Ahmed H - Search Results

1

Diversity in recognition of glycans by F-type lectins and galectins: molecular, structural, and biophysical aspects.

Vasta GR, Ahmed H, Bianchet MA, Fernández-Robledo JA, Amzel LM. Vasta GR, et al. Among authors: ahmed h. Ann N Y Acad Sci. 2012 Apr;1253:E14-26. doi: 10.1111/j.1749-6632.2012.06698.x. Ann N Y Acad Sci. 2012. PMID: 22973821 Free PMC article. Review.

2

Galectins: conservation of functionally and structurally relevant amino acid residues defines two types of carbohydrate recognition domains.

Ahmed H, Vasta GR. Ahmed H, et al. Glycobiology. 1994 Oct;4(5):545-8. doi: 10.1093/glycob/4.5.545. Glycobiology. 1994. PMID: 7881167 Review. No abstract available.

3

Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein.

Liao DI, Kapadia G, Ahmed H, Vasta GR, Herzberg O. Liao DI, et al. Among authors: ahmed h. Proc Natl Acad Sci U S A. 1994 Feb 15;91(4):1428-32. doi: 10.1073/pnas.91.4.1428. Proc Natl Acad Sci U S A. 1994. PMID: 8108426 Free PMC article.

4

A novel solid-phase assay for lectin binding. Comparative studies on beta-galactoside-binding S-type lectins from fish, amphibian, and mammalian tissues.

Ahmed H, Fink NE, Vasta GR. Ahmed H, et al. Ann N Y Acad Sci. 1994 Apr 15;712:315-7. doi: 10.1111/j.1749-6632.1994.tb33581.x. Ann N Y Acad Sci. 1994. PMID: 8192337 No abstract available.

5

Elasmobranch and teleost fish contain thiol-dependent beta-galactoside-binding lectins that are cross-reactive with those identified and characterized in bovine spleen.

Ahmed H, Fink NE, Vasta GR. Ahmed H, et al. Ann N Y Acad Sci. 1994 Apr 15;712:318-20. doi: 10.1111/j.1749-6632.1994.tb33582.x. Ann N Y Acad Sci. 1994. PMID: 8192338 No abstract available.

6

Animal lectins as self/non-self recognition molecules. Biochemical and genetic approaches to understanding their biological roles and evolution.

Vasta GR, Ahmed H, Fink NE, Elola MT, Marsh AG, Snowden A, Odom EW. Vasta GR, et al. Among authors: ahmed h. Ann N Y Acad Sci. 1994 Apr 15;712:55-73. doi: 10.1111/j.1749-6632.1994.tb33562.x. Ann N Y Acad Sci. 1994. PMID: 8192353 Review.

7

Animal lectins as cell surface receptors: current status for invertebrate species.

Vasta GR, Ahmed H. Vasta GR, et al. Among authors: ahmed h. Prog Mol Subcell Biol. 1996;17:158-82. doi: 10.1007/978-3-642-80106-8_8. Prog Mol Subcell Biol. 1996. PMID: 8822804 Review. No abstract available.

8

The primary structure and carbohydrate specificity of a beta-galactosyl-binding lectin from toad (Bufo arenarum Hensel) ovary reveal closer similarities to the mammalian galectin-1 than to the galectin from the clawed frog Xenopus laevis.

Ahmed H, Pohl J, Fink NE, Strobel F, Vasta GR. Ahmed H, et al. J Biol Chem. 1996 Dec 20;271(51):33083-94. doi: 10.1074/jbc.271.51.33083. J Biol Chem. 1996. PMID: 8955156 Free article.

When compared to the sequences of known galectins, the B. arenarum galectin exhibited the highest identity (48% for the whole molecule and 77% for the carbohydrate recognition domain (CRD)) with the bovine spleen galectin-1, but surprisingly less identity (38% for the whole molec …

When compared to the sequences of known galectins, the B. arenarum galectin exhibited the highest identity (48% for the whole molecule and 7 …

9

Galectin-1 from bovine spleen: biochemical characterization, carbohydrate specificity and tissue-specific isoform profiles.

Ahmed H, Fink NE, Pohl J, Vasta GR. Ahmed H, et al. J Biochem. 1996 Nov;120(5):1007-19. doi: 10.1093/oxfordjournals.jbchem.a021493. J Biochem. 1996. PMID: 8982870 Free article.

The overall carbohydrate specificity of the bovine galectin-1 isolated from spleen is similar to that of the galectin isolated from heart and to other mammalian galectins that exhibit "conserved" (Type I) carbohydrate recognition domains (CRDs) [Ahmed, H. and Vasta, …

The overall carbohydrate specificity of the bovine galectin-1 isolated from spleen is similar to that of the galectin isolated from heart an …

10

Thermodynamics of bovine spleen galectin-1 binding to disaccharides: correlation with structure and its effect on oligomerization at the denaturation temperature.

Schwarz FP, Ahmed H, Bianchet MA, Amzel LM, Vasta GR. Schwarz FP, et al. Among authors: ahmed h. Biochemistry. 1998 Apr 28;37(17):5867-77. doi: 10.1021/bi9716478. Biochemistry. 1998. PMID: 9558320

The number of contacts at distances <4.0 A between the disaccharide and galectin was determined from the energy-minimized conformation of the complex derived from the X-ray crystallographic structure of the galectin-N-acetyllactosamine complex determined by Liao et al. [Liao, …

The number of contacts at distances <4.0 A between the disaccharide and galectin was determined from the energy-minimized conformation of …

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