Results 241 to 250 of about 18,236,146 (293)

Exploratory Changes in Surfactant Protein D During Intermittent Hypoxia and Modulation by Galectin-3 Inhibition. [PDF]

Adv Respir Med
Al-Anazi S, Alshawakir YA, Habib SS, Gad H, Alotaibi AF, Aljasham AT, Althakfi WA, Mekhtiche MA, Al-Masri AA.   +8 more
europepmc   +1 more source

Analysis of Galectin-3 in Differentiating Non-malignant and Malignant Nodular Thyroid Lesions. [PDF]

Cureus
J S, Es K, Srinivasan S.
europepmc   +1 more source

Galectin-3 promotes FBXL5-dependent ubiquitination and degradation of YAP1 to constrain colorectal cancer growth. [PDF]

Front Immunol
Zeng X, Mak TK, Li N, Wang J, Huang Z, Lu W.   +5 more
europepmc   +1 more source

Galectin-3 Binds to the Allosteric Site and Activates Integrins αvβ3, αIIbβ3, and α5β1, and Lactose Inhibits This Activation. [PDF]

Biomolecules
Takada YK, Wan YY, Takada Y.
europepmc   +1 more source

γ-Tocotrienol inhibition of galectin-3 expression, distribution and oligomerization in highly metastatic breast cancer cells. [PDF]

Sci Rep
Grazier JJ, Sylvester PW.
europepmc   +1 more source

Expression and Significance of Galectin-3 and Galectin-3 Binding Proteins in Preeclampsia

Advances in Clinical Medicine
openaire   +1 more source

A novel circulating osteoimmunological signature for diagnosis: integrating CXCL2, FYN, galectin-3, and STING in postmenopausal osteoporosis. [PDF]

Front Physiol
Ma S, Yao Q, Bao X, Li Y.
europepmc   +1 more source

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Galectin-3 and metastasis

Glycoconjugate Journal, 2002
Galectin-3, a 31 kDa member of the beta-galactoside-binding proteins, is an intracellular and extracellular lectin which interacts with intracellular glycoproteins, cell surface molecules and extracellular matrix proteins. Galectin-3 is expressed widely in epithelial and immune cells and its expression is correlated with cancer aggressiveness and ...
Yukinori Takenaka, Avraham Raz, Tomoharu Fukumori   +2 more
exaly   +3 more sources

The regulation of inflammation by galectin‐3

Immunological Reviews, 2009
Summary:  Galectin‐3 is a β‐galactoside‐binding animal lectin of appro‐ ximately 30 kDa and is evolutionarily highly conserved. Galectin‐3 is promiscuous, its localization within the tissue micro‐environment may be extracellular, cytoplasmic, or nuclear, and it has a concentration‐dependent ability to be monomeric or form oligomers.
Neil Henderson
exaly   +4 more sources