- 同
- CD235A
WordNet
- the 1st letter of the Roman alphabet (同)a
- the blood group whose red cells carry the A antigen (同)type_A, group A
PrepTutorEJDIC
- answer / ampere
- arsenicの化学記号
UpToDate Contents
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English Journal
- Assessment of normal erythropoiesis by flow cytometry: important considerations for specimen preparation.
- Wangen JR1, Eidenschink Brodersen L, Stolk TT, Wells DA, Loken MR.Author information 1Hematologics Inc., Seattle, WA, USA.AbstractINTRODUCTION: The extension of quantitative flow cytometric studies to the erythroid lineage in patients with suspected myelodysplastic syndrome has prompted a reassessment of cell surface antigen expression during normal erythropoiesis. Erythropoiesis in normal and pathologic bone marrows was studied to determine the expected antigenic relationships of maturing erythroid cells.
- International journal of laboratory hematology.Int J Lab Hematol.2014 Apr;36(2):184-96. doi: 10.1111/ijlh.12151. Epub 2013 Oct 3.
- INTRODUCTION: The extension of quantitative flow cytometric studies to the erythroid lineage in patients with suspected myelodysplastic syndrome has prompted a reassessment of cell surface antigen expression during normal erythropoiesis. Erythropoiesis in normal and pathologic bone marrows was studi
- PMID 24118926
- Glycophorin C (CD236R) mediates vivax malaria parasite rosetting to normocytes.
- Lee WC1, Malleret B, Lau YL, Mauduit M, Fong MY, Cho JS, Suwanarusk R, Zhang R, Albrecht L, Costa FT, Preiser P, McGready R, Renia L, Nosten F, Russell B.Author information 1Department of Parasitology, Faculty of Medicine, University of Malaya, Kuala Lumpur, Malaysia;AbstractRosetting phenomenon has been linked to malaria pathogenesis. While rosetting occurs in all causes of human malaria, most data on this subject has been derived from Plasmodium falciparum. Here we investigate the function and factors affecting rosette formation in Plasmodium vivax. To achieve this, we utilised a range of novel ex vivo protocols to study fresh and cryopreserved P. vivax (n=135) and P. falciparum (n=77) isolates from Thailand. Rosetting is more common in vivax than falciparum malaria, both in terms of incidence in patient samples and percentage of infected erythrocytes forming rosettes. Rosetting to P. vivax asexual and sexual stages was evident 20 hrs post reticulocyte invasion, reaching a plateau after 30 hrs. Host ABO blood group, reticulocyte count and parasitemia were not correlated with P. vivax rosetting. Importantly, mature erythrocytes (normocytes) rather than reticulocytes preferentially form rosetting complexes, indicating this process is unlikely to directly facilitate merozoite invasion. While antibodies against host erythrocyte receptors CD235a and CD35 had no effect; Fab against the BRIC 4 region of CD236R significantly inhibited rosette formation. Rosetting assays using CD236R knock down normocytes derived from hematopoietic stem cells, further supports the role of Glycophorin C as a receptor in P. vivax rosette formation.
- Blood.Blood.2014 Mar 20. [Epub ahead of print]
- Rosetting phenomenon has been linked to malaria pathogenesis. While rosetting occurs in all causes of human malaria, most data on this subject has been derived from Plasmodium falciparum. Here we investigate the function and factors affecting rosette formation in Plasmodium vivax. To achieve this, w
- PMID 24652986
- A frequent, GxxxG-mediated, transmembrane association motif is optimized for the formation of interhelical Cα-H hydrogen bonds.
- Mueller BK1, Subramaniam S, Senes A.Author information 1Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706.AbstractCarbon hydrogen bonds between Cα-H donors and carbonyl acceptors are frequently observed between transmembrane helices (Cα-H···O=C). Networks of these interactions occur often at helix-helix interfaces mediated by GxxxG and similar patterns. Cα-H hydrogen bonds have been hypothesized to be important in membrane protein folding and association, but evidence that they are major determinants of helix association is still lacking. Here we present a comprehensive geometric analysis of homodimeric helices that demonstrates the existence of a single region in conformational space with high propensity for Cα-H···O=C hydrogen bond formation. This region corresponds to the most frequent motif for parallel dimers, GASright, whose best-known example is glycophorin A. The finding suggests a causal link between the high frequency of occurrence of GASright and its propensity for carbon hydrogen bond formation. Investigation of the sequence dependency of the motif determined that Gly residues are required at specific positions where only Gly can act as a donor with its "side chain" Hα. Gly also reduces the steric barrier for non-Gly amino acids at other positions to act as Cα donors, promoting the formation of cooperative hydrogen bonding networks. These findings offer a structural rationale for the occurrence of GxxxG patterns at the GASright interface. The analysis identified the conformational space and the sequence requirement of Cα-H···O=C mediated motifs; we took advantage of these results to develop a structural prediction method. The resulting program, CATM, predicts ab initio the known high-resolution structures of homodimeric GASright motifs at near-atomic level.
- Proceedings of the National Academy of Sciences of the United States of America.Proc Natl Acad Sci U S A.2014 Mar 11;111(10):E888-95. doi: 10.1073/pnas.1319944111. Epub 2014 Feb 25.
- Carbon hydrogen bonds between Cα-H donors and carbonyl acceptors are frequently observed between transmembrane helices (Cα-H···O=C). Networks of these interactions occur often at helix-helix interfaces mediated by GxxxG and similar patterns. Cα-H hydrogen bonds have been hypothesized to be imp
- PMID 24569864
Japanese Journal
- Predictions of Tertiary Structures of α-Helical Membrane Proteins by Replica-Exchange Method with Consideration of Helix Deformations
- Journal of the Physical Society of Japan 84(8), 084802-1-12, 2015-07-29
- NAID 40020552641
- 破砕赤血球を認めた骨髄異形成関連変化と赤芽球過形成を伴う急性骨髄性白血病の1例
Related Links
- Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of ...
- 赤芽球から成熟赤血球まで広く分布する Glycophorin A と特異的に反応します。赤芽球性白血病の検索に非常に有用な抗体 ... Disclaimer: Due to variances among color computer monitors, the colors you see on your screen may not be ...
Related Pictures
★リンクテーブル★
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- 英
- [[]]
- 同
- glycophorin A
- 関
- [[]]
- 同
- glycophorin A
[★]
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- 関
- adenoviral、adenovirus