Results 91 to 100 of about 12,222,224 (337)

Emerging experimental and computational methods for studying redox‐regulated structural transitions

open access: yesFEBS Letters, EarlyView.
Redox reactions can reshape proteins and alter how they behave in cells, with important consequences for health and disease. This review explores emerging experimental and computational approaches for discovering these redox‐sensitive protein switches, revealing their structural effects, and predicting their behavior, opening new opportunities to ...
Tasneem Rass   +2 more
wiley   +1 more source

Nuclear speckles: molecular organization, biological function and role in disease

open access: yesNucleic Acids Research, 2017
The nucleoplasm is not homogenous; it consists of many types of nuclear bodies, also known as nuclear domains or nuclear subcompartments. These self-organizing structures gather machinery involved in various nuclear activities.
Lukasz Galganski   +2 more
semanticscholar   +1 more source

A new role for clathrin adaptor proteins 1 and 3 in lipoplex trafficking [PDF]

open access: yes, 2014
Intracellular protein trafficking through secretory and endocytic pathways depends on the function of adaptor proteins that bind motifs on cargo proteins.
Gumbs, Jade   +10 more
core   +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

HMG Nuclear Proteins: Linking Chromatin Structure to Cellular Phenotype

open access: yesBiochimica et Biophysica Acta, 2009
I. Summary Although the three families of mammalian HMG proteins (HMGA, HMGB and HMGN) participate in many of the same nuclear processes, each family plays its own unique role in modulating chromatin structure and regulating genomic function. This review
R. Reeves
semanticscholar   +1 more source

The gateway to chloroplast: re-defining the function of chloroplast receptor proteins [PDF]

open access: yes, 2012
Chloroplast biogenesis often requires a tight orchestration between gene expression (both plastidial and nuclear) and translocation of similar to 3000 nuclear-encoded proteins into the organelle.
Bölter, Bettina   +2 more
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

Nucleoplasmic signals promote directed transmembrane protein import simultaneously via multiple channels of nuclear pores

open access: yesNature Communications, 2020
The contribution of central and peripheral channels of nuclear pores to transport of transmembrane proteins is unclear. Here the authors show that most inner nuclear membrane proteins use only peripheral channels, but some extend nuclear localization ...
Krishna C. Mudumbi   +9 more
doaj   +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

Structures of mycobacterial 3‐methylcrotonyl‐CoA carboxylase reveal carrier‐domain translocation between catalytic sites

open access: yesFEBS Letters, EarlyView.
Mycobacterial 3‐methylcrotonyl‐CoA carboxylase uses a mobile biotin‐carrying domain to shuttle a carboxyl group between two catalytic sites, enabling carboxylation of 3‐methylcrotonyl‐CoA during leucine breakdown. Cryo‐electron microscopy captures the carrier at both sites and reveals an inward loop movement that may prevent futile rebinding to the ...
Ajit Yadav   +2 more
wiley   +1 more source

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