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ProteomicsLamin A dimer and tetramer cross-links help explain disease mutations and polymer plasticity
Lamins are intermediate filament proteins responsible for nuclear mechanical integrity. Though linked to multiple heritable diseases, lamin structure and that of other intermediate filaments remains elusive. We employed cross-linking mass spectrometry to gain structural insights into lamin A dimer a...
ORGANISM(S): Homo sapiens (Human) Rattus norvegicus (Rat) 
2019-07-12 | PXD008337 | Pride
Silac Cross-link mass spectrometry Em Lamin a 
TranscriptomicsLamin binding profiles in the ENCODE regions
A systems understanding of nuclear organization and events is critical for determining how cells divide, differentiate and respond to stimuli and for identifying the causes of diseases. Chromatin remodeling complexes such as SWI/SNF have been implicated in a wide variety of cellular processes includ...
ORGANISM(S): Homo sapiens 
2011-01-10 | E-GEOD-24382 | biostudies-arrayexpress
GenomicsRedistribution of the Lamin B1 genomic binding profile affects spatial rearrangement of heterochromatic domains and gene expression during senescence
Senescence is a stress responsive form of stable cell cycle exit. Senescent cells have a distinct gene expression profile, which is often accompanied by the spatial redistribution of heterochromatin into senescence-associated heterochromatic foci (SAHFs). Studying a key component of the nuclear lami...
ORGANISM(S): Homo sapiens 
2013-08-22 | E-GEOD-49341 | biostudies-arrayexpress
ProteomicsAssembly of a nuclear lamin coil 2 fragment
Nuclear structure and function are governed by lamins, which are intermediate filaments mostly consisting of α-helices. Different lamin assembly models have been proposed based on low resolution or fragmented structures. However, their assembly mechanisms at the molecular level are poorly understood...
ORGANISM(S): Homo sapiens (Human) 
2025-12-15 | PXD014029 | Pride
Human Coil 2 Lamin Nuclear protein 
ProteomicsHuman lamin B1: stress-induced phosphorylation
This is a small scale study of the phosphorylation state of human lamin B1 immunoprecipitated from control cells or cells treated with methyl methane sulphonate (MMS, acting as a DNA damage stressor agent)
ORGANISM(S): Homo sapiens (Human) 
2017-05-30 | PXD006459 | Pride
Human Post translational modification Nuclear envelope Lamin 
TranscriptomicsDeleterious assembly of the lamin A/C mutant p.S143P causes ER stress in familial dilated cardiomyopathy
Mutation of the LMNA gene, encoding nuclear lamin A and lamin C (hereafter lamin A/C), is a common cause of familial dilated cardiomyopathy (DCM). Among Finnish DCM patients, the founder mutation c.427T>C (p.S143P) is the most frequently reported genetic variant. Here, we show that p.S143P lamin A/C...
ORGANISM(S): Homo sapiens 
2016-06-10 | E-GEOD-82290 | biostudies-arrayexpress
TranscriptomicsGene expression analysis of Lamin B receptor deficient hematopoietic cells
Gene expression analysis of Lamin B receptor deficient hematopoietic cells
ORGANISM(S): Mus musculus 
2011-12-21 | E-TABM-1134 | biostudies-arrayexpress
ProteomicsStructural basis for assembly of lamin at the molecular level
Nuclear structure and function are governed by lamins, which are intermediate filaments mostly consisting of alpha-helices. Different lamin assembly models have been proposed based on low resolution or fragmented structures. However, their assembly mechanisms at the molecular level are poorly unders...
ORGANISM(S): Homo sapiens (Human) 
2019-08-26 | PXD013144 | Pride
Chemical crosslinking Nuclear lamin protein X-ray crystallography Gel-based lc-msms Filament assembly structure 
ProteomicsReconstitution of lamin assembly on nuclear pore complex-containing membranes
Intermediate filaments called lamins line the metazoan nuclear envelope and organize the nucleus and genome. Unlike actin and microtubules, purified intermediate filament proteins assemble into non-physiological structures, making it difficult to connect lamin functions to their assembly and regulat...
ORGANISM(S): Xenopus laevis (African clawed frog) 
2026-09-16 | PXD067048 | Pride
Intermediate filaments Nuclear pore complex Nucleus Xenopus laevis Lamin Reconstitution Lc-ms/ms 
GenomicsCorrelated alterations in genome organization, histone methylation, and DNA-lamina interactions in Hutchinson-Gilford progeria syndrome (ChIP-seq)
Hutchinson-Gilford progeria syndrome (HGPS) is a premature aging disease that is frequently caused by a de novo point mutation at position 1824 in LMNA. This mutation activates a cryptic splice donor site in exon 11, and leads to an in-frame deletion within the prelamin A mRNA and the production of ...
ORGANISM(S): Homo sapiens 
2012-10-30 | E-GEOD-41757 | biostudies-arrayexpress
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