Results 101 to 110 of about 21,169,060 (256)

Signal transduction by glycophorin A: role of extracellular and cytoplasmic domains in a modulatable process

open access: yesJournal of Cell Biology, 1988
Binding of ligands to the extracellular region of the erythrocyte transmembrane protein glycophorin A induces a decrease in membrane deformability. Since the property of membrane deformability is regulated by the skeletal proteins on the cytoplasmic side
J. Chasis   +3 more
semanticscholar   +1 more source

The role of hydrophobic matching on transmembrane helix packing in cells

open access: yesCell Stress, 2017
Folding and packing of membrane proteins are highly influenced by the lipidic component of the membrane. Here, we explore how the hydrophobic mismatch (the difference between the hydrophobic span of a transmembrane protein region and the hydrophobic ...
Brayan Grau   +6 more
doaj   +1 more source

Atomistic mechanism of transmembrane helix association.

open access: yesPLoS Computational Biology, 2020
Transmembrane helix association is a fundamental step in the folding of helical membrane proteins. The prototypical example of this association is formation of the glycophorin dimer.
Jan Domański   +3 more
doaj   +1 more source

Near-infrared autofluorescence induced by intraplaque hemorrhage and heme degradation as marker for high-risk atherosclerotic plaques [PDF]

open access: yes, 2017
Atherosclerosis is a major cause of mortality and morbidity, which is mainly driven by complications such as myocardial infarction and stroke.
Chen, Yung Chih   +11 more
core   +2 more sources

Glycophorin A Inhibits Lysis by the Complement Attack Phase

open access: yesImmunobiology, 1983
A glycoprotein from human erythrocyte membranes has been found to inhibit lysis of target cells by the attack-phase components C5-C9 from human complement. The inhibiting molecule was purified and identified as glycophorin A. Thus, glycophorin A may have a regulatory function in the lytic complement attack on isologous cells.
H, Brauch, D, Roelcke, U, Rother
openaire   +2 more sources

Large‐Scale Chemoenzymatic Synthesis of a Glycophorin A Tetrasaccharide Motif and Its Analogues

open access: yesAsian Journal of Organic Chemistry, Volume 14, Issue 8, August 2025.
A large‐scale chemoenzymatic method was developed to synthesize natural and modified analogues of the Glycophorin A tetrasaccharide with either C9 or C5 terminal α‐2,3‐sialic acid variants. Selective α‐2,6‐sialylation of galactosamine was achieved by maintaining acetylation of the galactose during the course of enzymatic reactions. The products can aid
Ivan A. Gagarinov   +5 more
wiley   +1 more source

Molecular and clinical characterization of the first Palestinian case of anti-Gerbich

open access: yesAsian Journal of Transfusion Science
Antigens of the Gerbich (Ge) blood group system are highly prevalent proteins that are expressed on the glycophorin C and glycophorin D of the human erythrocytes.
Alex Ballout   +8 more
doaj   +1 more source

Molecular evolution of alleles of the glycophorin A gene

open access: yesLegal Medicine, 2002
Highly-homologous Glycophorin A (GPA), B and E genes are triplicate genes, and involve many subtypes and minor antigens constructing the Miltenberger subsystem. These genes and most of the variants are hypothesized to arise by recombination, because hot spots are located in the gene sequences. By sequencing exons 1-7 and introns 1-3 of standard alleles
Hajime, Mizukami   +3 more
openaire   +3 more sources

Annual Banned‐Substance Review 17th Edition—Analytical Approaches in Human Sports Drug Testing 2023/2024

open access: yesDrug Testing and Analysis, Volume 17, Issue 8, Page 1417-1442, August 2025.
Scenarios of drug exposure and administration as well as detection assays for drugs and methods of sports doping published between 2023 and 2024 are critically reviewed and evaluated in context with the Prohibited List 2024 as established by the World Anti‐Doping Agency.
Mario  Thevis   +2 more
wiley   +1 more source

Proteomic analysis of ERK1/2-mediated human sickle red blood cell membrane protein phosphorylation

open access: yesClinical Proteomics, 2013
Background In sickle cell disease (SCD), the mitogen-activated protein kinase (MAPK) ERK1/2 is constitutively active and can be inducible by agonist-stimulation only in sickle but not in normal human red blood cells (RBCs).
Soderblom Erik J   +6 more
doaj   +1 more source

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