloidosis by Mass Spectrometric Peptide Mapping and DNA Sequence Analysis

Lim, Amareth, Prokaeva, Tatiana, McComb, Mark E., O'Connor, Peter B., Théberge, Roger, Connors, Lawreen H., Skinner, Martha, Costello, Catherine E.·2002·Analytical Chemistry
DOI 10.1021/ac010780+
Open this paper in CoChat — free account

Abstract

Transthyretin (TTR) is a 127-amino acid residue transport protein. In plasma, TTR exists as a tetramer and binds the hormone thyroxine and the retinol-binding protein-vitamin A complex. Amino acid substitutions in TTR are hypothesized to destabilize the tetramer and cause the protein to form intermediates that self-associate into amyloid fibrils. Familial transthyretin amyloidosis (ATTR) is associated with extracellular deposition of wild-type TTR, its variants or fragments as amyloid fibrils in various tissues and organs. A definitive diagnosis of ATTR depends on the detection and identification of TTR variants. Electrospray ionization (ESI) and matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS), in combination with trypsin digestion, have been shown to be powerful tools in characterizing TTR variants. Typically, TTR or its tryptic digest is analyzed by MALDI-TOF MS, liquid chromatography ESI MS, or both. Analysis of tryptic digests by MALDI-TOF MS does not provide enough sequence coverage in TTR to identify all possible modifications. To improve sequence coverage, aliquots of immunoprecipitated TTR samples were digested with trypsin, lysyl endopeptidase Lys-C, or endoproteinase Asp-N. Identification of the peptides from each digest by MALDI-TOF MS provided preliminary information about the sites and mass shifts due to amino acid substitutions from genetic mutations and to posttranslational modifications. The location and identity…

Overview

Integrity signals

Registry

Crossref · 10.1021/ac010780+

Cites

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Citations

Cites

Still being checked.

Research works printed but not linked: 55

  1. Rostom A. A., 1998, Proteins, 11
  2. Benson, M. D.The Metabolic and Molecular Bases of Inherited Disease; Scriver, C. R., Beaudet, A. L., Sly, W. S., Valle, D., Eds.; McGraw-Hill: New York, 1995; pp 4159−4191.
  3. Falk R. H., 1997, Engl. J. Med., 337, 909
  4. Damas A. M., 2000, J. Struct. Biol., 130, 299, 10.1006/jsbi.2000.4273 · DOI
  5. Hund E., 2001, Neurology, 56, 435, 10.1212/WNL.56.4.431 · DOI
  6. Cornwell G. G., 1983, Am. J. Med., 75, 623, 10.1016/0002-9343(83)90443-6 · DOI
  7. Westermark P., 1990, Proc. Natl. Acad. Sci. U.S.A., 87, 2845
  8. Christmanson L., 1991, FEBS Lett., 281, 180, 10.1016/0014-5793(91)80387-I · DOI
  9. Gustavsson, 1995, Lab. Invest., 73, 708
  10. Kishikawa, M.; Nakanishi, T.; Miyazaki, A.; Shimizu, A.Amyloid: Int. J. Exp. Clin. Invest.1999,6, 183−186. · DOI
  11. Costa P. P., 1978, Proc. Natl. Acad. Sci. U.S.A., 75, 4503, 10.1073/pnas.75.9.4499 · DOI
  12. Skinner M., 1981, Biochem. Biophys. Res. Commun., 99, 1332, 10.1016/0006-291X(81)90764-6 · DOI
  13. Pras M., 1983, Proc. Natl. Acad. Sci. U.S.A., 80, 542, 10.1073/pnas.80.2.539 · DOI
  14. Lai Z., 1996, Biochemistry, 35, 6482
  15. Schormann, N.; Murrell, J. R.; Benson, M. D.Amyloid: Int. J. Exp. Clin.Invest.1998,5, 175−187. · DOI
  16. Olofsson A., 2001, J. Biol. Chem., 276, 39599, 10.1074/jbc.M103599200 · DOI
  17. Quintas A., 2001, J. Biol. Chem., 276, 27213, 10.1074/jbc.M101024200 · DOI
  18. Serag A. A., 2001, Biochemistry, 40, 9096, 10.1021/bi010655s · DOI
  19. Connors, L. H.; Richardson, A. M.; Théberge, R.; Costello, C. E.Amyloid: Int.J. Exp. Clin. Invest.2000,7, 54−69. · DOI
  20. Saraiva M. J. M., 2001, Hum. Mutat., 17, 503
  21. Bergethon P. R., 1996, Neurology, 47, 951, 10.1212/WNL.47.4.944 · DOI
  22. Pomfret E. A., 1998, Transplantation, 65, 925, 10.1097/00007890-199804150-00010 · DOI
  23. Wada Y., 1986, Biochim. Biophys. Acta, 873, 319, 10.1016/0167-4838(86)90061-0 · DOI
  24. Suzuki T., 1987, Neurology, 37, 711, 10.1212/WNL.37.4.708 · DOI
  25. Fenn J. B., 1989, Science, 246, 71, 10.1126/science.246.4926.71 · DOI
  26. Ando Y., 1996, Biochem. Biophys. Res. Commun., 228, 483, 10.1006/bbrc.1996.1685 · DOI
  27. Kishikawa M., 1996, J. Mass Spectrom., 31, 114, 10.1002/(SICI)1096-9888(199601)31:1<112::AID-JMS246>3.0.CO;2-E · DOI
  28. Ando, Y.; Ando, E.; Ohlsson, P.I.; Olofsson, A.; Sandgren, O.; Suhr, O.; Terazaki, H.; Obayashi, K.; Lundgren, E.; Ando, M.; Negi, A.Amyloid: Int.J. Exp. Clin. Invest.1999,6, 119−123. · DOI
  29. Kishikawa, M.; Nakanishi, T.; Miyazaki, A.; Shimizu, A.Amyloid: Int. J. Exp.Clin. Invest.1999,6, 48−53. · DOI
  30. Kishikawa, M.; Nakanishi, T.; Miyazaki, A.; Shimizu, A.; Kusaka, H.; Fukui, M.; Nishiue, T.Amyloid: Int. J. Exp. Clin. Invest.1999,6, 278−281. · DOI
  31. Théberge R., 1999, Anal. Chem., 71, 459, 10.1021/ac980531u · DOI
  32. Karas M., 1988, Anal. Chem., 60, 2301, 10.1021/ac00171a028 · DOI
  33. Tachibana, N.; Tokuda, T.; Yoshida, K.; Taketomi, T.; Nakazato, M.; Li, Y.F.; Masuda, Y.; Ikeda, S.I.Amyloid: Int. J. Exp. Clin. Invest.1999,6, 282−288. · DOI
  34. Théberge R., 2000, J. Am. Soc. Mass Spectrom., 11, 175, 10.1016/S1044-0305(99)00136-1 · DOI
  35. Bergquist J., 2000, Clin. Chem., 46, 1300, 10.1093/clinchem/46.9.1293 · DOI
  36. Terazaki H., 2001, Transplantation, 72, 299, 10.1097/00007890-200107270-00023 · DOI
  37. Wilm M., 1996, Anal. Chem., 68, 8
  38. Moini M., 1998, J. Am. Soc. Mass Spectrom., 9, 980
  39. Brown R. S., 1995, J. Anal. Chem., 67, 2003
  40. Vestal M. L., 1995, Rapid Commun. Mass Spectrom., 9, 1050, 10.1002/rcm.1290091115 · DOI
  41. Tang X., 1988, Anal. Chem., 60, 1799
  42. Annan R. S., 1996, Anal. Chem., 68, 3421, 10.1021/ac960221g · DOI
  43. Connors L. H., 1998, Biochim. Biophys. Acta, 1407, 192
  44. Kanda Y., 1974, J. Biol. Chem., 249, 6805, 10.1016/S0021-9258(19)42128-5 · DOI
  45. Lagerwerf F. M., 1996, Rapid Commun. Mass Spectrom., 10, 1910, 10.1002/(SICI)1097-0231(199612)10:15<1905::AID-RCM755>3.0.CO;2-9 · DOI
  46. Mo W., 2000, Rapid Commun. Mass Spectrom., 14, 2081
  47. Harrison H. H., 1991, Am. J. Med. Genet., 39, 452, 10.1002/ajmg.1320390415 · DOI
  48. Alves I. L., 1997, Eur. J. Biochem., 249, 668
  49. Hammarström P., 2001, Science, 293, 2462, 10.1126/science.1062245 · DOI
  50. Ii S., 1991, Neurology, 41, 898
  51. Roepstorff P., 1984, Biomed. Mass Spectrom., 11, 601, 10.1002/bms.1200111109 · DOI
  52. Biemann K., 1988, Biomed. Environ. Mass Spectrom., 16, 111, 10.1002/bms.1200160119 · DOI
  53. Fitch N. J. S., 1991, J. Endocrinol., 129, 313
  54. Jacobson D. R., 1995, Hum. Genet., 95, 312, 10.1007/BF00225199 · DOI
  55. Klein C. J., 1998, Neurology, 51, 1464, 10.1212/WNL.51.5.1462 · DOI

Cited by

Sorted by citations

See all 63

Metadata

Authors
Lim, A., Prokaeva, T., McComb, M. E., O'Connor, P. B., Théberge, R., Connors, L. H., Skinner, M., & Costello, C. E.
Affiliations
  • Boston University (US)
  • Mass Spectrometry Resource, Departments of Biochemistry, Medicine, Physiology and Biophysics, and Amyloid Treatment and Research Program, Boston University School of Medicine, Boston, Massachusetts 02118
ORCID
Venue
Analytical Chemistry
Publisher
American Chemical Society (ACS)
Published
2002-01-15
Volume
74
Issue
4
Pages
741-751
ISSN
  • 0003-2700 (ISSN-L)
  • 1520-6882
DOI
10.1021/ac010780+
OpenAlex
W2091095363
Cited by
63
References
0
Citations by year
2026: 2 · 2025: 2 · 2024: 3 · 2023: 1 · 2021: 2 · 2020: 1 · 2018: 2 · 2017: 5 · 2016: 2 · 2015: 2 · 2013: 4 · 2012: 3
FWCI
1.86
Type
journal article
Language
en
Open access
closed
Locations
  • Analytical Chemistry (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (1s10rr010493-01)
  • National Center for Research Resources (P41-RR-10888, S10 RR-10493, P41RR010888)
Topics
  • Health Sciences › Medicine › Internal Medicine › Amyloidosis: Diagnosis, Treatment, Outcomes
  • Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Keywords
prealbumin, TTR variants, peptide mapping, trypsin digestion, tandem mass spectrometry, post-translational modification, amino acid substitutions, amyloid fibrils
MeSH terms
Adult, Aged, Amino Acid Sequence, Amyloidosis, DNA, Female, Humans, Male, Middle Aged, Peptide Mapping, Prealbumin, Mass Spectrometry, Sequence Analysis, DNA, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Spectrometry, Mass, Electrospray Ionization

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

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Characterization of Transthyretin Variants in Familial Transthyretin Amyloidosis by Mass Spectrometric Peptide Mapping and DNA Sequence Analysis. https://app.cochat.ai/papers/10.1021/ac010780+
The paper
Lim, A., Prokaeva, T., McComb, M. E., O'Connor, P. B., Théberge, R., Connors, L. H., Skinner, M., & Costello, C. E. (2002). Characterization of Transthyretin Variants in Familial Transthyretin Amyloidosis by Mass Spectrometric Peptide Mapping and DNA Sequence Analysis. Analytical Chemistry. https://doi.org/10.1021/ac010780%2B