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Altered pre-lamin A processing is a common mechanism leading to lipodystrophy
Source:
Oxford University Press (OUP)
H3K9me2 orchestrates inheritance of spatial positioning of peripheral heterochromatin through mitosis
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Cold Spring Harbor Laboratory
Interaction between emerin and nuclear lamins.
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Oxford University Press (OUP)
An improved hidden Markov model for transmembrane protein detection and topology prediction and its applications to complete genomes
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Oxford University Press (OUP)
Next generation sequencing in functional genomics
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Oxford University Press (OUP)
MAN1, an integral protein of the inner nuclear membrane, binds Smad2 and Smad3 and antagonizes transforming growth factor-β signaling
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Oxford University Press (OUP)
Rapid one-step protein purification from plant material using the eight-amino acid StrepII epitope.
Source:
Springer Science and Business Media LLC
Subcellular localization of the yeast proteome
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Cold Spring Harbor Laboratory
In vivo and in vitro interaction between human transcription factor MOK2 and nuclear lamin A/C
Source:
Oxford University Press (OUP)
Nup-PI: the nucleopore-promoter interaction of genes in yeast.
Source:
Elsevier BV
Proteomic analysis of the mammalian nuclear pore complex
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Rockefeller University Press
Nup93, a vertebrate homologue of yeast Nic96p, forms a complex with a novel 205-kDa protein and is required for correct nuclear pore assembly.
Source:
American Society for Cell Biology (ASCB)
Chromatin histone modifications and rigidity affect nuclear morphology independent of lamins
Source:
Cold Spring Harbor Laboratory
Mislocalization to the nuclear envelope: An effect of the dystonia-causing torsinA mutation
Source:
Proceedings of the National Academy of Sciences
Effect of glycerol on the interactions and solubility of bovine pancreatic trypsin inhibitor.
Source:
Elsevier BV
Localizing the proteome
Source:
Springer Science and Business Media LLC
Identification of Direct Serum-response Factor Gene Targets during Me2SO-induced P19 Cardiac Cell Differentiation
Source:
Elsevier BV
Interactions among Drosophila Nuclear Envelope Proteins Lamin, Otefin, and YA
Source:
American Society for Microbiology
Genome-wide localization of the nuclear transport machinery couples transcriptional status and nuclear organization.
Source:
Elsevier BV
Towards defining the nuclear proteome
Source:
Springer Science and Business Media LLC
Use of sequential chemical extractions to purify nuclear membrane proteins for proteomics identification.
Source:
Humana Press
Building a nuclear envelope at the end of mitosis: coordinating membrane reorganization, nuclear pore complex assembly, and chromatin de-condensation
Source:
Springer Nature
Smurf2 regulates stability and the autophagic-lysosomal turnover of lamin A and its disease-associated form progerin.
Source:
Wiley
Single‐step Strep‐tag® purification for the isolation and identification of protein complexes from mammalian cells
Source:
Wiley
A nuclear envelope-associated kinase phosphorylates arginine-serine motifs and modulates interactions between the lamin B receptor and other nuclear proteins
Source:
Elsevier BV
Reverse Recruitment: The Nup84 Nuclear Pore Subcomplex Mediates Rap1/Gcr1/Gcr2 Transcriptional Activation
Source:
Proceedings of the National Academy of Sciences
Laminopathies
Source:
Wiley
Detection of in vivo protein-DNA interactions using DamID in mammalian cells.
Source:
Springer Science and Business Media LLC
Large-scale analysis of the yeast genome by transposon tagging and gene disruption
Source:
Springer Science and Business Media LLC
Nuc-PLoc: a new web-server for predicting protein subnuclear localization by fusing PseAA composition and PsePSSM.
Source:
Oxford University Press (OUP)
Nanoscale invaginations of the nuclear envelope: Shedding new light on wormholes with elusive function.
Source:
Informa UK Limited
Analysis of the Localization and Topology of Nurim, a Polytopic Protein Tightly Associated with the Inner Nuclear Membrane
Source:
Elsevier BV
A novel interaction between lamin A and SREBP1: implications for partial lipodystrophy and other laminopathies
Source:
Oxford University Press (OUP)
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