The DOI matches its Crossref record; 65 of the 65 references it cites were found in a registry or an index.
Growth-regulatory Human Galectin-1: Crystallographic Characterisation of the Structural Changes Induced by Single-site Mutations and their Impact on the Thermodynamics of Ligand Binding
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.
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
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
The CCP4 suite: programs for protein crystallography
Collaborative Computational Project, N. 4. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,270
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,715
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,085
Solvent content of protein crystals
Matthews, B. W. (1968) · Journal of Molecular Biology · doi:10.1016/0022-2836(68)90205-2 · Cited by 7,961
Nicholls, A., Sharp, K. A., & Honig, B. (1991) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340110407 · Cited by 5,240
AMoRe: an automated package for molecular replacement
Navaza, J. (1994) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767393007597 · Cited by 4,953
Rapid measurement of binding constants and heats of binding using a new titration calorimeter
Wiseman, T., Williston, S., Brandts, J. F., & Lin, L.-N. (1989) · Analytical Biochemistry · doi:10.1016/0003-2697(89)90213-3 · Cited by 2,675
The integration of macromolecular diffraction data
Leslie, A. G. W. (2006) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444905039107 · Cited by 1,341
ALSCRIPT: a tool to format multiple sequence alignments
Barton, G. J. (1993) · "Protein Engineering, Design and Selection" · doi:10.1093/protein/6.1.37 · Cited by 1,136
Cited by
Galectin-1: a small protein with major functions
Camby, I., Le Mercier, M., Lefranc, F., & Kiss, R. (2006) · Glycobiology · doi:10.1093/glycob/cwl025 · Cited by 893
Glycomimetics versus Multivalent Glycoconjugates for the Design of High Affinity Lectin Ligands
Cecioni, S., Imberty, A., & Vidal, S. (2015) · Chemical Reviews · doi:10.1021/cr500303t · Cited by 544
From lectin structure to functional glycomics: principles of the sugar code
Gabius, H.-J., André, S., Jiménez-Barbero, J., Romero, A., & Solís, D. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.01.005 · Cited by 483
Self-citationWhen Galectins Recognize Glycans: From Biochemistry to Physiology and Back Again
Di Lella, S., Sundblad, V., Cerliani, J. P., Guardia, C. M., Estrin, D. A., Vasta, G. R., & Rabinovich, G. A. (2011) · Biochemistry · doi:10.1021/bi201121m · Cited by 282
HSP70 Multi-Functionality in Cancer
Albakova, Z., Armeev, G. A., Kanevskiy, L. M., Kovalenko, E. I., & Sapozhnikov, A. M. (2020) · Cells · doi:10.3390/cells9030587 · Cited by 265
Metadata
- Authors
- López-Lucendo, M. F., Solís, D., André, S., Hirabayashi, J., Kasai, K.-I., Kaltner, H., Gabius, H.-J., & Romero, A.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2004-10
- Volume
- 343
- Issue
- 4
- Pages
- 957-970
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2137615007
- Cited by
- 295
- References
- 65
- FWCI
- 3.89
- Type
- journal article
- Language
- en
- Open access
- closed
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: Growth-regulatory Human Galectin-1: Crystallographic Characterisation of the Structural Changes Induced by Single-site Mutations and their Impact on the Thermodynamics of Ligand Binding. https://app.cochat.ai/papers/10.1016/j.jmb.2004.08.078
- The paper
- López-Lucendo, M. F., Solís, D., André, S., Hirabayashi, J., Kasai, K.-I., Kaltner, H., Gabius, H.-J., & Romero, A. (2004). Growth-regulatory Human Galectin-1: Crystallographic Characterisation of the Structural Changes Induced by Single-site Mutations and their Impact on the Thermodynamics of Ligand Binding. Journal of Molecular Biology. https://doi.org/10.1016/j.jmb.2004.08.078
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
