Results 71 to 80 of about 3,755 (143)

Plectin Missense Mutation p.Leu319Pro in the Pathogenesis of Autosomal Recessive Epidermolysis Bullosa Simplex

open access: yesActa Dermato-Venereologica, 2020
is missing (Short communication)
Wei-Ting Tu   +9 more
doaj   +1 more source

Purification and Structural Analysis of Plectin and BPAG1e

open access: yes, 2016
Plectin and BPAG1e belong to the plakin family of high-molecular-weight proteins that interconnect the cytoskeletal systems and anchor them to junctional complexes. Plectin and BPAG1e are prototypical plakins with a similar tripartite modular structure.
Manso, José A.   +8 more
openaire   +3 more sources

Functional and Morphological Plasticity of the Endolysosomal System: Pigment Organelles at the Crossroads of Physiology and Pathology

open access: yesBiology of the Cell, Volume 117, Issue 10, October 2025.
The morphodynamical plasticity of the endolysosomal system supports the formation and function of specialized intracellular compartments, as exemplified by the pigment organelles in skin cells. In epidermal melanocytes and keratinocytes, membrane trafficking and remodeling coordinate tissue pigmentation and protect the genome from photodamage ...
Laura Salavessa   +4 more
wiley   +1 more source

Three Is Better than One: A Multimetal Complex that Triggers Immunogenic Cell Death

open access: yesAngewandte Chemie, Volume 137, Issue 39, September 22, 2025.
A triple metal prodrug that codelivers PtII, RuII, and AuI species triggers a potent immunogenic cell death (ICD) response via combined Type I/II pathways. The tri‐metallic scaffold promotes tumor inhibition, immune memory, and peripheral leukocyte activation, offering a next‐generation chemo‐immunotherapeutic approach (created in BioRender.
Tomer Babu   +4 more
wiley   +1 more source

Epidermolysis bullosa simplex: genotype-phenotype correlations

open access: yesVestnik Dermatologii i Venerologii
Epidermolysis bullosa simplex (EBS) includes a group of diseases characterized by varying severity, possible damage to visceral organs, and various outcomes ranging from complete regression of the rash to death. The initial clinical manifestations of EBS
Vadim V. Chikin, Arfenia E. Karamova
doaj   +1 more source

PKD2 and RSK1 Regulate Integrin β4 Phosphorylation at Threonine 1736.

open access: yesPLoS ONE, 2015
The integrin α6β4, a major component of hemidesmosomes (HDs), stabilizes keratinocyte cell adhesion to the epidermal basement membrane through binding to the cytoskeletal linker protein plectin and association with keratin filaments.
Lisa Te Molder, Arnoud Sonnenberg
doaj   +1 more source

Desmin and Plectin Recruitment to the Nucleus and Nuclei Orientation Are Lost in Emery-Dreifuss Muscular Dystrophy Myoblasts Subjected to Mechanical Stimulation

open access: yesCells
In muscle cells subjected to mechanical stimulation, LINC complex and cytoskeletal proteins are basic to preserve cellular architecture and maintain nuclei orientation and positioning. In this context, the role of lamin A/C remains mostly elusive.
Vittoria Cenni   +7 more
doaj   +1 more source

Plectin-1 targeted AAV vector for the molecular imaging of pancreatic cancer

open access: yesFrontiers in Oncology, 2013
Pancreatic ductal adenocarcinoma (PDAC) is highly malignant disease that is the 4th leading cause of cancer-related death in the US. Gene therapy using AAV vectors to selectively deliver genes to PDAC cells is an attractive treatment option for ...
Prasad R. Konkalmatt   +6 more
doaj   +1 more source

Dlc1 interaction with non-muscle myosin heavy chain II-A (Myh9) and Rac1 activation

open access: yesBiology Open, 2016
The Deleted in liver cancer 1 (Dlc1) gene codes for a Rho GTPase-activating protein that also acts as a tumour suppressor gene. Several studies have consistently found that overexpression leads to excessive cell elongation, cytoskeleton changes and ...
Mohammad G. Sabbir   +2 more
doaj   +1 more source

Reconstitution of cytolinker-mediated crosstalk between actin and vimentin

open access: yesEuropean Journal of Cell Biology
Cell shape and motility are determined by the cytoskeleton, an interpenetrating network of actin filaments, microtubules, and intermediate filaments. The biophysical properties of each filament type individually have been studied extensively by cell-free
Irene Istúriz Petitjean   +6 more
doaj   +1 more source

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