Zobrazeno 1 - 10
of 102
pro vyhledávání: '"J. P. Luzio"'
Autor:
Dick J. H. van den Boomen, Agata Sienkiewicz, Ilana Berlin, Marlieke L. M. Jongsma, Daphne M. van Elsland, J. Paul Luzio, Jacques J. C. Neefjes, Paul J. Lehner
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-18 (2020)
Lysosomes play an important role in cellular LDL-cholesterol uptake. Here, the authors perform a genome-wide genetic screen for cholesterol regulators and identify C18orf8 as a conserved subunit of a trimeric Rab7 GEF that controls LDL trafficking an
Externí odkaz:
https://doaj.org/article/5ea86788f5ff452193f198cb9ba6bdd4
Autor:
Harriet Crawley-Snowdon, Ji-Chun Yang, Nathan R. Zaccai, Luther J. Davis, Lena Wartosch, Emily K. Herman, Nicholas A. Bright, James S. Swarbrick, Brett M. Collins, Lauren P. Jackson, Matthew N. J. Seaman, J. Paul Luzio, Joel B. Dacks, David Neuhaus, David J. Owen
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
VARP is bound to endosomes and functions as a protein:protein interaction platform. Here, the authors present the NMR structure of the complex between the retromer subunit VPS29 and a VARP Zn-fingernail microdomain that is structurally distinct from
Externí odkaz:
https://doaj.org/article/5179c14a82ba4080bfd7a8f14df6270f
Autor:
James R. Edgar, Anita K. Ho, Matilde Laurá, Rita Horvath, Mary M. Reilly, J. Paul Luzio, Rhys C. Roberts
Publikováno v:
Acta Neuropathologica Communications, Vol 8, Iss 1, Pp 1-16 (2020)
Abstract Autosomal dominant mutations in LITAF are responsible for the rare demyelinating peripheral neuropathy, Charcot–Marie–Tooth disease type 1C (CMT1C). The LITAF protein is expressed in many human cell types and we have investigated the con
Externí odkaz:
https://doaj.org/article/275f11a6cd874fd9bce07eb7b28c4413
Publikováno v:
Acta Médica Portuguesa, Vol 11, Iss 4 (1998)
A retrospective study was made of 83 diabetic patients admitted to the Department of Internal Medicine between January 1986 and December 1993, with acute intercurrence of the disease. The authors considered some clinical features (age, type and frequ
Externí odkaz:
https://doaj.org/article/df7caa1cb77146d49ab2ae66bb55a384
Publikováno v:
Acta Médica Portuguesa, Vol 10, Iss 12 (1997)
Female patient, 21 years of age, with diabetes mellitus type I, admitted due to progressive weight loss, with a recent history of impaired glycemic control, ketosis and amenorrhea for 12 months. Studies were conducted in order to exclude an endocrine
Externí odkaz:
https://doaj.org/article/64fdcbef35e34aba8c503981fd81d000
Autor:
Barbara M. Mullock, Margaret R. Lindsay, Paul R. Pryor, David E. James, J P Luzio, Robert C. Piper
Publikováno v:
Biochemical Society Transactions. 29:476-480
Delivery of endocytosed macromolecules to lysosomes occurs by means of direct fusion of late endosomes with lysosomes. This has been formally demonstrated in a cell-free content mixing assay using late endosomes and lysosomes from rat liver. There is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fae50050a4421f478f40f95fc609d6ee
https://doi.org/10.1042/bst0290476
https://doi.org/10.1042/bst0290476
Publikováno v:
Proceedings of the National Academy of Sciences. 98:3982-3987
Langerhans cells are a subset of dendritic cells (DCs) found in the human epidermis with unique morphological and molecular properties that enable their function as “sentinels” of the immune system. DCs are pivotal in the initiation and regulatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2588ce449fcebc589cc6caf45f3e5e8e
https://doi.org/10.1073/pnas.071477498
https://doi.org/10.1073/pnas.071477498
Publikováno v:
Biochemical Journal. 345:287-296
Endolyn (endolyn-78) is a membrane protein found in lysosomal and endosomal compartments of mammalian cells. Unlike ‘classical’ lysosomal membrane proteins, such as lysosome-associated membrane protein (lamp)-1, it is also present in a subapical
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bb8420191868d7d13f65668013b72237
https://doi.org/10.1042/bj3450287
https://doi.org/10.1042/bj3450287
Publikováno v:
Molecular Biology of the Cell. 9:1107-1122
Previous studies have shown that when the cytosolic domains of the type I membrane proteins TGN38 and lysosomal glycoprotein 120 (lgp120) are added to a variety of reporter molecules, the resultant chimeric molecules are localized to the trans-Golgi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57fb0028e8255c0263a505912d3a6cec
https://doi.org/10.1091/mbc.9.5.1107
https://doi.org/10.1091/mbc.9.5.1107
Publikováno v:
Molecular Membrane Biology. 15:133-139
TGN38 is a heavily glycosylated, type I integral membrane protein which is predominantly localized to the trans Golgi network (TGN), but which constitutively traffics between the TGN and the cell surface. The trafficking of TGN38 has been extensively
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f56c1f474b1dfd7672804950906149a
https://doi.org/10.3109/09687689809074524
https://doi.org/10.3109/09687689809074524