Results 81 to 90 of about 6,851,273 (294)
FEBS Letters, EarlyView.Plasma membranes contain dynamic nanoscale domains that organize lipids and receptors. Because viruses operate at similar scales, this architecture shapes early infection steps, including attachment, receptor engagement, and entry. Using influenza A virus and HIV‐1 as examples, we highlight how receptor nanoclusters, multivalent glycan interactions ...
Jan Schlegel, Christian Sieben
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Nuclear pore complex tethers to the cytoskeleton [PDF]
, 2017 The nuclear envelope is tethered to the cytoskeleton. The best known attachments of all elements of the cytoskeleton are via the so-called LINC complex.
Martin W. Goldberg, Goldberg, Martin W.
core +1 more source
Karyopherin binding interactions and nuclear import mechanism of nuclear pore complex protein Tpr
BMC Cell Biology, 2009 Background Tpr is a large protein with an extended coiled-coil domain that is localized within the nuclear basket of the nuclear pore complex. Previous studies 1 involving antibody microinjection into mammalian cells suggested a role for Tpr in nuclear ...
Frosst Phyllis D +2 more
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Expression of DNAJB12 or DNAJB14 causes coordinate invasion of the nucleus by membranes associated with a novel nuclear pore structure. [PDF]
PLoS ONE, 2014 DNAJB12 and DNAJB14 are transmembrane proteins in the endoplasmic reticulum (ER) that serve as co-chaperones for Hsc70/Hsp70 heat shock proteins. We demonstrate that over-expression of DNAJB12 or DNAJB14 causes the formation of elaborate membranous ...
Edward C Goodwin +4 more
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The major polypeptides of the nuclear pore complex [PDF]
Experimental Cell Research, 1978 Abstract Nuclear envelopes of maturing oocytes of various amphibia contain an unusually high number of pore complexes in very close packing. Consequently, nuclear envelopes, which can be manually isolated in great purity, provide a remarkable enrichment of nuclear pore complex material, relative to membranous and other interporous structures.
Krohne, Georg +2 more
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Biophysical approaches for studying viral entry
FEBS Letters, EarlyView.Viruses infect all living organisms and have been responsible for major epidemics and pandemics. Their ongoing evolutionary battle with host defenses creates a constant need for improved tools to study viral behavior. Advancing methods to probe viral attachment, fusion, and genome release deepen our understanding of how infections begin and support the
Inbar Yosibash, Raya Sorkin
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The Potential of Nuclear Pore Complexes in Cancer Therapy
MoleculesNuclear pore complexes (NPCs) play a critical role in regulating transport-dependent gene expression, influencing various stages of cancer development and progression.
Hanna Zaitsava +4 more
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Nuclear pore complex protein mediated nuclear localization of dicer protein in human cells.
PLoS ONE, 2011 Human DICER1 protein cleaves double-stranded RNA into small sizes, a crucial step in production of single-stranded RNAs which are mediating factors of cytoplasmic RNA interference. Here, we clearly demonstrate that human DICER1 protein localizes not only
Yoshinari Ando +14 more
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FEBS Letters, EarlyView.Septin 9 polybasic domains couple phosphoinositide‐rich membrane binding to centrosome positioning, Golgi organization, and microtubule acetylation to control epithelial polarity. Their loss disrupts this axis, causing centrosome mispositioning, Golgi fragmentation, reduced microtubule acetylation, and polarity inversion via upregulation of the ...
Ting ting Cai +4 more
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Nuclear pore dysfunction and disease: a complex opportunity
NucleusThe separation of genetic material from bulk cytoplasm has enabled the evolution of increasingly complex organisms, allowing for the development of sophisticated forms of life. However, this complexity has created new categories of dysfunction, including
Charlotte M. Fare, Jeffrey D. Rothstein
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