Results 91 to 100 of about 1,947,312 (301)

Nuclear Pore Complex StructureUnplugged and Dynamic Pores [PDF]

open access: yesDevelopmental Cell, 2004
Nuclear pore complexes (NPCs) are large protein assemblies embedded in the nuclear envelope that act as passageways for transport of molecules into and out of the nucleus. Two new studies, one in Nature Cell Biology and one in Science , offer direct evidence that the NPC is a highly dynamic structure.
openaire   +2 more sources

Synergistic perspectives—How single‐molecule biophysics complement biochemical understanding

open access: yesFEBS Letters, EarlyView.
In this review, we discuss how ensemble biochemistry and single‐molecule approaches are complementary, outline commonly used single‐molecule techniques, and illustrate their relevance through two representative case studies: chromatin organization by SMC complexes and pathway choice during DNA double‐strand break repair.
Sara De Bragança   +2 more
wiley   +1 more source

Structural and Biochemical Studies of the Human DEAD-box Helicase Dbp5 and Nucleoporin Nup214 Involved in mRNA Export [PDF]

open access: yes, 2009
The hallmark of eukaryotic evolution was the development of the nucleus in cells. This compartmentalization requires the nucleocytoplasmic transport of thousands of molecules. The gate into and out of the nucleus is the nuclear pore complex (NPC). One of
Moeller, Holger von, Moeller, H.
core   +1 more source

Nuclear Pore Proteins in Regulation of Chromatin State

open access: yesCells, 2019
Nuclear pore complexes (NPCs) are canonically known to regulate nucleocytoplasmic transport. However, research efforts over the last decade have demonstrated that NPCs and their constituent nucleoporins (Nups) also interact with the genome and perform ...
Terra M. Kuhn, Maya Capelson
doaj   +1 more source

mSphere of Influence: the Dynamic Nature of the Nuclear Envelope during Mitosis of Malaria Parasites

open access: yesmSphere, 2020
Sabrina Absalon works in the field of cellular and molecular biology of Plasmodium falciparum, the most virulent parasite causing malaria in humans. In this mSphere of Influence article, she reflects on how the paper “3D nuclear architecture reveals ...
Sabrina Absalon
doaj   +1 more source

Nuclear envelope: membrane bending for pore formation?

open access: yes, 2009
Membrane-shaping proteins known as reticulons help to sculpt the endoplasmic reticulum; recent findings indicate that they also play a role in the formation of nuclear-pore-complex-associated pores in the nuclear ...
Antonin, W.
core   +1 more source

Functional comparison of EncB and EncC cargo proteins in iron storage within the Myxococcus xanthus encapsulin

open access: yesFEBS Letters, EarlyView.
Encapsulins are protein nanocompartments that play an important role in iron storage. In the Myxococcus xanthus encapsulin system, two cargo proteins called EncB and EncC contribute to iron mineralization. Here, we show that EncB and EncC generate iron‐containing minerals with distinct chemical compositions, suggesting that the composition of stored ...
Harry B. McDowell   +2 more
wiley   +1 more source

Pore structure characterization of low permeability rocks [PDF]

open access: yes, 2014
Tese (doutorado) - Universidade Federal de Santa Catarina, Centro Tecnológico, Programa de Pós-Graduação em Ciência e Engenharia de Materiais, Florianópolis, 2014.Hoje as pesquisas em rochas de baixa permeabilidade (grande tendência no mundo e em breve ...
Schmitt, Mayka
core  

Herpes simplex virus ICP27 protein directly interacts with the nuclear pore complex through NUP62, inhibiting host nucleocytoplasmic transport pathways [PDF]

open access: yes, 2012
The herpes simplex virus ICP27 protein is important for the expression and nuclear export of viral mRNAs. Although several binding sites have been mapped along the ICP27 sequence for various RNA and protein partners including the transport receptor TAP ...
Graham, Sheila   +10 more
core   +1 more source

Structural and biochemical analysis of a B12 superbinder

open access: yesFEBS Letters, EarlyView.
BtuG proteins are vitamin B12 scavengers in Bacteroides thetaiotaomicron, a dominant human gut bacterium. We present crystal structures of three BtuG homologs bound to cobalamin and its precursor cobinamide, revealing picomolar binding affinities, among the highest known for any natural protein.
Jose M. Martinez Felices   +3 more
wiley   +1 more source

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