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Galectin 1
Known as:
Galactoside-Binding Lectin 1
, Galectin 1 [Chemical/Ingredient]
, 14 kDa Lectin
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Galectin-1 (135 aa, ~15 kDa) is encoded by the human LGALS1 gene. This protein may play a role in modulating cell-cell and cell-matrix interactions…
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National Institutes of Health
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Related topics
Related topics
17 relations
Apoptosis
Extracellular Matrix
In Blood
LGALS1 gene
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Broader (1)
Galactose Binding Lectin
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2015
Highly Cited
2015
Galectin-1, -3 and -9 Expression and Clinical Significance in Squamous Cervical Cancer
Simone Punt
,
V. Thijssen
,
J. Vrolijk
,
C. D. de Kroon
,
A. Gorter
,
Ekaterina Jordanova
PLoS ONE
2015
Corpus ID: 13539041
Galectins are proteins that bind β-galactoside sugars and provide a new type of potential biomarkers and therapeutic targets in…
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Highly Cited
2000
Highly Cited
2000
Expression of galectin‐1 mRNA correlates with the malignant potential of human gliomas and expression of antisense galectin‐1 inhibits the growth of 9 glioma cells
Kazuko Yamaoka
,
Kazuhiko Mishima
,
Y. Nagashima
,
Akio Asai
,
Y. Sanai
,
Takaaki Kirino
Journal of Neuroscience Research
2000
Corpus ID: 22916554
Although its precise function has not yet been established, galectin‐1 seems to play a role in tumor progression. In this study…
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Highly Cited
2000
Highly Cited
2000
Involvement of CD2 and CD3 in galectin-1 induced signaling in human Jurkat T-cells.
H. Walzel
,
M. Blach
,
J. Hirabayashi
,
K. Kasai
,
J. Brock
Glycobiology
2000
Corpus ID: 6644809
Galectin-1 (gal-1) a member of the mammalian beta-galactoside-binding proteins recognizes preferentially Galbeta1-4GlcNAc…
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Highly Cited
1999
Highly Cited
1999
Galectin-1 specifically modulates TCR signals to enhance TCR apoptosis but inhibit IL-2 production and proliferation.
G. Vespa
,
L. A. Lewis
,
+4 authors
M. Miceli
Journal of Immunology
1999
Corpus ID: 25407687
Galectin-1 is an endogenous lectin expressed by thymic and lymph node stromal cells at sites of Ag presentation and T cell death…
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Highly Cited
1999
Highly Cited
1999
The levels of expression of galectin‐1, galectin‐3, and the Thomsen–Friedenreich antigen and their binding sites decrease as clinical aggressiveness increases in head and neck cancers
G. Choufani
,
N. Nagy
,
+9 authors
S. Hassid
Cancer
1999
Corpus ID: 2615162
The aim of this study was to investigate whether an increase in malignancy level is accompanied by significant modifications of…
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Highly Cited
1995
Highly Cited
1995
Rapid mass spectrometric peptide sequencing and mass matching for characterization of human melanoma proteins isolated by two-dimensional PAGE.
K. Clauser
,
S. Hall
,
+5 authors
A. Burlingame
Proceedings of the National Academy of Sciences…
1995
Corpus ID: 31932917
We report a general mass spectrometric approach for the rapid identification and characterization of proteins isolated by…
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Review
1995
Review
1995
Tissue fibronectin is an endogenous ligand for galectin-1.
Y. Ozeki
,
T. Matsui
,
Yoshinobu Yamamoto
,
Masanori Funahashi
,
J. Hamako
,
K. Titani
Glycobiology
1995
Corpus ID: 34126795
A 14K beta-galactoside-binding lectin (galectin-1) is present in many animal tissues. In a search for endogenous ligands, we…
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Highly Cited
1993
Highly Cited
1993
Galaptin-mediated adhesion of human ovarian carcinoma A121 cells and detection of cellular galaptin-binding glycoproteins.
D. Skrincosky
,
H. Allen
,
R. Bernacki
Cancer Research
1993
Corpus ID: 17343707
Previously, we have shown that galaptin, an endogenous beta-galactoside-binding lectin, is present in extracellular matrix where…
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Highly Cited
1984
Highly Cited
1984
Peanut lectin binding sites in transitional cell carcinoma of the urinary bladder
MD THOMAS P. LEHMAN
,
MD Harry S. Cooper
,
MD S. GRANT MULHOLLAND
,
Ms. Geraldine Ms. Deborah Sedegren
,
Mooney Ms. Mary
,
Molinari
Cancer
1984
Corpus ID: 35801507
Peanut lectin (PNA) binds to D Gal B (1–3) D Gal NAc which is the purported antigenic determinant of the so‐called T blood group…
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Highly Cited
1981
Highly Cited
1981
Preparative nonlytic separation of Lyt2+ and Lyt2− T lymphocytes, functional analyses of the separated cells and demonstration of synergy in graft‐vs.‐host reaction of Lyt2+ and Lyt2− cells
M. Mage
,
Bonnie Mathiesonn
,
+6 authors
Michacl Mage
European Journal of Immunology
1981
Corpus ID: 27955718
A convenient, preparative scale, nonlytic separation of mouse T lymphocytes into Lyt2.2+ and Lyt2.2− populations is reported…
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