Results 31 to 40 of about 15,070 (269)

Nuclear lamina strain states revealed by intermolecular force biosensor

open access: yesNature Communications, 2023
Nuclear lamins have been considered an important structural element of the nucleus. The nuclear lamina is thought both to shield DNA from excessive mechanical forces and to transmit mechanical forces onto the DNA.
Brooke E. Danielsson   +8 more
doaj   +1 more source

Regulation of Lipid Metabolism by Lamin in Mutation-Related Diseases

open access: yesFrontiers in Pharmacology, 2022
Nuclear lamins, known as type 5 intermediate fibers, are composed of lamin A, lamin C, lamin B1, and lamin B2, which are encoded by LMNA and LMNB genes, respectively.
Yue Peng   +4 more
doaj   +1 more source

Lamin A, lamin B, and lamin B receptor analogues in yeast. [PDF]

open access: yesThe Journal of cell biology, 1989
Previous studies have shown that turkey erythrocyte lamin B is anchored to the nuclear envelope via a 58-kD integral membrane protein termed p58 or lamin B receptor (Worman H. J., J. Yuan, G. Blobel, and S. D. Georgatos. 1988. Proc. Natl. Acad. Sci. USA. 85:8531-8534). We now identify a p58 analogue in the yeast Saccharomyces cerevisiae.
Georgatos, S. D.   +2 more
openaire   +3 more sources

Chromosome positioning is largely unaffected in lymphoblastoid cell lines containing emerin or A-type lamin mutations [PDF]

open access: yes, 2005
Gene-poor human chromosomes are reproducibly found at the nuclear periphery in proliferating cells. There are a number of inner nuclear envelope proteins that may have roles in chromosome location and anchorage, e.g. emerin and A-type lamins.
Bridger, JM   +3 more
core   +1 more source

Probing the environment of emerin by Enhanced ascorbate peroxidase 2 (APEX2)-mediated proximity labeling. [PDF]

open access: yes, 2020
Emerin is one of the best characterized proteins of the inner nuclear membrane, but can also occur at the level of the endoplasmic reticulum. We now use enhanced ascorbate peroxidase 2 (APEX2) to probe the environment of emerin.
James, C.   +4 more
core   +1 more source

Metabolic Dysfunction in Hutchinson–Gilford Progeria Syndrome

open access: yesCells, 2020
Hutchinson−Gilford Progeria Syndrome (HGPS) is a segmental premature aging disease causing patient death by early teenage years from cardiovascular dysfunction.
Ray Kreienkamp, Susana Gonzalo
doaj   +1 more source

Genome organization in cardiomyocytes expressing mutated A-type lamins

open access: yesFrontiers in Cell and Developmental Biology, 2022
Cardiomyopathy is a myocardial disorder, in which the heart muscle is structurally and functionally abnormal, often leading to heart failure. Dilated cardiomyopathy is characterized by a compromised left ventricular function and contributes significantly
Marie Kervella   +3 more
doaj   +1 more source

Farnesyltransferase inhibitor treatment restores chromosome territory positions and active chromosome dynamics in Hutchinson-Gilford progeria syndrome cells [PDF]

open access: yes, 2011
Copyright @ 2011 Mehta et al.; licensee BioMed Central Ltd. This article has been made available through the Brunel Open Access Publishing Fund. This is an open access article distributed under the terms of the Creative Commons Attribution License ...
Arican, HD   +4 more
core   +2 more sources

The innate immunity adaptor SARM translocates to the nucleus to stabilize lamins and prevent DNA fragmentation in response to pro-apoptotic signaling. [PDF]

open access: yesPLoS ONE, 2013
Sterile alpha and armadillo-motif containing protein (SARM), a highly conserved and structurally unique member of the MyD88 family of Toll-like receptor adaptors, plays an important role in innate immunity signaling and apoptosis.
Chad R Sethman, Jacek Hawiger
doaj   +1 more source

Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore [PDF]

open access: yes, 2004
Resident integral proteins of the inner nuclear membrane (INM) are synthesized as membrane-integrated proteins on the peripheral endoplasmic reticulum (ER) and are transported to the INM throughout interphase using an unknown trafficking mechanism.
Gerace, Larry   +3 more
core   +3 more sources

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