Results 81 to 90 of about 8,612,670 (377)

A Cre‐dependent lentiviral vector for neuron subtype‐specific expression of large proteins

open access: yesFEBS Letters, EarlyView.
We designed a versatile and modular lentivector comprising a Cre‐dependent switch and self‐cleaving 2A peptide and tested it for co‐expression of GFP and a 2.8 kb gene of interest (GOI) in mouse cortical parvalbumin (PV+) interneurons and midbrain dopamine (TH+) neurons.
Weixuan Xue   +6 more
wiley   +1 more source

Expression of the DNA mismatch repair proteins hMLH1 and hPMS2 in normal human tissues. [PDF]

open access: yes, 1997
hMLH1 and hPMS2 are part of the DNA mismatch repair complex. Mutations in these genes have been linked to hereditary non-polyposis colon cancer; they also occur in a variety of sporadic cancers. Western blot analysis and immunohistochemistry demonstrated
Aebi, S   +6 more
core   +1 more source

Nuclear tau and its potential role in Alzheimer’s disease [PDF]

open access: yes, 2016
Tau protein, found in both neuronal and non-neuronal cells, forms aggregates in neurons that constitutes one of the hallmarks of Alzheimer’s disease (AD).
Al-Hilaly, Youssra   +2 more
core   +2 more sources

Reconstitution of nuclear protein export in isolated nuclear envelopes [PDF]

open access: yesThe Journal of Cell Biology, 2002
Signal-dependent nuclear protein export was studied in perforated nuclei and isolated nuclear envelopes of Xenopus oocytes by optical single transporter recording. Manually isolated and purified oocyte nuclei were attached to isoporous filters and made permeable for macromolecules by perforation.
Siebrasse, Jan Peter   +2 more
openaire   +2 more sources

Nucleoskeleton proteins for nuclear dynamics

open access: yesThe Journal of Biochemistry, 2021
AbstractThe eukaryotic nucleus shows organized structures of chromosomes, transcriptional components and their associated proteins. It has been believed that such a dense nuclear environment prevents the formation of a cytoskeleton-like network of protein filaments. However, accumulating evidence suggests that the cell nucleus also possesses structural
Kei Miyamoto, Masahiko Harata
openaire   +2 more sources

Chromatin condensation modulates access and binding of nuclear proteins

open access: yesThe FASEB Journal, 2010
The condensation level of chromatin is controlled by epigenetic modifications and associated regulatory factors and changes throughout differentiation and cell cycle progression.
Robert M. Martin, M. Cardoso
semanticscholar   +1 more source

Structural insights into lacto‐N‐biose I recognition by a family 32 carbohydrate‐binding module from Bifidobacterium bifidum

open access: yesFEBS Letters, EarlyView.
Bifidobacterium bifidum establishes symbiosis with infants by metabolizing lacto‐N‐biose I (LNB) from human milk oligosaccharides (HMOs). The extracellular multidomain enzyme LnbB drives this process, releasing LNB via its catalytic glycoside hydrolase family 20 (GH20) lacto‐N‐biosidase domain.
Xinzhe Zhang   +5 more
wiley   +1 more source

Nucleocytoplasmic Shuttling of Cytoskeletal Proteins: Molecular Mechanism and Biological Significance

open access: yesInternational Journal of Cell Biology, 2012
Various nuclear functional complexes contain cytoskeletal proteins as regulatory subunits; for example, nuclear actin participates in transcriptional complexes, and actin-related proteins are integral to chromatin remodeling complexes.
Masahiro Kumeta   +3 more
doaj   +1 more source

Nuclear envelopathies: a complex LINC between nuclear envelope and pathology

open access: yesOrphanet Journal of Rare Diseases, 2017
Since the identification of the first disease causing mutation in the gene coding for emerin, a transmembrane protein of the inner nuclear membrane, hundreds of mutations and variants have been found in genes encoding for nuclear envelope components ...
Alexandre Janin   +4 more
doaj   +1 more source

The Caenorhabditis elegans DPF‐3 and human DPP4 have tripeptidyl peptidase activity

open access: yesFEBS Letters, EarlyView.
The dipeptidyl peptidase IV (DPPIV) family comprises serine proteases classically defined by their ability to remove dipeptides from the N‐termini of substrates, a feature that gave the family its name. Here, we report the discovery of a previously unrecognized tripeptidyl peptidase activity in DPPIV family members from two different species.
Aditya Trivedi, Rajani Kanth Gudipati
wiley   +1 more source

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