A. Leppänen

发表

A Novel Glycosulfopeptide Binds to P-selectin and Inhibits Leukocyte Adhesion to P-selectin*

R. Cummings, P. Mehta, T. Ju, 1999, The Journal of Biological Chemistry.

Distinct molecular and cellular contributions to stabilizing selectin-mediated rolling under flow

Cheng Zhu, Richard D. Cummings, Rodger P. McEver, 2002, The Journal of cell biology.

Model Glycosulfopeptides from P-selectin Glycoprotein Ligand-1 Require Tyrosine Sulfation and a Core 2-branched O-Glycan to Bind to L-selectin*

R. Cummings, V. Otto, R. McEver, 2003, Journal of Biological Chemistry.

Binding of Glycosulfopeptides to P-selectin Requires Stereospecific Contributions of Individual Tyrosine Sulfate and Sugar Residues*

R. Cummings, R. McEver, A. Leppänen, 2000, The Journal of Biological Chemistry.

Glycosulfopeptides modeled on P‐selectin glycoprotein ligand‐1 inhibit P‐selectin‐dependent leukocyte rolling in vivo

R. Cummings, P. Hellewell, R. McEver, 2002, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Enzyme‐assisted synthesis of a bivalent high‐affinity dodecasaccharide inhibitor of mouse gamete adhesion The length of the chains carrying distal α1,3‐bonded galactose residues is critical

H. Maaheimo, J. Taskinen, A. Seppo, 1995, FEBS letters.

Human L-selectin preferentially binds synthetic glycosulfopeptides modeled after endoglycan and containing tyrosine sulfate residues and sialyl Lewis x in core 2 O-glycans.

R. Cummings, N. Kalkkinen, V. Parviainen, 2010, Glycobiology.

Glycoforms of human endothelial CD34 that bind L-selectin carry sulfated sialyl Lewis x capped O- and N-glycans.

R. Cummings, Kari-Pekka Skarp, R. Renkonen, 2009, Blood.

Replacing a Lectin Domain Residue in L-selectin Enhances Binding to P-selectin Glycoprotein Ligand-1 but Not to 6-Sulfo-sialyl Lewis x*

R. Cummings, N. Bovin, P. Mehta, 2008, Journal of Biological Chemistry.

Oligo-N-acetyllactosaminoglycans bearing Galβ1-4(Fucα1-3)GlcNAc sequences reveal lower affinities than their nonfucosylated, or α(1-2) fucosylated counterparts for immobilized wheat germ agglutinin

K. Hård, H. Maaheimo, A. Seppo, 1991, Glycoconjugate Journal.

Structurally Distinct Requirements for Binding of P-selectin Glycoprotein Ligand-1 and Sialyl Lewis x to Anaplasma phagocytophilum and P-selectin*

R. Cummings, E. Fikrig, M. Akkoyunlu, 2003, Journal of Biological Chemistry.

Discordant expression of selectin ligands and sialyl Lewis x-related epitopes on murine myeloid cells.

R. Cummings, R. McEver, V. Ramachandran, 2002, Blood.

Glycosulfopeptides with O-Glycans Containing Sialylated and Polyfucosylated Polylactosamine Bind with Low Affinity to P-selectin*

R. Cummings, L. Penttilä, O. Renkonen, 2002, The Journal of Biological Chemistry.

Selectin ligands promote ultrasound contrast agent adhesion under shear flow.

S. Acton, R. Cummings, R. Cummings, 2006, Molecular pharmaceutics.

Human serum contains a novel beta 1,6-N-acetylglucosaminyltransferase activity that is involved in midchain branching of oligo (N-acetyllactosaminoglycans).

A. Seppo, L. Penttilä, R. Niemelä, 1991, Biochemistry.

Bi-antennary oligo-(N-acetyllactosamino)glycans of I-type are galactosylated preferentially at the GlcNAcβ1-6Gal linked arms by α1,3-galactosyltransferase of bovine thymus

J. Wieruszeski, H. Maaheimo, A. Seppo, 1994, Glycoconjugate Journal.

Antibody responses to the fucosylated LacdiNAc glycan antigen in Schistosoma mansoni-infected mice and expression of the glycan among schistosomes.

R. Cummings, R D Cummings, A. Leppänen, 2000, Experimental parasitology.

N-Acetyllactosaminooligosaccharides that contain the β-d-GlcpNAc-(1→6)-d-Gal or β-d-GlcpNAc-(1→6)-d-GalNAc sequences reveal reduction-sensitive affinites for wheat germ agglutinin

H. Maaheimo, A. Seppo, L. Penttilä, 1991 .

Single mid-chain GlcNAcβ1-6Galβ1-4R sequences of linear oligosaccharides are resistant to endo-β-galactosidase ofBacteroides fragilis

L. Penttilä, R. Niemelä, O. Renkonen, 1991, Glycoconjugate Journal.

Construction of linear GlcNAcβ1-6Galβ1-OR type oligosaccharides by partial cleavage of GlcNAcβ1-3(GlcNAcβ1-6)Galβ1-OR sequences with jack bean β-N-acetylhexosaminidase

H. Maaheimo, A. Seppo, L. Penttilä, 1991, Glycoconjugate Journal.

Elongation of both branches of biantennary backbones of oligo-(N-acetyllactosamino)glycans by human serum (1----3)-N-acetyl-beta-D- glucosaminyltransferase.

H. Maaheimo, A. Seppo, L. Penttilä, 1992, Carbohydrate research.

Glycoproteins of human teratocarcinoma cells (PA1) carry both anomers of O-glycosyl-linked D-galactopyranosyl-(1----3)-2-acetamido- 2-deoxy-alpha-D-galactopyranosyl group.

O. Renkonen, A. Leppänen, K. Puro, 1986, Carbohydrate research.

Dimeric Galectin-1 Binds with High Affinity to α2,3-Sialylated and Non-sialylated Terminal N-Acetyllactosamine Units on Surface-bound Extended Glycans*

S. Stowell, R. Cummings, O. Blixt, 2005, Journal of Biological Chemistry.

The linear tetrasaccharide, Galβ1-4GlcNAcβ1-6Galβ1-4GlcNAc, isolated from radiolabeled teratocarcinoma poly-N-acetyllactosaminoglycan resists the action ofE. freundii endo-β-galactosidase

L. Penttilä, R. Niemelä, O. Renkonen, 2005, Glycoconjugate Journal.

Purification and Characterization of UDP-GlcNAc:Galβ1–4GlcNAcβ1–3*Galβ1–4Glc(NAc)-R(GlcNAc to *Gal) β1,6N-Acetylglucosaminyltransferase from Hog Small Intestine*

Y. Tano, N. Taniguchi, T. Taguchi, 1998, The Journal of Biological Chemistry.

Biosynthesis of Branched Polylactosaminoglycans

E. Lehtonen, H. Maaheimo, A. Leppänen, 1998, The Journal of Biological Chemistry.

The β1,6‐GlcNAc transferase activity present in hog gastric mucosal microsomes catalyses site‐specific branch formation on a long polylactosamine backbone

H. Maaheimo, L. Penttilä, O. Renkonen, 1997, FEBS letters.

Site-directed enzymatic α-(1 → 3)-l-fucosylation of the tetrasaccharide Galβ(1 → 4)GlcNAcβ(1 → 3)Galβ(1 → 4)GlcNAc at the distal N-acetyllactosamine unit

H. Maaheimo, R. Niemelä, O. Renkonen, 1995 .

Enzymatic in vitro synthesis of radiolabeled pentasaccharides GlcNAcβ1-3(Galβ1-4GlcNAcβl-6)Galβ1-4GlcNAc/Glc and the isomeric Galβ1-4GlcNAcβ1-3(GlcNAcβ1-6)Galβ1-4GlcNAc/Glc

J. Suopanki, H. Maaheimo, A. Seppo, 1992 .

Examination of whole cell galectin binding by solid phase and flow cytometric analysis.

S. Stowell, R. Cummings, C. Arthur, 2015, Methods in molecular biology.

Fluorescence-based solid-phase assays to study glycan-binding protein interactions with glycoconjugates.

R. Cummings, A. Leppänen, 2010, Methods in enzymology.

Human L-selectin preferentially binds synthetic glycosulfopeptides modeled after endoglycan and containing tyrosine sulfate residues and sialyl Lewis x in core 2 O-glycans.

R. Cummings, N. Kalkkinen, V. Parviainen, 2010, Glycobiology.