Deepa V. Dabir

ORCID: 0000-0002-9149-9614
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About
Contact & Profiles
Research Areas
  • Mitochondrial Function and Pathology
  • ATP Synthase and ATPases Research
  • Alzheimer's disease research and treatments
  • Metal-Catalyzed Oxygenation Mechanisms
  • Photosynthetic Processes and Mechanisms
  • Endoplasmic Reticulum Stress and Disease
  • Neuroscience and Neuropharmacology Research
  • Prion Diseases and Protein Misfolding
  • Neuroinflammation and Neurodegeneration Mechanisms
  • Metalloenzymes and iron-sulfur proteins
  • Liver physiology and pathology
  • Sperm and Testicular Function
  • Neurological Disorders and Treatments
  • Neurological Disease Mechanisms and Treatments
  • Heat shock proteins research
  • Metabolism and Genetic Disorders
  • DNA Repair Mechanisms
  • Cancer, Hypoxia, and Metabolism
  • Pharmacological Effects and Toxicity Studies
  • Bone health and osteoporosis research
  • Enzyme Structure and Function
  • Redox biology and oxidative stress
  • RNA and protein synthesis mechanisms
  • Biotin and Related Studies
  • Click Chemistry and Applications

Loyola Marymount University
2012-2024

Dabur (India)
2015

Sappasithiprasong Hospital
2015

University of California, Los Angeles
2007-2013

University of Pennsylvania
2003-2006

Carl von Ossietzky Universität Oldenburg
2004

Philadelphia University
2003

Society for Neuroscience
2003

Filamentous tau inclusions in neurons and glia are neuropathological hallmarks of sporadic familial tauopathies. Because gene mutations pathogenic for the autosomal dominant tauopathy “frontotemporal dementia parkinsonism linked to chromosome 17,” abnormalities implicated directly onset and/or progression disease. Although filamentous aggregates acknowledged play roles degenerative mechanisms resulting neuron loss, contributions glial pathology neurodegeneration remain essentially...

10.1523/jneurosci.0081-05.2005 article EN cc-by-nc-sa Journal of Neuroscience 2005-04-06

Filamentous tau inclusions in neurons and glia are neuropathological hallmarks of tauopathies. The discovery microtubule-associated protein gene mutations that pathogenic for a heterogenous group neurodegenerative disorders, called frontotemporal dementia parkinsonism linked to chromosome-17 (FTDP-17), directly implicate abnormalities the onset/progression disease. Although role pathology disease pathogenesis is well accepted, contribution glial essentially unknown. We recently generated...

10.1523/jneurosci.3861-05.2006 article EN cc-by-nc-sa Journal of Neuroscience 2006-01-11

Mia40 and Erv1 execute a disulfide relay to import the small Tim proteins into mitochondrial intermembrane space. Here, we have reconstituted oxidative folding pathway in vitro with Tim13 as substrate determined midpoint potentials of Tim13. Specifically, served direct oxidant Tim13, was required reoxidize Mia40. During oxidation, four electrons were transferred from insertion two bonds succession. The extent oxidation directly dependent on concentration independent concentration....

10.1091/mbc.e08-10-1062 article EN Molecular Biology of the Cell 2009-05-29

Tau-positive inclusions in oligodendrocytes are consistent neuropathological features of corticobasal degeneration, progressive supranuclear palsy, and frontotemporal dementias with Parkinsonism linked to chromosome 17. Here we show by immunohistochemistry that tau-positive oligodendroglial inclusion bodies also contain the small heat-shock protein (HSP) alphaB-crystallin but not HSP70. To study molecular mechanisms underlying body formation, engineered an oligodendroglia cell line (OLN-t40)...

10.1523/jneurosci.23-26-08872.2003 article EN Journal of Neuroscience 2003-10-01

Prokaryotes have aerobic and anaerobic electron acceptors for oxidative folding of periplasmic proteins. The mitochondrial intermembrane space has an analogous pathway with the oxidoreductase Mia40 sulfhydryl oxidase Erv1, termed assembly (MIA) pathway. include oxygen cytochrome c, but acceptor that can function under conditions not been identified. Here we show fumarate reductase Osm1, which facilitates transfer from to succinate, fills this gap as a new acceptor. In addition microsomes,...

10.1091/mbc.e16-10-0712 article EN cc-by-nc-sa Molecular Biology of the Cell 2017-08-16

The TIM22 protein import pathway mediates the of membrane proteins into mitochondrial inner and consists two intermembrane space chaperone complexes, Tim9-Tim10 Tim8-Tim13 complexes. To facilitate mechanistic studies, we developed a chemical-genetic approach to identify small molecule agonists that caused lethality tim10-1 yeast mutant at permissive temperature. One molecule, MitoBloCK-1, attenuated carrier including ADP/ATP phosphate carriers, but not used TIM23 or Mia40/Erv1 translocation...

10.1073/pnas.0914387107 article EN Proceedings of the National Academy of Sciences 2010-05-08

Meiosis 1 arresting protein (M1ap) is a novel vertebrate gene expressed exclusively in germ cells of the embryonic ovary and adult testis. In male mice, M1ap expression, which present from spermatogonia to secondary spermatocytes, evolutionarily conserved has specific spatial temporal pattern suggestive role during cell development. To test its function, mice deficient were created. Whereas females had histologically normal ovaries, males exhibited reduced testicular size myriad tubular...

10.1095/biolreprod.111.098673 article EN Biology of Reproduction 2012-12-27

The Mia40 import pathway facilitates the and oxidative folding of cysteine-rich protein substrates into mitochondrial intermembrane space. Here we describe in vitro organello Cmc1, a twin CX(9)C-containing substrate, which contains an unpaired cysteine. In vitro, Cmc1 can be oxidized by receptor alone when excess or at lower rate only sulfhydryl oxidase Erv1. However, physiological efficient oxidation requires Erv1 Mia40. forms stable intermediate with is released from this interaction...

10.1074/jbc.m112.383562 article EN cc-by Journal of Biological Chemistry 2012-07-06

Yeast is a facultative anaerobe and uses diverse electron acceptors to maintain redox-regulated import of cysteine-rich precursors via the mitochondrial intermembrane space assembly (MIA) pathway. With growing diversity substrates utilizing MIA pathway, understanding capacity (IMS) handle different types stress crucial. We used MS identify additional proteins that interacted with sulfhydryl oxidase Erv1 Altered inheritance mitochondria 32 (Aim32), thioredoxin-like [2Fe-2S] ferredoxin...

10.1016/j.jbc.2021.101135 article EN cc-by Journal of Biological Chemistry 2021-08-28

Mitochondrial respiratory complexes, the ATP synthase, and mitoribosomes have a genetic hybrid origin. Most of their components are encoded by nuclear genome few mitochondrial DNA (mtDNA). gene expression is finely regulated, yeast studies unveiled several regulatory events in translation proteins (Tang et al., 2020). ribosomes functionally specialized for synthesis essential inner membrane chain. Extensive interactions with factors involved all steps posttranscriptional occurs higher-order...

10.1016/j.jbc.2024.106696 article EN cc-by Journal of Biological Chemistry 2024-03-01

The mitochondrion is a key player in basic cellular homeostasis eukaryotic cells, contributing to the synthesis of ATP, prevention oxidative damage from reactive oxygen species and regulation cell death. In yeast, most mitochondrial proteins are synthesized cytoplasm imported post‐translationally into organelle. One particularly interesting translocation pathway Erv1 folding pathway, disulfide relay system comprising Mia40 that couples folding, oxidation import intermembrane space (IMS)....

10.1096/fasebj.30.1_supplement.600.14 article EN The FASEB Journal 2016-04-01
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