Homology modelling and molecular dynamics studies of human placental tissue protein 13 (galectin-13)

B Visegrády, NG Than, F Kilár, B Sümegi… - Protein …, 2001 - academic.oup.com
The primary structure of the newly sequence analysed placental tissue protein 13 (PP13)
was highly homologous to several members of the β-galactoside-binding S-type lectin …

Functional analyses of placental protein 13/galectin‐13

NG Than, E Pick, S Bellyei, A Szigeti… - European Journal of …, 2004 - Wiley Online Library
Placental protein 13 (PP13) was cloned from human term placenta. As sequence analyses,
alignments and computational modelling showed its conserved structural and functional …

[HTML][HTML] Galectin-13, a different prototype galectin, does not bind β-galacto-sides and forms dimers via intermolecular disulfide bridges between Cys-136 and Cys-138

J Su, Y Wang, Y Si, J Gao, C Song, L Cui, R Wu… - Scientific reports, 2018 - nature.com
Abstract During pregnancy, placental protein-13 (galectin-13) is highly expressed in the
placenta and fetal tissue, and less so in maternal serum that is related to pre-eclampsia. To …

An integrated computational analysis of the structure, dynamics, and ligand binding interactions of the human galectin network

CMA Guardia, DF Gauto, S Di Lella… - Journal of chemical …, 2011 - ACS Publications
Galectins, a family of evolutionarily conserved animal lectins, have been shown to modulate
signaling processes leading to inflammation, apoptosis, immunoregulation, and …

Structure–function studies of galectin‐14, an important effector molecule in embryology

Y Si, Y Li, T Yang, X Li, GJ Ayala, KH Mayo… - The FEBS …, 2021 - Wiley Online Library
The expression of prototype galectin‐14 (Gal‐14) in human placenta is higher than any
other galectin, suggesting that it may play a role in fetal development and regulation of …

Inhibition mechanism of human galectin‐7 by a novel galactose‐benzylphosphate inhibitor

G Masuyer, T Jabeen, CT Öberg, H Leffler… - The FEBS …, 2012 - Wiley Online Library
Galectins are involved in many cellular processes due to their ability to bind carbohydrates.
Understanding their functions has shown the necessity for potent and specific galectin …

Computational studies of human galectin-1: role of conserved tryptophan residue in stacking interaction with carbohydrate ligands

C Meynier, F Guerlesquin, P Roche - Journal of Biomolecular …, 2009 - Taylor & Francis
Galectins belong to the family of glycan-binding proteins, defined by at least one conserved
carbohydrate-recognition domain with a highly conserved amino acid sequence and affinity …

Structural Basis for the Recognition of Carbohydrates by Human Galectin-7,

DD Leonidas, EH Vatzaki, H Vorum, JE Celis… - Biochemistry, 1998 - ACS Publications
Knowledge about carbohydrate recognition domains of galectins, formerly known as S-type
animal lectins, is important in understanding their role (s) in cell− cell interactions. Here we …

X‐ray structure of a protease‐resistant mutant form of human galectin‐8 with two carbohydrate recognition domains

H Yoshida, S Yamashita, M Teraoka, A Itoh… - The FEBS …, 2012 - Wiley Online Library
Galectin‐8 is a tandem‐repeat‐type β‐galactoside‐specific animal lectin possessing N‐
terminal and C‐terminal carbohydrate recognition domains (N‐CRD and C‐CRD …

[HTML][HTML] Expression, regulation, and functions of the galectin-16 gene in human cells and tissues

JD Kaminker, AV Timoshenko - Biomolecules, 2021 - mdpi.com
Galectins comprise a family of soluble β-galactoside-binding proteins, which regulate a
variety of key biological processes including cell growth, differentiation, survival, and death …