Results 31 to 40 of about 1,480,665 (235)

A role for nuclear lamins in nuclear envelope assembly [PDF]

The Journal of Cell Biology, 2001
The molecular interactions responsible for nuclear envelope assembly after mitosis are not well understood. In this study, we demonstrate that a peptide consisting of the COOH-terminal domain of Xenopus lamin B3 (LB3T) prevents nuclear envelope assembly in Xenopus interphase extracts.
Lopez-Soler, Reynold I., Moir, Robert D., Spann, Timothy P., Stick, Reimer, Goldman, Robert D.   +4 more
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Nuclear lamins and laminopathies [PDF]

The Journal of Pathology, 2011
AbstractNuclear lamins are intermediate filament proteins that polymerize to form the nuclear lamina on the inner aspect of the inner nuclear membrane. Long known to be essential for maintaining nuclear structure and disassembling/reassembling during mitosis in metazoans, research over the past dozen years has shown that mutations in genes encoding ...
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Nuclear lamins: building blocks of nuclear architecture [PDF]

Genes & Development, 2002
Nuclear lamins were initially identified as the major components of the nuclear lamina, a proteinaceous layer found at the interface between chromatin and the inner nuclear membrane (Fawcett 1966). Due to their position at the periphery of the nucleus, lamins were originally proposed to support the nuclear envelope and provide anchorage sites for ...
Robert D, Goldman, Yosef, Gruenbaum, Robert D, Moir, Dale K, Shumaker, Timothy P, Spann   +4 more
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Myopathic lamin mutations cause reductive stress and activate the nrf2/keap-1 pathway. [PDF]

PLoS Genetics, 2015
Mutations in the human LMNA gene cause muscular dystrophy by mechanisms that are incompletely understood. The LMNA gene encodes A-type lamins, intermediate filaments that form a network underlying the inner nuclear membrane, providing structural support ...
George Dialynas, Om K Shrestha, Jessica M Ponce, Monika Zwerger, Dylan A Thiemann, Grant H Young, Steven A Moore, Liping Yu, Jan Lammerding, Lori L Wallrath   +9 more
doaj   +1 more source

Modulation of muscle redox and protein aggregation rescues lethality caused by mutant lamins

Redox Biology, 2021
Mutations in the human LMNA gene cause a collection of diseases called laminopathies, which includes muscular dystrophy and dilated cardiomyopathy. The LMNA gene encodes lamins, filamentous proteins that form a meshwork on the inner side of the nuclear ...
Gary S. Coombs, Jose L. Rios-Monterrosa, Shuping Lai, Qiang Dai, Ashley C. Goll, Margaret R. Ketterer, Maria F. Valdes, Nnamdi Uche, Ivor J. Benjamin, Lori L. Wallrath   +9 more
doaj   +1 more source

Fibroblasts lacking nuclear lamins do not have nuclear blebs or protrusions but nevertheless have frequent nuclear membrane ruptures. [PDF]

Proc Natl Acad Sci U S A, 2018
The nuclear lamina, an intermediate filament meshwork lining the inner nuclear membrane, is formed by the nuclear lamins (lamins A, C, B1, and B2). Defects or deficiencies in individual nuclear lamin proteins have been reported to elicit nuclear blebs ...
Chen NY, Kim P, Weston TA, Edillo L, Tu Y, Fong LG, Young SG.   +6 more
europepmc   +2 more sources

Lamins A and C but Not Lamin B1 Regulate Nuclear Mechanics [PDF]

Journal of Biological Chemistry, 2006
Mutations in the nuclear envelope proteins lamins A and C cause a broad variety of human diseases, including Emery-Dreifuss muscular dystrophy, dilated cardiomyopathy, and Hutchinson-Gilford progeria syndrome. Cells lacking lamins A and C have reduced nuclear stiffness and increased nuclear fragility, leading to increased cell death under mechanical ...
Jan, Lammerding, Loren G, Fong, Julie Y, Ji, Karen, Reue, Colin L, Stewart, Stephen G, Young, Richard T, Lee   +6 more
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The Role of Lamins in the Nucleoplasmic Reticulum, a Pleiomorphic Organelle That Enhances Nucleo-Cytoplasmic Interplay

Frontiers in Cell and Developmental Biology, 2022
Invaginations of the nuclear membrane occur in different shapes, sizes, and compositions. Part of these pleiomorphic invaginations make up the nucleoplasmic reticulum (NR), while others are merely nuclear folds.
Merel Stiekema, Merel Stiekema, Frederik Houben, Frederik Houben, Fons Verheyen, Marcel Borgers, Julia Menzel, Martin Meschkat, Marc A. M. J. van Zandvoort, Marc A. M. J. van Zandvoort, Marc A. M. J. van Zandvoort, Marc A. M. J. van Zandvoort, Frans C. S. Ramaekers, Frans C. S. Ramaekers, Jos L. V. Broers, Jos L. V. Broers, Jos L. V. Broers   +16 more
doaj   +1 more source

Glycosylated forms of nuclear lamins

FEBS Letters, 1989
Chromatin and pore complex‐lamina preparations were obtained from pig and chicken tissues, and their proteins were analysed by mono‐ and bidimensional electrophoresis. A glycosylated form of lamin A, recognized by concanavalin A, was shown to be present in at least 3 of the tissues examined.
FERRARO, Anna, EUFEMI, Margherita, CERVONI, Laura, R. Marinetti, TURANO, Carlo   +4 more
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Aging and nuclear organization: lamins and progeria [PDF]

Current Opinion in Cell Biology, 2004
The discoveries of at least eight human diseases arising from mutations in LMNA, which encodes the nuclear A-type lamins, have revealed the nuclear envelope as an organelle associated with a variety of fundamental cellular processes. The most recently discovered diseases associated with LMNA mutations are the premature aging disorders Hutchinson ...
Mounkes, Leslie C., Stewart, Colin L.
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