Results 71 to 80 of about 1,436,031 (236)

Cytomegaloviral proteins that associate with the nuclear lamina: components of a postulated nuclear egress complex

open access: yesJournal of General Virology, 2009
The nuclear egress of cytomegaloviral capsids traversing the nuclear envelope is dependent on a locally restricted destabilization of the rigid nuclear lamina. It has been suggested that the multi-component nuclear egress complex (NEC) that is formed is comprised of both viral and cellular proteins which act to recruit lamin-phosphorylating protein ...
Jens, Milbradt   +3 more
openaire   +2 more sources

Proteomic Analysis of the Multimeric Nuclear Egress Complex of Human Cytomegalovirus

open access: yesMolecular & Cellular Proteomics, 2014
Herpesviral capsids are assembled in the host cell nucleus before being translocated into the cytoplasm for further maturation. The crossing of the nuclear envelope represents a major event that requires the formation of the nuclear egress complex (NEC).
Milbradt, Jens   +14 more
openaire   +5 more sources

Infection-induced chromatin modifications facilitate translocation of herpes simplex virus capsids to the inner nuclear membrane.

open access: yesPLoS Pathogens, 2021
Herpes simplex virus capsids are assembled and packaged in the nucleus and move by diffusion through the nucleoplasm to the nuclear envelope for egress.
Vesa Aho   +7 more
doaj   +1 more source

Structural insights and therapeutic targets in Acinetobacter baumannii capsule biosynthesis

open access: yesFEBS Letters, EarlyView.
Hypervirulent KL49 A. baumannii's capsular polysaccharide contains the nonulosonic acid 8‐epi‐Leg5,7Ac2, synthesized by epimerization via ElaA, ElaB, and ElaC. Crystal structures of ElaA, ElaB, and ElaC reveal their role in CMP‐Leg5,7Ac2 synthesis and regioselective C8 epimerization.
Woo Cheol Lee   +7 more
wiley   +1 more source

Nuclear egress of TDP-43 and FUS occurs independently of Exportin-1/CRM1

open access: yesScientific Reports, 2018
TDP-43 and FUS are nuclear proteins with multiple functions in mRNA processing. They play key roles in ALS (amyotrophic lateral sclerosis) and FTD (frontotemporal dementia), where they are partially lost from the nucleus and aggregate in the cytoplasm of
Helena Ederle   +7 more
doaj   +1 more source

Investigating transcription factor dynamics in health and disease using FRAP

open access: yesFEBS Letters, EarlyView.
FRAP analysis of GFP‐tagged transcription factors reveals how molecular mobility and target engagement change in response to drug treatment. By combining live‐cell imaging, quantitative model fitting, and statistical analysis, this approach uncovers transcription factor dynamics linked to disease mechanisms, providing a powerful framework for ...
Kannan Govindaraj   +3 more
wiley   +1 more source

Conserved binding mode but diverse interfaces of MreC‐PBP2 interactions

open access: yesFEBS Letters, EarlyView.
The crystal structure of abMreC reveals a conserved two β‐barrel architecture and provides structural insights into its role within the bacterial elongasome. The abMreC–abPBP2 complex model identifies the molecular basis of MreC‐mediated PBP2 recognition, contributing to the regulation of peptidoglycan synthesis.
Hyunseok Jang   +4 more
wiley   +1 more source

Tegument Protein pp150 Sequence-Specific Peptide Blocks Cytomegalovirus Infection

open access: yesViruses, 2021
Human cytomegalovirus (HCMV) tegument protein pp150 is essential for the completion of the final steps in virion maturation. Earlier studies indicated that three pp150nt (N-terminal one-third of pp150) conformers cluster on each triplex (Tri1, Tri2A and ...
Dipanwita Mitra   +4 more
doaj   +1 more source

Structure‐forward targeting of claudins with synthetic binders

open access: yesFEBS Letters, EarlyView.
Claudins form the paracellular barriers between epithelial and endothelial tissues at tight junctions and are targets for molecular binders with the goal of modulating barrier permeability. Claudin‐binding molecules are relevant in drug delivery or in altering claudin interactions with disease‐causing proteins.
Alex J. Vecchio
wiley   +1 more source

Nutrient/TOR signaling controls adipose mitochondrial transcription factor A (TFAM) to regulate organismal growth in Drosophila

open access: yesFEBS Letters, EarlyView.
Animals must match their growth rate to available nutrients. We show that in Drosophila larvae, the nutrient‐sensing TOR kinase controls growth by regulating levels of TFAM, a key regulator of mitochondrial function, in the adipose tissue. When nutrients are abundant, high TOR activity suppresses TFAM, lowering mitochondrial bioenergetic activity and ...
Shrivani Sriskanthadevan‐Pirahas   +4 more
wiley   +1 more source

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