Results 71 to 80 of about 1,727,162 (300)

A role for Tctex-1 (DYNLT1) in controlling primary cilium length [PDF]

open access: yes, 2011
The microtubule motor complex cytoplasmic dynein is known to be involved in multiple processes including endomembrane organization and trafficking, mitosis, and microtubule organization.
MacCarthy-Morrogh, LJ   +3 more
core   +2 more sources

Genomic structure of the mouse A‐type lamin gene locus encoding somatic and germ cell‐specific lamins [PDF]

open access: yesFEBS Letters, 1995
Mouse A‐type lamin genes were isolated. Structural analyses revealed that all the three known mouse A‐type lamins (A, C and C2) were coded in a single genomic locus in a 22 kilobase DNA segment. The three lamins were coded in 12, 10 and 10 exons for A, C and C2, respectively, and shared 8 exons among them.
Nakajima, Noboru, Abe, Kenji
openaire   +2 more sources

Lamin A/C Haploinsufficiency Modulates the Differentiation Potential of Mouse Embryonic Stem Cells [PDF]

open access: yes, 2013
BACKGROUND: Lamins are structural proteins that are the major determinants of nuclear architecture and play important roles in various nuclear functions including gene regulation and cell differentiation.
Chaturvedi, P.   +4 more
core   +2 more sources

Nurturing the genome [PDF]

open access: yesNucleus, 2010
A-type lamins provide a scaffold for tethering chromatin and protein complexes regulating nuclear structure and function. Interest in lamins increased after mutations in the LMNA gene were found to be associated with a variety of human disorders termed laminopathies. These include muscular dystrophy, cardiomyopathy, lipodystrophy, peripheral neuropathy
Gonzalez-Suarez, Ignacio   +1 more
openaire   +3 more sources

Lamin A, Chromatin and FPLD2: Not Just a Peripheral Ménage-à-Trois

open access: yesFrontiers in Cell and Developmental Biology, 2018
At the nuclear periphery, the genome is anchored to A- and B-type nuclear lamins in the form of heterochromatic lamina-associated domains. A-type lamins also associate with chromatin in the nuclear interior, away from the peripheral nuclear lamina.
Nolwenn Briand   +8 more
doaj   +1 more source

Lamin post-translational modifications: emerging toggles of nuclear organization and function.

open access: yesTIBS -Trends in Biochemical Sciences. Regular ed, 2021
Nuclear lamins are ancient type V intermediate filaments with diverse functions that include maintaining nuclear shape, mechanosignaling, tethering and stabilizing chromatin, regulating gene expression, and contributing to cell cycle progression. Despite
Laura A Murray-Nerger, I. Cristea
semanticscholar   +1 more source

Cardiovascular Progerin Suppression and Lamin A Restoration Rescue Hutchinson-Gilford Progeria Syndrome

open access: yesCirculation, 2021
Supplemental Digital Content is available in the text. Background: Hutchinson-Gilford progeria syndrome (HGPS) is a rare disorder characterized by premature aging and death mainly because of myocardial infarction, stroke, or heart failure. The disease is
A. Sánchez-López   +17 more
semanticscholar   +1 more source

Nuclear lamin A in rotator cuff tear margin tenocytes: an antiapoptotic and cell mechanostat factor

open access: yesJournal of Orthopaedic Surgery and Research, 2021
Background The network of intermediate filament proteins underlying the inner nuclear membrane forms the nuclear lamin. A- and B-type lamins are the major components of the nuclear lamina. Lamins function in many nuclear activities.
Stefano Gumina   +6 more
doaj   +1 more source

A Rare Mutation in LMNB2 Associated with Lipodystrophy Drives Premature Cell Senescence

open access: yesCells, 2021
Many proteins are causative for inherited partial lipodystrophies, including lamins, the essential constituents of the nuclear envelope scaffold called the lamina.
Alice-Anaïs Varlet   +10 more
doaj   +1 more source

Polyphyly of nuclear lamin genes indicates an early eukaryotic origin of the metazoan-type intermediate filament proteins

open access: yesScientific Reports, 2015
The nuclear lamina is a protein meshwork associated with the inner side of the nuclear envelope contributing structural, signalling and regulatory functions.
M. Kollmar
semanticscholar   +1 more source

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