Cargando…

Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranes

Paradoxically, aggregation of specific proteins is characteristic of many human diseases and aging, yet aggregates have increasingly been found to be unnecessary for initiating pathogenesis. Here we determined the NMR topology and dynamics of a helical mutant in a membrane environment transformed fr...

Descripción completa

Detalles Bibliográficos
Autores principales:	Qin, Haina, Lim, Liangzhong, Wei, Yuanyuan, Gupta, Garvita, Song, Jianxing
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	F1000Research 2014
Materias:	Research Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4168755/ https://www.ncbi.nlm.nih.gov/pubmed/25254094 http://dx.doi.org/10.12688/f1000research.2-221.v2

Ejemplares similares

Structural, Stability, Dynamic and Binding Properties of the ALS-Causing T46I Mutant of the hVAPB MSP Domain as Revealed by NMR and MD Simulations
por: Lua, Shixiong, et al.
Publicado: (2011)

Protein dynamics at Eph receptor-ligand interfaces as revealed by crystallography, NMR and MD simulations
por: Qin, Haina, et al.
Publicado: (2012)

Intrinsically Unstructured Domain 3 of Hepatitis C Virus NS5A Forms a “Fuzzy Complex” with VAPB-MSP Domain Which Carries ALS-Causing Mutations
por: Gupta, Garvita, et al.
Publicado: (2012)

Intrinsically Disordered and Aggregation Prone Regions Underlie β-Aggregation in S100 Proteins
por: Carvalho, Sofia B., et al.
Publicado: (2013)

Excessive aggregation of membrane proteins in the Martini model
por: Javanainen, Matti, et al.
Publicado: (2017)

Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins
por: García-Fruitós, Elena, et al.
Publicado: (2005)

A novel approach for the purification of aggregation prone proteins
por: Royster, Austin, et al.
Publicado: (2021)

Insights into Protein Aggregation by NMR Characterization of Insoluble SH3 Mutants Solubilized in Salt-Free Water
por: Liu, Jingxian, et al.
Publicado: (2009)

NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics
por: Gupta, Garvita, et al.
Publicado: (2015)

Thermal aggregation of SARS-CoV membrane protein
por: Lee, Yi-Nung, et al.
Publicado: (2005)

Role of solvent accessibility for aggregation-prone patches in protein folding
por: Mishra, Avinash, et al.
Publicado: (2018)

Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in Caenorhabditis elegans
por: Huang, Chaolie, et al.
Publicado: (2019)

Aggregation-Prone Structural Ensembles of Transthyretin Collected With Regression Analysis for NMR Chemical Shift
por: Yang, Wonjin, et al.
Publicado: (2021)

ON THE INFLUENCE OF AGGREGATES ON THE MEMBRANE POTENTIALS AND THE OSMOTIC PRESSURE OF PROTEIN SOLUTIONS
por: Loeb, Jacques
Publicado: (1922)

Cytosolic aggregates perturb the degradation of nontranslocated secretory and membrane proteins
por: Chakrabarti, Oishee, et al.
Publicado: (2011)

Autoimmune Responses to Soluble Aggregates of Amyloidogenic Proteins Involved in Neurodegenerative Diseases: Overlapping Aggregation Prone and Autoimmunogenic regions
por: Kumar, Sandeep, et al.
Publicado: (2016)

Structure of the AAA protein Msp1 reveals mechanism of mislocalized membrane protein extraction
por: Wang, Lan, et al.
Publicado: (2020)

A Consensus Method for the Prediction of ‘Aggregation-Prone’ Peptides in Globular Proteins
por: Tsolis, Antonios C., et al.
Publicado: (2013)

Aggregation-Prone Proteins Modulate Huntingtin Inclusion Body Formation in Yeast
por: Kantcheva, Ralitsa B., et al.
Publicado: (2014)

Classification model of amino acid sequences prone to aggregation of therapeutic proteins
por: Marczak, Monika, et al.
Publicado: (2016)

The effect of mutation on an aggregation-prone protein: An in vivo, in vitro, and in silico analysis
por: Guthertz, N., et al.
Publicado: (2022)

Identification of interaction partners using protein aggregation and NMR spectroscopy
por: Chae, Young Kee, et al.
Publicado: (2022)

Paradoxical Role of Prion Protein Aggregates in Redox-Iron Induced Toxicity
por: Das, Dola, et al.
Publicado: (2010)

Signature of an aggregation-prone conformation of tau
por: Eschmann, Neil A., et al.
Publicado: (2017)

Specialized membrane-localized chaperones prevent aggregation of polytopic proteins in the ER
por: Kota, Jhansi, et al.
Publicado: (2005)

Puromycin-sensitive aminopeptidase protects against aggregation-prone proteins via autophagy
por: Menzies, Fiona M., et al.
Publicado: (2010)

CGG repeats trigger translational frameshifts that generate aggregation-prone chimeric proteins
por: Wright, Shannon E, et al.
Publicado: (2022)

Rhomboid protease RHBDL4 promotes retrotranslocation of aggregation-prone proteins for degradation
por: Bock, Josephine, et al.
Publicado: (2022)

The AAA protein Msp1 mediates clearance of excess tail-anchored proteins from the peroxisomal membrane
por: Weir, Nicholas R, et al.
Publicado: (2017)

ATP-independent reversal of a membrane protein aggregate by a chloroplast SRP
por: Jaru-Ampornpan, Peera, et al.
Publicado: (2010)

Physicochemical and Functional Properties of Membrane-Fractionated Heat-Induced Pea Protein Aggregates
por: Asen, Nancy D., et al.
Publicado: (2022)

Chemical fixation creates nanoscale clusters on the cell surface by aggregating membrane proteins
por: Ichikawa, Takehiko, et al.
Publicado: (2022)

Editorial: Protein Degradation, Aggregation, Membrane Trafficking and Exosomes in Neuronal Health and Disease
por: Campbell, Douglas S., et al.
Publicado: (2022)

Cell surface protein aggregation triggers endocytosis to maintain plasma membrane proteostasis
por: Paul, David, et al.
Publicado: (2023)

Genome comparison implies the role of Wsm2 in membrane trafficking and protein degradation
por: Zhang, Guorong, et al.
Publicado: (2018)

In silico engineering of aggregation-prone recombinant proteins for substrate recognition by the chaperonin GroEL
por: Kumar, Vipul, et al.
Publicado: (2012)

A Chemical Mutagenesis Approach to Insert Post-translational Modifications in Aggregation-Prone Proteins
por: Ge, Ying, et al.
Publicado: (2022)

C-Terminal Auto-Regulatory Motif of Hepatitis C Virus NS5B Interacts with Human VAPB-MSP to Form a Dynamic Replication Complex
por: Gupta, Garvita, et al.
Publicado: (2016)

The aggregation paradox for statistical rankings and nonparametric tests
por: Nagaraja, Haikady N., et al.
Publicado: (2020)

Mutational probing of protein aggregates to design aggregation‐resistant proteins
por: Kamal, Mohamad Zahid, et al.
Publicado: (2016)

Cannot write session to /tmp/vufind_sessions/sess_shsiiu0rv6r61f5b2bjhgoihsn