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The Journal of Membrane Biology
Resumen/Descripción – provisto por la editorial en inglés
The Journal of Membrane Biology is dedicated to publishing high-quality science related to membrane biology, biochemistry and biophysics. In particular, we welcome work that uses modern experimental or computational methods including but not limited to those with microscopy, diffraction, NMR, computer simulations, or biochemistry aimed at membrane associated or membrane embedded proteins or model membrane systems. These methods might be applied to study topics like membrane protein structure and function, membrane mediated or controlled signaling mechanisms, cell-cell communication via gap junctions, the behavior of proteins and lipids based on monolayer or bilayer systems, or genetic and regulatory mechanisms controlling membrane function.Palabras clave – provistas por la editorial
No disponibles.
Disponibilidad
Institución detectada | Período | Navegá | Descargá | Solicitá |
---|---|---|---|---|
No detectada | desde ene. 1997 / hasta dic. 2023 | SpringerLink |
Información
Tipo de recurso:
revistas
ISSN impreso
0022-2631
ISSN electrónico
1432-1424
Editor responsable
Springer Nature
País de edición
Estados Unidos
Fecha de publicación
1969-
Cobertura temática
Tabla de contenidos
Role of Cholesterol and its Biosynthetic Precursors on Membrane Organization and Dynamics: A Fluorescence Approach
Sandeep Shrivastava; Yamuna Devi Paila; Amitabha Chattopadhyay
Palabras clave: Cell Biology; Physiology; Biophysics.
Pp. No disponible
Peptide Flexibility and the Hydrophobic Moment are Determinants to Evaluate the Clinical Potential of Magainins
Daniel Balleza
Palabras clave: Cell Biology; Physiology; Biophysics.
Pp. No disponible
Effect of γ-Oryzanol on the LE–LC Phase Coexistence Region of DPPC Langmuir Monolayer
Raghavendra; Bharat Kumar; Siva N. Chari
Palabras clave: Cell Biology; Physiology; Biophysics.
Pp. No disponible
The Effect of Benzyl Alcohol on the Voltage-Current Characteristics of Tethered Lipid Bilayers
Hadeel Alobeedallah; Bruce Cornell; Mohammed Ghazal; Hans Coster
Palabras clave: Cell Biology; Physiology; Biophysics.
Pp. No disponible
Cationic Proteins Rich in Lysine Residue Trigger Formation of Non-bilayer Lipid Phases in Model and Biological Membranes: Biophysical Methods of Study
Meiyi Li; Edward S. Gasanoff
Palabras clave: Cell Biology; Physiology; Biophysics.
Pp. No disponible
Role of Hydrophobic Amino-Acid Side-Chains in the Narrow Selectivity Filter of the CFTR Chloride Channel Pore in Conductance and Selectivity
Paul Linsdell
Palabras clave: Cell Biology; Physiology; Biophysics.
Pp. No disponible
Study of the Membrane Activity of the Synthetic Peptide ∆M3 Against Extended-Spectrum β-lactamase Escherichia coli Isolates
Estefanía Fandiño-Devia; Gloria A. Santa-González; Maria C. Klaiss-Luna; Marcela Manrique-Moreno
<jats:title>Abstract</jats:title><jats:p><jats:italic>Escherichia coli</jats:italic> is the most common microorganism causing nosocomial or community-acquired bacteremia, and extended-spectrum <jats:italic>β</jats:italic>-lactamase-producing <jats:italic>Escherichia coli</jats:italic> isolates are identified worldwide with increasing frequency. For this reason, it is necessary to evaluate potential new molecules like antimicrobial peptides. They are recognized for their biological potential which makes them promising candidates in the fight against infections. The goal of this research was to evaluate the potential of the synthetic peptide ΔM3 on several extended-spectrum <jats:italic>β</jats:italic>-lactamase producing <jats:italic>E. coli</jats:italic> isolates. The antimicrobial and cytotoxic activity of the peptide was spectrophotometrically determined. Additionally, the capacity of the peptide to interact with the bacterial membrane was monitored by fluorescence microscopy and infrared spectroscopy. The results demonstrated that the synthetic peptide is active against <jats:italic>Escherichia coli</jats:italic> isolates at concentrations similar to Meropenem. On the other hand, no cytotoxic effect was observed in HaCaT keratinocyte cells even at 10 times the minimal inhibitory concentration. Microscopy results showed a permeabilizing effect of the peptide on the bacteria. The infrared results showed that ΔM3 showed affinity for the lipids of the microorganism’s membrane. The results suggest that the ∆M3 interacts with the negatively charged lipids from the <jats:italic>E. coli</jats:italic> by a disturbing effect on membrane. Finally, the secondary structure experiments of the peptide showed a random structure in solution that did not change during the interaction with the membranes.</jats:p> <jats:p><jats:bold>Graphic Abstract</jats:bold></jats:p>
Palabras clave: Cell Biology; Physiology; Biophysics.
Pp. No disponible
Potential Role of Nrf2, HER2, and ALDH in Cancer Stem Cells: A Narrative Review
Azadeh Fakhrioliaei; Sepideh Tanhaei; SeyedAbbas Pakmehr; Maha Noori Shakir; Maytham T. Qasim; Maryam Hariri; Alireza Nouhi Kararoudi; Mohammad Valilo
Palabras clave: Cell Biology; Physiology; Biophysics.
Pp. No disponible
Bioinformatic Study of Possible Acute Regulation of Acid Secretion in the Stomach
Yan Hay Grace Lee; Nicole T. Cerf; Nicholas Shalaby; Mónica R. Montes; Ronald J. Clarke
<jats:title>Abstract</jats:title><jats:p>The gastric H<jats:sup>+</jats:sup>,K<jats:sup>+</jats:sup>-ATPase is an integral membrane protein which derives energy from the hydrolysis of ATP to transport H<jats:sup>+</jats:sup> ions from the parietal cells of the gastric mucosa into the stomach in exchange for K<jats:sup>+</jats:sup> ions. It is responsible for the acidic environment of the stomach, which is essential for digestion. Acid secretion is regulated by the recruitment of the H<jats:sup>+</jats:sup>,K<jats:sup>+</jats:sup>-ATPase from intracellular stores into the plasma membrane on the ingestion of food. The similar amino acid sequences of the lysine-rich N-termini α-subunits of the H<jats:sup>+</jats:sup>,K<jats:sup>+</jats:sup>- and Na<jats:sup>+</jats:sup>,K<jats:sup>+</jats:sup>-ATPases, suggests similar acute regulation mechanisms, specifically, an electrostatic switch mechanism involving an interaction of the N-terminal tail with the surface of the surrounding membrane and a modulation of the interaction via regulatory phosphorylation by protein kinases. From a consideration of sequence alignment of the H<jats:sup>+</jats:sup>,K<jats:sup>+</jats:sup>-ATPase and an analysis of its coevolution with protein kinase C and kinases of the Src family, the evidence points towards a phosphorylation of tyrosine-7 of the N-terminus by either Lck or Yes in all vertebrates except cartilaginous fish. The results obtained will guide and focus future experimental research.</jats:p>
Palabras clave: Cell Biology; Physiology; Biophysics.
Pp. No disponible
Construction and Analysis of a Mitochondrial Metabolism-Related Prognostic Model for Breast Cancer to Evaluate Survival and Immunotherapy
Yuting Lin; Zhongxin Huang; Baogen Zhang; Hanhui Yang; Shu Yang
Palabras clave: Cell Biology; Physiology; Biophysics.
Pp. No disponible