Cargando…

Oncogenic Mutations Differentially Affect Bax Monomer, Dimer, and Oligomeric Pore Formation in the Membrane

Dysfunction of Bax, a pro-apoptotic regulator of cellular metabolism is implicated in neurodegenerative diseases and cancer. We have constructed the first atomistic models of the Bax oligomeric pore consisting with experimental residue-residue distances. The models are stable, capturing well double...

Descripción completa

Detalles Bibliográficos
Autores principales:	Zhang, Mingzhen, Zheng, Jie, Nussinov, Ruth, Ma, Buyong
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Nature Publishing Group 2016
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5024136/ https://www.ncbi.nlm.nih.gov/pubmed/27630059 http://dx.doi.org/10.1038/srep33340

Ejemplares similares

Release of Cytochrome C from Bax Pores at the Mitochondrial Membrane
por: Zhang, Mingzhen, et al.
Publicado: (2017)

Bax monomers form dimer units in the membrane that further self-assemble into multiple oligomeric species
por: Subburaj, Yamunadevi, et al.
Publicado: (2015)

Conformational Heterogeneity of Bax Helix 9 Dimer for Apoptotic Pore Formation
por: Liao, Chenyi, et al.
Publicado: (2016)

An amphipathic Bax core dimer forms part of the apoptotic pore wall in the mitochondrial␣membrane
por: Lv, Fujiao, et al.
Publicado: (2021)

Conformational study of the protegrin-1 (PG-1) dimer interaction with lipid bilayers and its effect
por: Jang, Hyunbum, et al.
Publicado: (2007)

Bax Activation Initiates the Assembly of a Multimeric Catalyst that Facilitates Bax Pore Formation in Mitochondrial Outer Membranes
por: Kushnareva, Yulia, et al.
Publicado: (2012)

Membrane insertion of the BAX core, but not latch domain, drives apoptotic pore formation
por: Flores-Romero, Hector, et al.
Publicado: (2017)

DNA-assisted oligomerization of pore-forming toxin monomers into precisely-controlled protein channels
por: Henning-Knechtel, Anja, et al.
Publicado: (2017)

The mechanism of Raf activation through dimerization
por: Zhang, Mingzhen, et al.
Publicado: (2021)

Molecular Recognition between Aβ-Specific Single-Domain Antibody and Aβ Misfolded Aggregates
por: Zhang, Mingzhen, et al.
Publicado: (2018)

A dimer between monomers and hexamers—Oligomeric variations in glucosamine-6-phosphate deaminase family
por: Srinivasachari, Sathya, et al.
Publicado: (2023)

Three-dimensional structure of Bax-mediated pores in membrane bilayers
por: Xu, X-P, et al.
Publicado: (2013)

Grb2 monomer–dimer equilibrium determines normal versus oncogenic function
por: Ahmed, Zamal, et al.
Publicado: (2015)

Creation of distinctive Bax-lipid complexes at mitochondrial membrane surfaces drives pore formation to initiate apoptosis
por: Clifton, Luke A., et al.
Publicado: (2023)

Mutational Analysis and Allosteric Effects in the HIV-1 Capsid Protein Carboxyl-Terminal Dimerization Domain
por: Yu, Xiang, et al.
Publicado: (2009)

Pro-apoptotic Bax molecules densely populate the edges of membrane pores
por: Kuwana, Tomomi, et al.
Publicado: (2016)

Corrigendum: Grb2 monomer–dimer equilibrium determines normal versus oncogenic function
por: Ahmed, Zamal, et al.
Publicado: (2015)

Taking deterministic control of membrane protein monomer–dimer measurements
por: Fleming, Karen G.
Publicado: (2018)

Medin Oligomer Membrane Pore Formation: A Potential Mechanism of Vascular Dysfunction
por: Younger, Scott, et al.
Publicado: (2020)

Visual and functional demonstration of growing Bax-induced pores in mitochondrial outer membranes
por: Gillies, Laura A, et al.
Publicado: (2015)

The quaternary assembly of KRas4B with Raf-1 at the membrane
por: Jang, Hyunbum, et al.
Publicado: (2020)

Regulating highly dynamic unstructured proteins and their coding mRNAs
por: Ma, Buyong, et al.
Publicado: (2009)

Protein dynamics and conformational selection in bidirectional signal transduction
por: Nussinov, Ruth, et al.
Publicado: (2012)

Structured Crowding and Its Effects on Enzyme Catalysis
por: Ma, Buyong, et al.
Publicado: (2013)

Bioinformatics Study of Cancer-Related Mutations within p53 Phosphorylation Site Motifs
por: Ji, Xiaona, et al.
Publicado: (2014)

JNK3 phosphorylates Bax protein and induces ability to form pore on bilayer lipid membrane
por: Gupta, Rajeev, et al.
Publicado: (2017)

Incorporation of Coumarin-Based Fluorescent Monomers into Co-Oligomeric Molecules
por: Teixeira, Edgar, et al.
Publicado: (2018)

Prebiotic oligomerization and self-assembly of structurally diverse xenobiological monomers
por: Chandru, Kuhan, et al.
Publicado: (2020)

Oncogenic KRAS G12D mutation promotes dimerization through a second, phosphatidylserine–dependent interface: a model for KRAS oligomerization
por: Lee, Ki-Young, et al.
Publicado: (2021)

The monomer-dimer algorithm and QCD at finite density
por: Karsch, Frithjof
Publicado: (1990)

Probing protein aggregation at buried interfaces: distinguishing between adsorbed protein monomers, dimers, and a monomer–dimer mixture in situ
por: Lu, Tieyi, et al.
Publicado: (2021)

Key residues of Bacillus thuringiensis Cry2Ab for oligomerization and pore-formation activity
por: Pan, Zhi-Zhen, et al.
Publicado: (2021)

Differential cooperation of oncogenes with p53 and Bax to induce apoptosis in rhabdomyosarcoma
por: Taylor, Alan C, et al.
Publicado: (2006)

Synergistic Interactions between Repeats in Tau Protein and Aβ Amyloids May Be Responsible for Accelerated Aggregation via Polymorphic States
por: Miller, Yifat, et al.
Publicado: (2011)

Structural and Functional Consequences of Phosphate–Arsenate Substitutions in Selected Nucleotides: DNA, RNA, and ATP
por: Xu, Yu, et al.
Publicado: (2012)

Polymorphism in Alzheimer Aβ Amyloid Organization Reflects Conformational Selection in a Rugged Energy Landscape
por: Miller, Yifat, et al.
Publicado: (2010)

Polymorphism in Self-Assembly of Peptide-Based β-Hairpin Contributes to Network Morphology and Hydrogel Mechanical Rigidity
por: Miller, Yifat, et al.
Publicado: (2014)

Antigen binding allosterically promotes Fc receptor recognition
por: Zhao, Jun, et al.
Publicado: (2018)

Inhibition of Bax protects neuronal cells from oligomeric Aβ neurotoxicity
por: Kudo, W, et al.
Publicado: (2012)

Tubulin Dimers Oligomerize before Their Incorporation into Microtubules
por: Mozziconacci, Julien, et al.
Publicado: (2008)

Cannot write session to /tmp/vufind_sessions/sess_tumokrbigbas0grejkcb88tenr