Výsledky vyhledávání - "Morris F. Manolson"

Akademický článek

The Human Mutation K237_V238del in a Putative Lipid Binding Motif within the V-ATPase a2 Isoform Suggests a Molecular Mechanism Underlying Cutis Laxa

Autor: Anh Chu, Yeqi Yao, Miroslawa Glibowicka, Charles M. Deber, Morris F. Manolson

Publikováno v: International Journal of Molecular Sciences, Vol 25, Iss 4, p 2170 (2024)

Vacuolar ATPases (V-ATPases), proton pumps composed of 16 subunits, are necessary for a variety of cellular functions. Subunit “a” has four isoforms, a1–a4, each with a distinct cellular location. We identified a phosphoinositide (PIP) interact

Externí odkaz: https://doaj.org/article/4d7705eff4974f0299322ffff43f505d

Zobrazit plný text záznamu

Plný text ve formátu HTML

Akademický článek

Characterization of a PIP Binding Site in the N-Terminal Domain of V-ATPase a4 and Its Role in Plasma Membrane Association

Autor: Anh Chu, Yeqi Yao, Golam T. Saffi, Ji Hyun Chung, Roberto J. Botelho, Miroslawa Glibowicka, Charles M. Deber, Morris F. Manolson

Publikováno v: International Journal of Molecular Sciences, Vol 24, Iss 5, p 4867 (2023)

Vacuolar ATPases (V-ATPases) are multi-subunit ATP-dependent proton pumps necessary for cellular functions, including pH regulation and membrane fusion. The evidence suggests that the V-ATPase a-subunit’s interaction with the membrane signaling lip

Externí odkaz: https://doaj.org/article/36bf4037a564495d8d0aeeeefd4a8e81

Zobrazit plný text záznamu

Plný text ve formátu HTML

Akademický článek

Advances in understanding N-glycosylation structure, function, and regulation in health and disease

Autor: Sally Esmail, Morris F. Manolson

Publikováno v: European Journal of Cell Biology, Vol 100, Iss 7, Pp 151186- (2021)

N-linked glycosylation is a post-translational modification crucial for membrane protein folding, stability and other cellular functions. Alteration of membrane protein N-glycans is implicated in wide range of pathological conditions including cancer

Externí odkaz: https://doaj.org/article/2b42ae9b895c4685aa4a5dd7be8c7d9c

Zobrazit plný text záznamu

Akademický článek

The V-ATPase a3 Subunit: Structure, Function and Therapeutic Potential of an Essential Biomolecule in Osteoclastic Bone Resorption

Autor: Anh Chu, Ralph A. Zirngibl, Morris F. Manolson

Publikováno v: International Journal of Molecular Sciences, Vol 22, Iss 13, p 6934 (2021)

This review focuses on one of the 16 proteins composing the V-ATPase complex responsible for resorbing bone: the a3 subunit. The rationale for focusing on this biomolecule is that mutations in this one protein account for over 50% of osteopetrosis ca

Externí odkaz: https://doaj.org/article/426f663cf2cb410f91b5f095adc4c359

Zobrazit plný text záznamu

Plný text ve formátu HTML

Novel c.G630A TCIRG1 mutation causes aberrant splicing resulting in an unusually mild form of autosomal recessive osteopetrosis

Autor: Morris F. Manolson, Yeqi Yao, Lucie Dupuis, Irina Voronov, Roberto Mendoza-Londono, Andrew Wang, Joerg Krueger, Ralph A Zirngibl

Publikováno v: Journal of Cellular Biochemistry. 120:17180-17193

Autosomal recessive osteopetrosis (ARO) is a severe genetic bone disease characterized by high bone density due to mutations that affect formation or function of osteoclasts. Mutations in the a3 subunit of the vacuolar-type H+ -ATPase (encoded by T-c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::976a297014bb1e606240f9bf57a0ba5c
https://doi.org/10.1002/jcb.28979

Zobrazit plný text záznamu

Molecular mechanisms of cutis laxa– and distal renal tubular acidosis–causing mutations in V-ATPase a subunits, ATP6V0A2 and ATP6V0A4

Autor: Morris F. Manolson, Yeqi Yao, Joo Wan Kim, Reinhart A. F. Reithmeier, Norbert Kartner, Sally Esmail

Publikováno v: Journal of Biological Chemistry. 293:2787-2800

The a subunit is the largest of 15 different subunits that make up the vacuolar H(+)-ATPase (V-ATPase) complex, where it functions in proton translocation. In mammals, this subunit has four paralogous isoforms, a1–a4, which may encode signals for t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab9540f7b91ffc22f5c22c9964f4ca46
https://doi.org/10.1074/jbc.m117.818872

Zobrazit plný text záznamu

Purification of active human vacuolar H+-ATPase in native lipid-containing nanodiscs

Autor: Stephan Wilkens, Morris F. Manolson, Yeqi Yao, Rebecca A. Oot

Publikováno v: The Journal of Biological Chemistry

Vacuolar H+-ATPases (V-ATPases) are large, multisubunit proton pumps that acidify the lumen of organelles in virtually every eukaryotic cell and in specialized acid-secreting animal cells, the enzyme pumps protons into the extracellular space. In hig

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0873f6ad396a93ac64148b542c7cd30b
https://doi.org/10.1016/j.jbc.2021.100964

Zobrazit plný text záznamu

N‐linked glycosylation of a subunit isoforms is critical for vertebrate vacuolar H + ‐ATPase (V‐ATPase) biosynthesis

Autor: Morris F. Manolson, Joo Wan Kim, Yeqi Yao, Norbert Kartner, Reinhart A. F. Reithmeier, Sally Esmail

Publikováno v: Journal of Cellular Biochemistry. 119:861-875

The a subunit of the V0 membrane-integrated sector of human V-ATPase has four isoforms, a1-a4, with diverse and crucial functions in health and disease. They are encoded by four conserved paralogous genes, and their vertebrate orthologs have position

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1b7731de4174fe24a89d44531b154234
https://doi.org/10.1002/jcb.26250

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání