The DOI matches its Crossref record; 37 of the 38 references it cites were found in a registry or an index.
The Redox State of the Cell Regulates the Ligand Binding Affinity of Human Neuroglobin and Cytoglobin
Open accessAbstract
Neuroglobin and cytoglobin reversibly bind oxygen in competition with the distal histidine, and the observed oxygen affinity therefore depends on the properties of both ligands. In the absence of an external ligand, the iron atom of these globins is hexacoordinated. There are three cysteine residues in human neuroglobin; those at positions CD7 and D5 are sufficiently close to form an internal disulfide bond. Both cysteine residues in cytoglobin, although localized in other positions than in human neuroglobin, may form a disulfide bond as well. The existence and position of these disulfide bonds was demonstrated by mass spectrometry and thiol accessibility studies. Mutation of the cysteines involved, or the use of reducing agents to break the S-S bond, led to a decrease in the observed oxygen affinity of human neuroglobin by an order of magnitude. The critical parameter is the histidine dissociation rate, which changes by about a factor of 10. The same effect is observed with human cytoglobin, although to a much lesser extent (less than a factor of 2). These results suggest a novel mechanism for the regulation of oxygen binding; contact with an appropriate electron donor would provoke the release of oxygen. Hence the oxygen affinity would be directly linked to the redox state of the cell.
Overview
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
Cites
Statistics
Verification
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?
In the citing paper
“neuroglobin will increase its penta-coordinated character upon oxidation of Cys46 and Cys55 to form a disulfide bond [64, 80-82].”
From Current perspectives and challenges in understanding the role of nitrite as an integral player in nitric oxide biology and therapy (2011) · cites this paper as [80]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control
Jia, L., Bonaventura, C., Bonaventura, J., & Stamler, J. S. (1996) · Nature · doi:10.1038/380221a0 · Cited by 1,592
A vertebrate globin expressed in the brain
Burmester, T., Weich, B., Reinhardt, S., & Hankeln, T. (2000) · Nature · doi:10.1038/35035093 · Cited by 1,025
Self-citationDisulfide bonds as switches for protein function.
Hogg, P. (2003) · TIBS -Trends in Biochemical Sciences. Regular ed · doi:10.1016/s0968-0004(03)00057-4 · Cited by 581
Nonvertebrate Hemoglobins: Functions and Molecular Adaptations
Weber, R. E., & Vinogradov, S. N. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.569 · Cited by 511
Determinants of a protein fold
Bashford, D., Chothia, C., & Lesk, A. M. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90521-3 · Cited by 496
Cytoglobin: A Novel Globin Type Ubiquitously Expressed inVertebrate Tissues
Burmester, T., Ebner, B., Weich, B., & Hankeln, T. (2002) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a004096 · Cited by 496
Self-citationDewilde, S., Kiger, L., Burmester, T., Hankeln, T., Baudin‐Creuza, V., Aerts, T., Marden, M. C., Caubergs, R. J., & Moens, L. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106438200 · Cited by 453
Self-citationNeuroglobin is up-regulated by and protects neurons from hypoxic-ischemic injury
Sun, Y., Jin, K., Mao, X. O., Zhu, Y., & Greenberg, D. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251466698 · Cited by 448
Wittenberg, J. B., Bolognesi, M., Wittenberg, B. A., & Guertin, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.r100058200 · Cited by 376
Self-citationA Ubiquitously Expressed Human Hexacoordinate Hemoglobin
Trent, J. T., & Hargrove, M. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201934200 · Cited by 358
Flagged first, then by citations
1 of the 38 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 201–274 of 274
Protein self‐modification by heme‐generated reactive species
Monzani, E., Nicolis, S., Roncone, R., Barbieri, M., Granata, A., & Casella, L. (2007) · IUBMB Life · doi:10.1002/iub.10 · Cited by 10
Russo, R., Giordano, D., di Prisco, G., Hoa, G. H. B., Marden, M. C., Verde, C., & Kiger, L. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2013.02.013 · Cited by 10
Self-citationMaintenance of aerobic metabolism increases immunoisolated islet survival
Stagner, J. I., Seelan, R. S., & Parthasarathy, R. N. (2011) · Islets · doi:10.4161/isl.3.3.15404 · Cited by 10
Nanoporous gold based electrodes for electrochemical studies of human neuroglobin
Mie, Y., Takahashi, K., Yuka, I., Sueyoshi, K., Tsujino, H., Yamashita, T., & Uno, T. (2019) · Electrochemistry Communications · doi:10.1016/j.elecom.2019.106621 · Cited by 10
Kaliszuk, S. J., Morgan, N. I., Ayers, T. N., Sparacino-Watkins, C. E., DeMartino, A. W., Bocian, K. A., Ragireddy, V., Tong, Q., & Tejero, J. (2022) · Nitric Oxide · doi:10.1016/j.niox.2022.06.001 · Cited by 9
Circular dichroism spectral studies on the recombinant human neuroglobin
Zhao, C., Li, L., Wang, L., & Ji, H. (2006) · Chinese Science Bulletin · doi:10.1007/s11434-006-2144-7 · Cited by 9
Doorslaer, S. V., & Cuypers, B. (2017) · Molecular Physics · doi:10.1080/00268976.2017.1392629 · Cited by 9
Hankeln, T., & Burmester, T. (2008) · Elsevier eBooks · doi:10.1016/b978-044452839-1.50009-7 · Cited by 9
Self-citationOxygenation and gender effects on photopic frequency-doubled contrast sensitivity
Connolly, D. M., & Hosking, S. L. (2008) · Vision Research · doi:10.1016/j.visres.2007.11.006 · Cited by 9
Charged Amino Acid Substitutions Affect Conformation of Neuroglobin and Cytochrome c Heme Groups
Semenova, M. A., Bochkova, Z. V., Smirnova, O. M., Maksimov, G. V., Kirpichnikov, M. P., Dolgikh, D. A., Brazhe, N. A., & Chertkova, R. V. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46040211 · Cited by 8
Leuven, W. V., Cuypers, B., Desmet, F., Giordano, D., Verde, C., Moens, L. J., Doorslaer, S. V., & Dewilde, S. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2013.01.042 · Cited by 8
Self-citationImpact of A90P, F106L and H64V mutations on neuroglobin stability and ligand binding kinetics
André, E., Derrien, V., Sebban, P., Assrir, N., Lescop, E., & Bernad, S. (2018) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-018-1625-x · Cited by 8
Neuroglobin deficiency increases seizure susceptibility but does not affect basal behavior in mice
Gøtzsche, C. R., Woldbye, D. P. D., Hundahl, C. A., & Hay‐Schmidt, A. (2022) · Journal of Neuroscience Research · doi:10.1002/jnr.25105 · Cited by 8
Neuroglobin and Other Nerve Haemoglobins
Burmester, T., & Hankeln, T. (2008) · Springer eBooks · doi:10.1007/978-88-470-0807-6_18 · Cited by 8
Self-citationExploiting a list of protein sequences
Marden, M. C., Dewilde, S., Kiger, L., Hamdane, D., Uzan, J., Burmester, T., Hankeln, T., Moens, L. J., Baudin‐Creuza, V., Célier, C., et al. (2007) · Gene · doi:10.1016/j.gene.2007.01.036 · Cited by 8
Self-citationNitric Oxide Sensing by a Blue Fluorescent Protein
Montali, C., Abbruzzetti, S., Franzen, A., Casini, G., Bruno, S., Delcanale, P., Burgstaller, S., Ramadani‐Muja, J., Malli, R., Gensch, T., et al. (2022) · Antioxidants · doi:10.3390/antiox11112229 · Cited by 7
Xu, J., Yin, G., Huang, F., Wang, B., & Du, W. (2009) · Journal of Molecular Modeling · doi:10.1007/s00894-009-0581-3 · Cited by 7
Structural Plasticity in Globins
Estarellas, C., Capece, L., Seira, C., Bidon‐Chanal, A., Estrin, D. A., & Luque, F. J. (2016) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2016.07.002 · Cited by 7
Vetromile, C. M., Mikšovská, J., & Larsen, R. W. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.01.009 · Cited by 7
Semenova, M. A., Bochkova, Z. V., Smirnova, O. M., Ignatova, A. A., Parshina, E. Y., Ziganshin, R., Bocharov, E. V., Brazhe, N. A., Maksimov, G. V., Kirpichnikov, M. P., et al. (2023) · Russian Journal of Bioorganic Chemistry · doi:10.1134/s1068162023030196 · Cited by 6
Reductive nitrosylation of ferric microperoxidase-11
Ascenzi, P., Simone, G. D., Sbardella, D., & Coletta, M. (2018) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-018-1623-z · Cited by 6
Tertiary and quaternary effects in the allosteric regulation of animal hemoglobins
Ronda, L., Bruno, S., & Bettati, S. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2013.03.013 · Cited by 6
Cytoglobin scavenges intracellular hydrogen peroxide and regulates redox signals in the vasculature
Jourd’heuil, F. L., Mathai, C., Pham, L. G. C., Gilliard, K., Balnis, J., Overmyer, K. A., Coon, J. J., Jaitovich, A., Boivin, B., & Jourd’heuil, D. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103633 · Cited by 5
Meglioli, M., Sebastiani, F., Bellei, M., Rocco, G. D., Ranieri, A., Bortolotti, C. A., Sola, M., Borsari, M., Smulevich, G., & Battistuzzi, G. (2025) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.5c00551 · Cited by 5
The molecular mechanism of redox interaction between neuroglobin and cytochrome c
Bochkova, Z. V., Semenova, M. A., Smirnova, O. M., Maksimov, G. V., Rubin, A. B., Kirpichnikov, M. P., Dolgikh, D. A., Chertkova, R. V., & Brazhe, N. A. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.145040 · Cited by 5
Jusman, S. W. A., Iswanti, F. C., Suyatna, F. D., Ferdinal, F., Wanandi, S. I., & Sadikin, M. (2014) · Medical Journal of Indonesia · doi:10.13181/mji.v23i3.1025 · Cited by 5
Structural characterization of spectroscopic substates in carbonmonoxy neuroglobin
Lutz, S., & Meuwly, M. (2011) · Faraday Discussions · doi:10.1039/c0fd00003e · Cited by 5
Doorslaer, S. V., Trandafir, F., Harmer, J. R., Moens, L. J., & Dewilde, S. (2014) · Biophysical Chemistry · doi:10.1016/j.bpc.2014.03.007 · Cited by 4
Self-citationChen, L., Yuan, H., Wang, X., Li, L., Tan, X., & Lin, Y. (2022) · ChemBioChem · doi:10.1002/cbic.202200531 · Cited by 4
Cloning, expression and purification of Atlantic salmon (Salmo salar, L.) neuroglobin
Bjørlykke, G. A., Kvamme, B. O., Slinde, E., & Raae, A. J. (2012) · Protein Expression and Purification · doi:10.1016/j.pep.2012.09.010 · Cited by 4
Cytochrome b5 reductase 4 efficiently reduces neuroglobin and cytoglobin
DeMartino, A. W., Cunningham, O., Mulluri, S., Cassel, D., Hutar, M., Ji, L., Deligiannidis, E. A., Kaliszuk, S. J., Huang, X. N., Tong, Q., et al. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.12.010 · Cited by 3
Zhou, S., Tian, O., Li, W., Li, J., Li, W., & Han, F. (2023) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2023.109217 · Cited by 3
Nanotechnological Approach in Combating Pesticide Induced Fish Toxicity: Pros and Cons Controversy
Sow, P., & Samadder, A. (2021) · Proceedings of the Zoological Society · doi:10.1007/s12595-021-00421-2 · Cited by 3
Insights into heme degradation and hydrogen peroxide-induced dimerization of human neuroglobin
Cassiani, A., Furtmüller, P. G., Borsari, M., Battistuzzi, G., & Hofbauer, S. (2024) · Bioscience Reports · doi:10.1042/bsr20241265 · Cited by 4
Neuroglobin in rat brain neurons
Узлова, Е. В., & Zimatkin, S. M. (2021) · Сибирский научный медицинский журнал · doi:10.18699/ssmj20210404 · Cited by 2
Nikinmaa, M. (2010) · Cambridge University Press eBooks · doi:10.1017/cbo9780511845178.003 · Cited by 2
Kinetics Inside the Protein: Shape of the Geminate Kinetics in Myoglobin
Hamdane, D., Kiger, L., Hoa, G. H. B., & Marden, M. C. (2011) · The Journal of Physical Chemistry B · doi:10.1021/jp107168b · Cited by 2
Self-citationStructure, function and the related mechanism of cytoglobin
Liu, X., Zhou, D., & Luo, A. (2018) · Scientia Sinica Vitae · doi:10.1360/n052017-00107 · Cited by 1
Hafideddine, Z., Loier, T., Brempt, N. V., Henau, S. D., Ching, H. Y. V., Neukermans, S., Defossé, S., Berghmans, H., Sgammato, R., Aerts, R., et al. (2022) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2022.112063 · Cited by 2
Self-citationSook, B. R. (2022) · Digital Archive @ GSU · doi:10.57709/1059262 · Cited by 2
The Phylogeny and Structural Properties of 2/2 Haemoglobins
Vuletich, D. A., & Lecomte, J. T. J. (2008) · Springer eBooks · doi:10.1007/978-88-470-0807-6_5 · Cited by 2
Photodissociation of Hemoglobin Molecules in Vivo Under External Irradiation
Мамилов, С. А., & Bezuglyi, M. A. (2025) · Studies in systems, decision and control · doi:10.1007/978-3-031-82035-9_4 · Cited by 1
Quantum yields of the photodissociation of HbO2in the visible and near IR spectral region
Мамилов, С. А., Esman, S. S., Asimov, M. M., & Gisbrecht, A. I. (2015) · Proceedings of SPIE, the International Society for Optical Engineering/Proceedings of SPIE · doi:10.1117/12.2175629 · Cited by 1
Aydemir, H. B., & Korkmaz, E. M. (2023) · Biologia · doi:10.1007/s11756-023-01389-4 · Cited by 1
Semenova, M. A., Dolgikh, D. A., Kirpichnikov, M. P., Maksimov, G. V., Brazhe, N. A., Bocharov, E. V., Ziganshin, R., Parshina, E. Y., Ignatova, A. A., Smirnova, O. M., et al. (2023) · Биоорганическая химия · doi:10.31857/s013234232303020x · Cited by 1
Wu, L., Sun, Y., Li, M., Li, Y., Yao, Y., Liu, X., Hao, Y., Li, D., & Wu, Y. (2015) · Journal für Ornithologie · doi:10.1007/s10336-015-1290-6 · Cited by 1
Maguire, D. (2006) · Springer eBooks · doi:10.1007/0-387-29540-2_53 · Cited by 1
Conformational Dynamics Associated with Ligand Binding to Vertebrate Hexa-coordinate Hemoglobins
Astudillo, L. (2014) · doi:10.25148/etd.fi14040865 · Cited by 1
A role for neuroglobin in the inhibition of cytochrome c-mediated apoptosome formation
Henty, K. (2011) · ResearchSpace (University of Auckland) · Cited by 1
Mathai, C., Jourd’heuil, F. L., Pham, L. G. C., Gilliard, K., Balnis, J., Jen, A., Overmyer, K. A., Coon, J. J., Jaitovich, A., Boivin, B., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.31.535146 · Cited by 1
Carpenter, M. (2010) · University of Birmingham Institutional Research Archive (University of Birmingham) · Cited by 1
Stone, L. C. (2015) · University of Birmingham Institutional Research Archive (University of Birmingham)
Hb Octamers by Introduction of Surface Cysteines
Baudin‐Creuza, V., Ho, C., & Marden, M. C. (2011) · doi:10.1002/9781119975427.ch26
Self-citationFunctional and comparative studies of haemoproteins from polar fishes
Riccio, A. (2011) · Università degli Studi di Napoli Federico II · doi:10.6092/unina/fedoa/8865
Thorne, L. S. (2016) · University of Birmingham Institutional Research Archive (University of Birmingham)
Electron transfer and redox chemistry in hexa-coordinate hemoglobins
Singh, N. (2016) · Iowa State University Digital Repository (Iowa State University) · doi:10.31274/etd-180810-4808
Quyen, B. T. L., Nguyen, T. L. H., & Ngo, V. T. (2016) · Communications in Physics · doi:10.15625/0868-3166/26/2/8618
Effect of H64V Mutation on the Dynamical Properties of Human Neuroglobin: A Simulation Study
Bui, T. L. Q., Hoang, V. T., Nguyen, T.-L. H., & Ngo, V. T. (2017) · World Congress on Medical Physics and Biomedical Engineering, September 7 - 12, 2009, Munich, Germany · doi:10.1007/978-981-10-4361-1_47
Hexacoordinate Globins: Characterization and Engineering for Development of Novel Therapeutic Agents
Amdahl, M. B. (2018) · D-Scholarship@Pitt (University of Pittsburgh)
Ma, Q., Han, Y. M., Qi, C., Man, X., & Min, J. Z. (2022) · SSRN Electronic Journal · doi:10.2139/ssrn.4098789
Molecular analysis of the human cytoglobin mRNA isoforms
Porto, E., Loula, P., Strand, S., & Hankeln, T. (2023) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2023.112422
Self-citationHuman neuroglobin and H64A distal variant: how mutation and pH affect the heme pocketPreprint
Meglioli, M., Cesati, L., Battistuzzi, G., Borsari, M., Sebastiani, F., & Smulevich, G. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5574498
Human neuroglobin and H64A distal variant: how mutation and pH affect the heme pocketPreprint
Meglioli, M., Cesati, L., Battistuzzi, G., Borsari, M., Sebastiani, F., & Smulevich, G. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5574476
Caselli, M., Sebastianelli, L., Meglioli, M., Battistuzzi, G., & Borsari, M. (2025) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2025.113109
Cipriano, A., Fang, Q., Hwang, K. K.-L., Chiavellini, P., Mu, W., Aymard, E., Schaeffer, P., Renault, M., Naiken, T., Leblanc, E., et al. (2025) · Cosmetics · doi:10.3390/cosmetics12050230
Evolution of the animal globin superfamily: Insights from the blood clam Anadara granosa
Zhang, W., Chen, T., Hu, Y., Shi, X., & Bao, Y. (2025) · Comparative Biochemistry and Physiology Part D Genomics and Proteomics · doi:10.1016/j.cbd.2025.101703
Human neuroglobin and H64A distal variant: How mutation and pH affect the heme pocket
Meglioli, M., Cesati, L., Battistuzzi, G., Borsari, M., Sebastiani, F., & Smulevich, G. (2025) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2025.127401
Therapeutic Potential of Cytoglobin and Neuroglobin in Oxidative Stress-Driven Liver Diseases
Thủy, L. T. T., Hai, H., Anh, P. T., Chi, N. B. T., Bao, T. V., Huyen, T. D. A., Sang, N. T. Q., & Hermiston, M. L. (2026) · Antioxidants · doi:10.3390/antiox15040485
Andre, D., Fabrizius, A., Hagmaier, M., Waisman, A., Reifenberg, K., Burmester, T., Reuss, S., & Hankeln, T. (2026) · Neuroscience · doi:10.1016/j.neuroscience.2026.07.062
Self-citationAtrikhalov, R. G., Semenova, M. A., Khodnenko, A. P., Smirnova, O. M., Britikov, V. V., Britikova, E. V., Ignatova, A. A., Pakhomov, A. A., Bochkova, Z. V., Brazhe, N. A., et al. (2026) · Russian Journal of Bioorganic Chemistry · doi:10.1134/s1068162026603733
Metadata
- Authors
- Hamdane, D., Kiger, L., Dewilde, S., Green, B. N., Pesce, A., Uzan, J., Burmester, T., Hankeln, T., Bolognesi, M., Moens, L., & Marden, M. C.
- Affiliations
- Inserm (FR)
- University of Antwerp (BE)
- University of Genoa (IT)
- Johannes Gutenberg University Mainz (DE)
- Corresponding author
- Marden, Michael C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-12
- Volume
- 278
- Issue
- 51
- Pages
- 51713-51721
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2164923948
- Cited by
- 274
- References
- 38
- Citations by year
- 2026: 3 · 2025: 11 · 2024: 3 · 2023: 11 · 2022: 10 · 2021: 8 · 2020: 8 · 2019: 8 · 2018: 11 · 2017: 14 · 2016: 13 · 2015: 12 · 2014: 11 · 2013: 15 · 2012: 8
- FWCI
- 5.22
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- CINECA IRIS Institutial Research Information System (University of Genoa) (submittedVersion)
- INFM-OAR (INFN Catania) (submittedVersion, cc-by)
- Funders
- European Commission (QLG3-CT-2002-01548)
- Deutsche Forschungsgemeinschaft (Ha2103/3, Bu956/5)
- Institut National de la Santé et de la Recherche Médicale
- Consiglio Nazionale delle Ricerche
- Universiteit Antwerpen
- Vlaamse regering
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- neuroglobin, cytoglobin, oxygen affinity, redox regulation, disulfide bonds, cysteine residues, distal histidine, reducing agents, electron donors
- MeSH terms
- Neuroglobin, Cytoglobin, Cysteine, Disulfides, Globins, Histidine, Humans, Kinetics, Ligands, Models, Molecular, Nerve Tissue Proteins, Oxidation-Reduction, Oxygen, Protein Binding, Recombinant Proteins, 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
