Cargando…

Porphyromonas gingivalis GroEL Induces Osteoclastogenesis of Periodontal Ligament Cells and Enhances Alveolar Bone Resorption in Rats

Porphyromonas gingivalis is a major periodontal pathogen that contains a variety of virulence factors. The antibody titer to P. gingivalis GroEL, a homologue of HSP60, is significantly higher in periodontitis patients than in healthy control subjects, suggesting that P. gingivalis GroEL is a potenti...

Descripción completa

Detalles Bibliográficos
Autores principales:	Lin, Feng-Yen, Hsiao, Fung-Ping, Huang, Chun-Yao, Shih, Chun-Ming, Tsao, Nai-Wen, Tsai, Chien-Sung, Yang, Shue-Fen, Chang, Nen-Chung, Hung, Shan-Ling, Lin, Yi-Wen
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Public Library of Science 2014
Materias:	Research Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4109931/ https://www.ncbi.nlm.nih.gov/pubmed/25058444 http://dx.doi.org/10.1371/journal.pone.0102450

Ejemplares similares

GroEL1, a Heat Shock protein 60 of Chlamydia pneumoniae, Impairs Neovascularization by Decreasing Endothelial Progenitor Cell Function
por: Lin, Yi-Wen, et al.
Publicado: (2013)

Creating the Functional Single-Ring GroEL-GroES Chaperonin Systems via Modulating GroEL-GroES Interaction
por: Illingworth, Melissa, et al.
Publicado: (2017)

GroEL1, from Chlamydia pneumoniae, Induces Vascular Adhesion Molecule 1 Expression by p37(AUF1) in Endothelial Cells and Hypercholesterolemic Rabbit
por: Huang, Chun-Yao, et al.
Publicado: (2012)

Inhibition of osteoclastogenesis by opsonized Porphyromonas gingivalis
por: Pandruvada, Subramanya N., et al.
Publicado: (2019)

Correction: GroEL1, from Chlamydia pneumoniae, Induces Vascular Adhesion Molecule 1 Expression by p37(AUF1) in Endothelial Cells and Hypercholesterolemic Rabbit
por: Huang, Chun-Yao, et al.
Publicado: (2012)

Myxococcus xanthus DK1622 Coordinates Expressions of the Duplicate groEL and Single groES Genes for Synergistic Functions of GroELs and GroES
por: Zhuo, Li, et al.
Publicado: (2017)

Back to GroEL-Assisted Protein Folding: GroES Binding-Induced Displacement of Denatured Proteins from GroEL to Bulk Solution
por: Marchenkov, Victor, et al.
Publicado: (2020)

Aging Aggravates Periodontal Inflammatory Responses and Alveolar Bone Resorption by Porphyromonas gingivalis Infection
por: Song, Yuri, et al.
Publicado: (2023)

Micromolar sodium fluoride mediates anti-osteoclastogenesis in Porphyromonas gingivalis-induced alveolar bone loss
por: Bhawal, Ujjal K, et al.
Publicado: (2015)

Markov propagation of allosteric effects in biomolecular systems: application to GroEL–GroES
por: Chennubhotla, Chakra, et al.
Publicado: (2006)

Transient conformational remodeling of folding proteins by GroES—individually and in concert with GroEL
por: Moparthi, Satish Babu, et al.
Publicado: (2013)

Functional Differences between E. coli and ESKAPE Pathogen GroES/GroEL
por: Sivinski, Jared, et al.
Publicado: (2021)

Novel cryo-EM structure of an ADP-bound GroEL–GroES complex
por: Kudryavtseva, Sofia S., et al.
Publicado: (2021)

B-Cell Epitopes in GroEL of Francisella tularensis
por: Lu, Zhaohua, et al.
Publicado: (2014)

Dataset concerning GroEL chaperonin interaction with proteins
por: Marchenkov, V.V., et al.
Publicado: (2016)

Folding of maltose binding protein outside of and in GroEL
por: Ye, Xiang, et al.
Publicado: (2018)

In-Vivo Effect of Andrographolide on Alveolar Bone Resorption Induced by Porphyromonas gingivalis and Its Relation with Antioxidant Enzymes
por: Al Batran, Rami, et al.
Publicado: (2013)

Perturbation-based Markovian Transmission Model for Probing Allosteric Dynamics of Large Macromolecular Assembling: A Study of GroEL-GroES
por: Lu, Hsiao-Mei, et al.
Publicado: (2009)

Topologies of a Substrate Protein Bound to the Chaperonin GroEL
por: Elad, Nadav, et al.
Publicado: (2007)

Probing the Dynamic Process of Encapsulation in Escherichia coli GroEL
por: Mizuta, Toshifumi, et al.
Publicado: (2013)

Suppression of amyloid fibrils using the GroEL apical domain
por: Ojha, Bimlesh, et al.
Publicado: (2016)

Probing Water Density and Dynamics in the Chaperonin GroEL Cavity
por: Franck, John M., et al.
Publicado: (2014)

GroEL is an immunodominant surface-exposed antigen of Rickettsia typhi
por: Rauch, Jessica, et al.
Publicado: (2021)

Structural and Computational Study of the GroEL–Prion Protein Complex
por: Mamchur, Aleksandra A., et al.
Publicado: (2021)

Folding of newly translated membrane protein CCR5 is assisted by the chaperonin GroEL-GroES
por: Chi, Haixia, et al.
Publicado: (2015)

In vivo client proteins of the chaperonin GroEL-GroES provide insight into the role of chaperones in protein evolution
por: Taguchi, Hideki, et al.
Publicado: (2023)

Self-assembly of the chaperonin GroEL nanocage induced at submicellar detergent
por: Chen, Jin, et al.
Publicado: (2014)

Immunization Using GroEL Decreases Clostridium difficile Intestinal Colonization
por: Péchiné, Séverine, et al.
Publicado: (2013)

Chaperonin GroEL Reassembly: An Effect of Protein Ligands and Solvent Composition
por: Ryabova, Nataliya, et al.
Publicado: (2014)

The Chaperonin GroEL: A Versatile Tool for Applied Biotechnology Platforms
por: O'Neil, Pierce T., et al.
Publicado: (2018)

Borrelia burgdorferi Surface Exposed GroEL Is a Multifunctional Protein
por: Cafiero, Thomas, et al.
Publicado: (2021)

GroEL Chaperonin-Based Assay for Early Diagnosis of Scrub Typhus
por: Indrawattana, Nitaya, et al.
Publicado: (2022)

Protein chain collapse modulation and folding stimulation by GroEL-ES
por: Naqvi, Mohsin M., et al.
Publicado: (2022)

Slowdown of Water Dynamics from the Top to the Bottom of the GroEL Cavity
por: Macro, Nicolas, et al.
Publicado: (2021)

GroEL—A Versatile Chaperone for Engineering and a Plethora of Applications
por: Yurkova, Maria S., et al.
Publicado: (2022)

GroEL-Proteotyping of Bacterial Communities Using Tandem Mass Spectrometry
por: Klaes, Simon, et al.
Publicado: (2023)

Multi-Scale Simulations Provide Supporting Evidence for the Hypothesis of Intramolecular Protein Translocation in GroEL/GroES Complexes
por: Coluzza, Ivan, et al.
Publicado: (2008)

The Mycobacterium tuberculosis sRNA F6 Modifies Expression of Essential Chaperonins, GroEL2 and GroES
por: Houghton, Joanna, et al.
Publicado: (2021)

GroEL as a molecular scaffold for structural analysis of the anthrax toxin pore
por: Katayama, Hiroo, et al.
Publicado: (2008)

Probing the Functional Mechanism of Escherichia coli GroEL Using Circular Permutation
por: Mizobata, Tomohiro, et al.
Publicado: (2011)

Cannot write session to /tmp/vufind_sessions/sess_dj36c9so3qqhlrotda7talho2j