Magnus Monné

ORCID: 0000-0003-2344-3878
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About
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Research Areas
  • Mitochondrial Function and Pathology
  • Metabolism and Genetic Disorders
  • RNA and protein synthesis mechanisms
  • Lipid Membrane Structure and Behavior
  • RNA Interference and Gene Delivery
  • ATP Synthase and ATPases Research
  • Amino Acid Enzymes and Metabolism
  • Drug Transport and Resistance Mechanisms
  • Bacterial Genetics and Biotechnology
  • RNA modifications and cancer
  • Bacteriophages and microbial interactions
  • DNA and Nucleic Acid Chemistry
  • Sperm and Testicular Function
  • Glycosylation and Glycoproteins Research
  • Hepatitis B Virus Studies
  • Metabolomics and Mass Spectrometry Studies
  • Endoplasmic Reticulum Stress and Disease
  • Trace Elements in Health
  • Cholinesterase and Neurodegenerative Diseases
  • Reproductive Biology and Fertility
  • Biochemical Acid Research Studies
  • Natural Antidiabetic Agents Studies
  • Invertebrate Immune Response Mechanisms
  • Photosynthetic Processes and Mechanisms
  • Plant Virus Research Studies

University of Basilicata
2016-2025

University of Bari Aldo Moro
2015-2024

Karolinska Institutet
2006-2011

Medical Research Council
2004-2007

University of Groningen
2007

Wellcome Trust
2004-2005

Stockholm University
1998-2005

MRC Human Nutrition Research
2003

MRC Mitochondrial Biology Unit
2003

ABSTRACT Hepatitis C virus (HCV) belongs to the Hepacivirus genus in Flaviviridae family. Among least known viral proteins this family is nonstructural protein NS4B, which has been suggested be a part of replication complex. Hydrophobicity plots indicate common profile among NS4B from different members family, suggesting function. In order gain deeper understanding nature HCV we have determined localization and topology by using recombinant constructs. The localized endoplasmic reticulum...

10.1128/jvi.77.9.5428-5438.2003 article EN Journal of Virology 2003-04-11

Mitochondrial carriers are believed widely to be dimers both in structure and function. However, the structural fold is a barrel of six transmembrane alpha-helices without an obvious dimerisation interface. Here, we show by negative dominance studies that yeast mitochondrial ADP/ATP carrier 2 from Saccharomyces cerevisiae (AAC2) functional as monomer membrane. Adenine nucleotide transport wild-type AAC2 inhibited sulfhydryl reagent 2-sulfonatoethyl-methanethiosulfonate (MTSES), whereas...

10.1073/pnas.0703969104 article EN Proceedings of the National Academy of Sciences 2007-06-14

ABSTRACT Alzheimer's disease is a neurodegenerative chronic with severe social and economic impact in the societies, which still lacks an efficient therapy. Several pathophysiological events ( β ‐amyloid [A ] deposits, τ ‐protein aggregation, loss of cholinergic activity, oxidative stress) occurs progression disease. Therefore, search for multi‐targeted agents treatment becomes indispensable. In this paper we evaluated AChE inhibition by Ellman's method antioxidant activity DPPH assay nine...

10.1111/cbdd.70049 article EN Chemical Biology & Drug Design 2025-01-01

We have characterized the membrane topology of a 60-kDa inner protein from Escherichia coli that is homologous to recently identified Oxa1p in Saccharomyces cerevisiae mitochondria implicated assembly mitochondrial proteins. Hydrophobicity and alkaline phosphatase fusion analyses suggest with six transmembrane segments, including an N-terminal signal-anchor sequence not present Oxa1p. In contrast partial constructs, full-length folds into protease-resistant conformation, suggesting important...

10.1074/jbc.273.46.30415 article EN cc-by Journal of Biological Chemistry 1998-11-01

The overproduction of eukaryotic membrane proteins is a major impediment in their structural and functional characterization. Here we have used the nisin-inducible expression system Lactococcus lactis for 11 mitochondrial transport from yeast. They were expressed at high levels state cytoplasmic membrane. results also show that level influenced by N-terminal regions transporters. Expression improved >10-fold either replacing or truncating these adding lactococcal signal peptides. observed...

10.1110/ps.051689905 article EN Protein Science 2005-11-01
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