Zobrazeno 1 - 10
of 27
pro vyhledávání: '"May M Paing"'
Autor:
May M Paing, Nichole D Salinas, Yvonne Adams, Anna Oksman, Anja TR Jensen, Daniel E Goldberg, Niraj H Tolia
Publikováno v:
eLife, Vol 7 (2018)
Erythrocyte Binding Antigen of 175 kDa (EBA-175) has a well-defined role in binding to glycophorin A (GpA) during Plasmodium falciparum invasion of erythrocytes. However, EBA-175 is shed post invasion and a role for this shed protein has not been def
Externí odkaz:
https://doaj.org/article/0b9e9aa91f4f44c7a8316cff9ae63c1a
Autor:
May M Paing, Niraj H Tolia
Publikováno v:
PLoS Pathogens, Vol 10, Iss 6, p e1004120 (2014)
Externí odkaz:
https://doaj.org/article/a8680a70e7aa41649d1555ff4a84cb34
Publikováno v:
PLoS Pathogens, Vol 9, Iss 5, p e1003390 (2013)
Disrupting erythrocyte invasion by Plasmodium falciparum is an attractive approach to combat malaria. P. falciparum EBA-175 (PfEBA-175) engages the host receptor Glycophorin A (GpA) during invasion and is a leading vaccine candidate. Antibodies that
Externí odkaz:
https://doaj.org/article/6ba0ccc5583442c8813124c3557cd6e0
Autor:
Andrew R. Findlay, May M. Paing, Jil A. Daw, Meade Haller, Rocio Bengoechea, Sara K. Pittman, Shan Li, Feng Wang, Timothy M. Miller, Heather L. True, Tsui-Fen Chou, Conrad C. Weihl
Publikováno v:
Molecular Therapy: Nucleic Acids, Vol 32, Iss , Pp 937-948 (2023)
Dominant missense mutations in DNAJB6, a co-chaperone of HSP70, cause limb girdle muscular dystrophy (LGMD) D1. No treatments are currently available. Two isoforms exist, DNAJB6a and DNAJB6b, each with distinct localizations in muscle. Mutations resi
Externí odkaz:
https://doaj.org/article/98875bfcbb0241d7a450adbfdbc2b0b5
Autor:
Andrew R. Findlay, May M. Paing, Jil A. Daw, Rocio Bengoechea, Sara K. Pittman, Shan Li, Feng Wang, Timothy M. Miller, Heather L. True, Tsui-Fen Chou, Conrad C. Weihl
Dominant missense mutations in DNAJB6, an HSP40 co-chaperone, cause limb girdle muscular dystrophy (LGMD) D1. No treatments are currently available. Two isoforms exist, DNAJB6a and DNAJB6b, each with distinct localizations in muscle. Mutations reside
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::456b308c6f7fd816e0e1cc8af0a89474
https://doi.org/10.1101/2022.11.17.516920
https://doi.org/10.1101/2022.11.17.516920
Plasmodium falciparum erythrocyte-binding antigen 140 (EBA-140) plays a role in tight junction formation during parasite invasion of red blood cells and is a potential vaccine candidate for malaria. Individuals in areas where malaria is endemic posse
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d77db4197938b96fbe938922fb8519fe
https://europepmc.org/articles/PMC6434137/
https://europepmc.org/articles/PMC6434137/
Autor:
Anna Oksman, Yvonne Adams, Anja T. R. Jensen, Daniel E. Goldberg, May M. Paing, Niraj H. Tolia, Nichole D. Salinas
Publikováno v:
eLife
eLife, Vol 7 (2018)
Paing, M M, Salinas, N D, Adams, Y, Oksman, A, Jensen, A TR, Goldberg, D E & Tolia, N H 2018, ' Shed EBA-175 mediates red blood cell clustering that enhances malaria parasite growth and enables immune evasion ', eLife, vol. 7, e43224 . https://doi.org/10.7554/eLife.43224
eLife, Vol 7 (2018)
Paing, M M, Salinas, N D, Adams, Y, Oksman, A, Jensen, A TR, Goldberg, D E & Tolia, N H 2018, ' Shed EBA-175 mediates red blood cell clustering that enhances malaria parasite growth and enables immune evasion ', eLife, vol. 7, e43224 . https://doi.org/10.7554/eLife.43224
Erythrocyte Binding Antigen of 175 kDa (EBA-175) has a well-defined role in binding to glycophorin A (GpA) during Plasmodium falciparum invasion of erythrocytes. However, EBA-175 is shed post invasion and a role for this shed protein has not been def
Autor:
William A. Montagne, Huilan Lin, JoAnn Trejo, May M. Paing, Adriano Marchese, Michael R. Dores
Publikováno v:
Molecular Biology of the Cell
A GPCR ubiquitin-independent MVB/lysosomal sorting pathway is regulated by the adaptor protein complex-3 (AP-3) and ALIX, a noncanonical ESCRT component. AP-3 binds to a PAR1 C-tail–localized, tyrosine-based motif and mediates PAR1 lysosomal degrad
Publikováno v:
Annual Review of Pharmacology and Toxicology. 48:601-629
The heptahelical G protein–coupled receptors (GPCRs) belong to the largest family of cell surface signaling receptors encoded in the human genome. GPCRs signal to diverse extracellular stimuli and control a vast number of physiological responses, m