Results 41 to 50 of about 59,930 (249)

Special Delivery: Distributing Iron in the Cytosol of Mammalian cells

Frontiers in Pharmacology, 2014
Eukaryotic cells contain hundreds of proteins that require iron cofactors for activity. These iron enzymes are located in essentially every subcellular compartment; thus, iron cofactors must travel to every compartment in the cell.
Caroline C Philpott, Moon-Suhn eRyu
doaj   +1 more source

Structure and molecular evolution of CDGSH iron-sulfur domains. [PDF]

PLoS ONE, 2011
The recently discovered CDGSH iron-sulfur domains (CISDs) are classified into seven major types with a wide distribution throughout the three domains of life.
Jinzhong Lin, Liman Zhang, Shaomei Lai, Keqiong Ye   +3 more
doaj   +1 more source

Miniaturized metalloproteins: Application to iron–sulfur proteins [PDF]

Proceedings of the National Academy of Sciences, 2000
The miniaturization process applied to rubredoxins generated a class of peptide-based metalloprotein models, named METP ( m iniaturized e lectron t ransfer p rotein).
LOMBARDI, ANGELINA, MARASCO, DANIELA, O. MAGLIO, L. DI COSTANZO, NASTRI, FLAVIA, PAVONE, VINCENZO   +5 more
openaire   +4 more sources

Dynamics of Metal Centers Monitored by Nuclear Inelastic Scattering

, 2005
Nuclear inelastic scattering of synchrotron radiation has been used now since 10 years as a tool for vibrational spectroscopy. This method has turned out especially useful in case of large molecules that contain a M\"ossbauer active metal center.
A. Becke, A. I. Chumakov, A. McLean, A. Schaefer, A. Schaefer, A. Silvestri, A. Wachters, A. X. Trautwein, A.I. Chumakov, B.M. Leu, C. Schmidt, G. Barone, G. Barone, G. La Manna, H. Paulsen, H. Paulsen, H. Paulsen, H. Paulsen, H. Paulsen, H. Winkler, I. Sergueev, J. A. Wolny, J. Binkley, J. Kusz, J.T. Sage, K. Achterhold, K. Dobbs, K. Dobbs, K. Dobbs, L. H. Böttger, M. Gordon, M. Seto, O. Zakharieva, P. Hay, P. Wegner, R. Czernuszewicz, R. Krishnan, R. Rüffer, T. Asthalter, T. Cundari, U.A. Jayasooriya, V. Schünemann, V.S. Oganesyan, W. Pietro, W. Stevens, W. Stevens, W. Stuhrhahn   +46 more
core   +1 more source

Structure of a Wbl protein and implications for NO sensing by M. tuberculosis [PDF]

, 2017
Mycobacterium tuberculosis causes pulmonary tuberculosis (TB) and claims ~1.8 million human lives per annum. Host nitric oxide (NO) is important in controlling TB infection. M.
A Laganowsky, A Singh, A Singh, AJC Steyn, AM Abdallah, AT Brunger, B Zhang, CD Hengst Den, DM Hunt, G Karimova, I Bertini, I Bertini, J Burian, JA MacGurn, JA Soliveri, JC Crack, JC Crack, JC Crack, JC Crack, JD MacMicking, JL Flynn, KA Johnson, KF Chater, KM Guinn, L Feng, L Holm, L Rickman, LA Kelley, LG Wayne, LJ Smith, LJ Smith, M Bradford, M Sharma, M Sritharan, M Tiso, M Ventura, MI Voskuil, MP Williamson, MR Stapleton, MS Paget, N Agarwal, N Agarwal, N Banaiee, N Wel van der, O Neyrolles, P Jakimowicz, PN Serrano, RP Morris, S Balayssac, SA Stanley, SA Stanley, SM Fortune, ST Cole, TL Hadfield, VB Chen, VF Wendisch, Y Shen, Z Chen   +57 more
core   +3 more sources

The CRISPR associated protein Cas4 Is a 5' to 3' DNA exonuclease with an iron-sulfur cluster.

PLoS ONE, 2012
The Cas4 protein is one of the core CRISPR-associated (Cas) proteins implicated in the prokaryotic CRISPR system for antiviral defence. Cas4 is thought to play a role in the capture of new viral DNA sequences for incorporation into the host genome.
Jing Zhang, Taciana Kasciukovic, Malcolm F White   +2 more
doaj   +1 more source

Altered sterol metabolism in budding yeast affects mitochondrial iron–sulfur (Fe-S) cluster synthesis [PDF]

, 2018
Ergosterol synthesis is essential for cellular growth and viability of the budding yeast Saccharomyces cerevisiae, and intracellular sterol distribution and homeostasis are therefore highly regulated in this species. Erg25 is an iron-containing C4-methyl
Bard, Martin, Bhuiyan, Shah Alam, Chen, Opal S., Cox, James E., Kaplan, Jerry, Li, Liangtao, Natarajan, Selvamuthu K., Ward, Diane M.   +7 more
core   +1 more source

Structural biology of ferritin nanocages

FEBS Letters, EarlyView.
Ferritin is a conserved iron‐storage protein that sequesters iron as a ferric mineral core within a nanocage, protecting cells from oxidative damage and maintaining iron homeostasis. This review discusses ferritin biology, structure, and function, and highlights recent cryo‐EM studies revealing mechanisms of ferritinophagy, cellular iron uptake, and ...
Eloise Mastrangelo, Flavio Di Pisa
wiley   +1 more source

The Iron Maiden. Cytosolic Aconitase/IRP1 Conformational Transition in the Regulation of Ferritin Translation and Iron Hemostasis

Biomolecules, 2021
Maintaining iron homeostasis is fundamental for almost all living beings, and its deregulation correlates with severe and debilitating pathologies.
Cécilia Hognon, Emmanuelle Bignon, Guillaume Harle, Nadège Touche, Stéphanie Grandemange, Antonio Monari   +5 more
doaj   +1 more source

The site of synthesis of the iron-sulfur subunits of the flavoprotein and iron-protein fractions of human NADH dehydrogenase [PDF]

, 1988
The site of synthesis of the iron-sulfur subunits of the flavoprotein and iron-protein fractions of the human respiratory chain NADH dehydrogenase has been investigated to test the possibility that any of them is synthesized in mitochondria.
Attardi, Giuseppe, Chomyn, Anne, Cleeter, Michael W. J., Patel, Salil D., Ragan, C. Ian   +4 more
core