LIVIVO - Search results -

Search results

Result 1 - 10 of total 50

Search options

Article ; Online: Mitochondria function in cytoplasmic FeS protein biogenesis.

Dancis, Andrew / Pandey, Ashutosh K / Pain, Debkumar

Biochimica et biophysica acta. Molecular cell research

2024 Volume 1871, Issue 5, Page(s) 119733

Abstract: Iron‑sulfur (FeS) clusters are cofactors of numerous proteins involved in essential cellular functions including respiration, protein translation, DNA synthesis and repair, ribosome maturation, anti-viral responses, and isopropylmalate isomerase activity. ...

Abstract	Iron‑sulfur (FeS) clusters are cofactors of numerous proteins involved in essential cellular functions including respiration, protein translation, DNA synthesis and repair, ribosome maturation, anti-viral responses, and isopropylmalate isomerase activity. Novel FeS proteins are still being discovered due to the widespread use of cryogenic electron microscopy (cryo-EM) and elegant genetic screens targeted at protein discovery. A complex sequence of biochemical reactions mediated by a conserved machinery controls biosynthesis of FeS clusters. In eukaryotes, a remarkable epistasis has been observed: the mitochondrial machinery, termed ISC (Iron-Sulfur Cluster), lies upstream of the cytoplasmic machinery, termed CIA (Cytoplasmic Iron‑sulfur protein Assembly). The basis for this arrangement is the production of a hitherto uncharacterized intermediate, termed X-S or (Fe-S)
Language	English
Publishing date	2024-04-18
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamcr.2024.119733
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.247: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Essential mitochondrial role in iron-sulfur cluster assembly of the cytoplasmic isopropylmalate isomerase Leu1 in Saccharomyces cerevisiae.

Pandey, Ashutosh K / Pain, Jayashree / J, Brindha / Dancis, Andrew / Pain, Debkumar

Mitochondrion

2023 Volume 69, Page(s) 104–115

Abstract: Iron-sulfur (Fe-S) cluster assembly in mitochondria and cytoplasm is essential for cell viability. In the yeast S. cerevisiae, Leu1 [4Fe-4S] is the cytoplasmic isopropylmalate isomerase involved in leucine biosynthesis. Using permeabilized Δleu1 cells ... ...

Abstract	Iron-sulfur (Fe-S) cluster assembly in mitochondria and cytoplasm is essential for cell viability. In the yeast S. cerevisiae, Leu1 [4Fe-4S] is the cytoplasmic isopropylmalate isomerase involved in leucine biosynthesis. Using permeabilized Δleu1 cells and recombinant apo-Leu1
MeSH term(s)	Cytoplasm/metabolism ; Iron/metabolism ; Iron-Sulfur Proteins/genetics ; Iron-Sulfur Proteins/metabolism ; Mitochondria/metabolism ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Sulfur/metabolism ; Hydro-Lyases/genetics ; Hydro-Lyases/metabolism
Chemical Substances	Iron (E1UOL152H7) ; Iron-Sulfur Proteins ; isopropylmalate isomerase (EC 4.2.1.33) ; Saccharomyces cerevisiae Proteins ; Sulfur (70FD1KFU70) ; LEU1 protein, S cerevisiae (EC 4.2.1.33) ; Hydro-Lyases (EC 4.2.1.-)
Language	English
Publishing date	2023-02-09
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2056923-3
ISSN	1872-8278 ; 1567-7249
ISSN (online)	1872-8278
ISSN	1567-7249
DOI	10.1016/j.mito.2023.02.006
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Child Neurology: Progressive Cerebellar Atrophy and Retinal Dystrophy: Clues to an Ultrarare

Lail, Noor / Pandey, Ashutosh K / Venkatesh, Sundararajan / Noland, Roberto D / Swanson, Gabriel / Pain, Debkumar / Branson, Helen M / Suzuki, Carolyn K / Yoon, Grace

Neurology

2023 Volume 101, Issue 15, Page(s) e1567–e1571

Abstract: Pathogenic biallelic variants ... ...

Abstract	Pathogenic biallelic variants in
MeSH term(s)	Female ; Humans ; Child ; Child, Preschool ; Aconitate Hydratase ; Retinal Dystrophies/diagnosis ; Retinal Dystrophies/genetics ; Microcephaly ; Nervous System Malformations ; Atrophy
Chemical Substances	Aconitate Hydratase (EC 4.2.1.3) ; ACO2 protein, human (EC 4.2.1.3)
Language	English
Publishing date	2023-07-17
Publishing country	United States
Document type	Case Reports ; Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	207147-2
ISSN	1526-632X ; 0028-3878
ISSN (online)	1526-632X
ISSN	0028-3878
DOI	10.1212/WNL.0000000000207649
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Ui II Zs.153: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
Zs.MG 18: Show issues
Zs.MO 374: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Mitochondria export iron-sulfur and sulfur intermediates to the cytoplasm for iron-sulfur cluster assembly and tRNA thiolation in yeast.

Pandey, Ashutosh K / Pain, Jayashree / Dancis, Andrew / Pain, Debkumar

The Journal of biological chemistry

2019 Volume 294, Issue 24, Page(s) 9489–9502

Abstract: Iron-sulfur clusters are essential cofactors of proteins. In eukaryotes, iron-sulfur cluster biogenesis requires a mitochondrial iron-sulfur cluster machinery (ISC) and a cytoplasmic iron-sulfur protein assembly machinery (CIA). Here we used mitochondria ...

Abstract	Iron-sulfur clusters are essential cofactors of proteins. In eukaryotes, iron-sulfur cluster biogenesis requires a mitochondrial iron-sulfur cluster machinery (ISC) and a cytoplasmic iron-sulfur protein assembly machinery (CIA). Here we used mitochondria and cytoplasm isolated from yeast cells, and [
MeSH term(s)	Biological Transport ; Cytoplasm/metabolism ; Iron/metabolism ; Iron-Sulfur Proteins/metabolism ; Mitochondrial Proteins/metabolism ; RNA, Fungal/metabolism ; RNA, Transfer/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Sulfhydryl Compounds/metabolism ; Sulfur/metabolism
Chemical Substances	Iron-Sulfur Proteins ; Mitochondrial Proteins ; RNA, Fungal ; Saccharomyces cerevisiae Proteins ; Sulfhydryl Compounds ; Sulfur (70FD1KFU70) ; RNA, Transfer (9014-25-9) ; Iron (E1UOL152H7)
Language	English
Publishing date	2019-04-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA119.008600
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.108: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Roles of Fe-S proteins: from cofactor synthesis to iron homeostasis to protein synthesis.

Pain, Debkumar / Dancis, Andrew

Current opinion in genetics & development

2016 Volume 38, Page(s) 45–51

Abstract: Fe-S cluster assembly is an essential process for all cells. Impairment of Fe-S cluster assembly creates diseases in diverse and surprising ways. In one scenario, the loss of function of lipoic acid synthase, an enzyme with Fe-S cluster cofactor in ... ...

Abstract	Fe-S cluster assembly is an essential process for all cells. Impairment of Fe-S cluster assembly creates diseases in diverse and surprising ways. In one scenario, the loss of function of lipoic acid synthase, an enzyme with Fe-S cluster cofactor in mitochondria, impairs activity of various lipoamide-dependent enzymes with drastic consequences for metabolism. In a second scenario, the heme biosynthetic pathway in red cell precursors is specifically targeted, and iron homeostasis is perturbed, but lipoic acid synthesis is unaffected. In a third scenario, tRNA modifications arising from action of the cysteine desulfurase and/or Fe-S cluster proteins are lost, which may lead to impaired protein synthesis. These defects can then result in cancer, neurologic dysfunction or type 2 diabetes.
MeSH term(s)	Carbon-Sulfur Lyases/genetics ; Diabetes Mellitus, Type 2/genetics ; Diabetes Mellitus, Type 2/metabolism ; Erythrocytes/metabolism ; Heme/biosynthesis ; Heme/genetics ; Humans ; Iron/metabolism ; Iron-Sulfur Proteins/genetics ; Iron-Sulfur Proteins/metabolism ; Mitochondria/genetics ; Mitochondria/metabolism ; Multigene Family ; Neoplasms/genetics ; Neoplasms/metabolism ; Protein Biosynthesis/genetics ; RNA, Transfer/genetics ; Sulfurtransferases/genetics
Chemical Substances	Iron-Sulfur Proteins ; Heme (42VZT0U6YR) ; RNA, Transfer (9014-25-9) ; Iron (E1UOL152H7) ; Sulfurtransferases (EC 2.8.1.-) ; lipoic acid synthase (EC 2.8.1.-) ; Carbon-Sulfur Lyases (EC 4.4.-) ; cysteine desulfurase (EC 4.4.1.-)
Language	English
Publishing date	2016-04-07
Publishing country	England
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1077312-5
ISSN	1879-0380 ; 0959-437X
ISSN (online)	1879-0380
ISSN	0959-437X
DOI	10.1016/j.gde.2016.03.006
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 3240: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Splitting the functions of Rim2, a mitochondrial iron/pyrimidine carrier.

Knight, Simon A B / Yoon, Heeyong / Pandey, Ashutosh K / Pain, Jayashree / Pain, Debkumar / Dancis, Andrew

Mitochondrion

2019 Volume 47, Page(s) 256–265

Abstract: Rim2 is an unusual mitochondrial carrier protein capable of transporting both iron and pyrimidine nucleotides. Here we characterize two point mutations generated in the predicted substrate-binding site, finding that they yield disparate effects on iron ... ...

Abstract	Rim2 is an unusual mitochondrial carrier protein capable of transporting both iron and pyrimidine nucleotides. Here we characterize two point mutations generated in the predicted substrate-binding site, finding that they yield disparate effects on iron and pyrimidine transport. The Rim2 (E248A) mutant was deficient in mitochondrial iron transport activity. By contrast, the Rim2 (K299A) mutant specifically abrogated pyrimidine nucleotide transport and exchange, while leaving iron transport activity largely unaffected. Strikingly, E248A preserved TTP/TTP homoexchange but interfered with TTP/TMP heteroexchange, perhaps because proton coupling was dependent on the E248 acidic residue. Rim2-dependent iron transport was unaffected by pyrimidine nucleotides. Rim2-dependent pyrimidine transport was competed by Zn
MeSH term(s)	Amino Acid Substitution ; Iron/metabolism ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Mutation, Missense ; Nucleotide Transport Proteins/genetics ; Nucleotide Transport Proteins/metabolism ; Pyrimidines/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	Mitochondrial Proteins ; Nucleotide Transport Proteins ; Pyrimidines ; RIM2 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Iron (E1UOL152H7) ; pyrimidine (K8CXK5Q32L)
Language	English
Publishing date	2019-01-18
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2056923-3
ISSN	1872-8278 ; 1567-7249
ISSN (online)	1872-8278
ISSN	1567-7249
DOI	10.1016/j.mito.2018.12.005
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Characteristics of the Isu1 C-terminus in relation to [2Fe-2S] cluster assembly and ISCU Myopathy.

Lewis, Brianne E / Campbell, Courtney J / Rodrigues, Andria / Thompson, Lindsey / Pandey, Ashutosh K / Gallagher, Sarah N / Pain, Debkumar / Dancis, Andrew / Stemmler, Timothy L

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry

2022 Volume 27, Issue 8, Page(s) 759–773

Abstract: Mitochondrial [2Fe-2S] cluster biosynthesis is driven by the coordinated activities of the Iron-Sulfur Cluster (ISC) pathway protein machinery. Within the ISC machinery, the protein that provides a structural scaffold on which [2Fe-2S] clusters are ... ...

Abstract	Mitochondrial [2Fe-2S] cluster biosynthesis is driven by the coordinated activities of the Iron-Sulfur Cluster (ISC) pathway protein machinery. Within the ISC machinery, the protein that provides a structural scaffold on which [2Fe-2S] clusters are assembled is the ISCU protein in humans; this protein is referred to as the "Scaffold" protein. Truncation of the C-terminal portion of ISCU causes the fatal disease "ISCU Myopathy", which exhibits phenotypes of reduced Fe-S cluster assembly in cells. In this report, the yeast ISCU ortholog "Isu1" has been characterized to gain a better understanding of the role of the scaffold protein in relation to [2Fe-2S] assembly and ISCU Myopathy. Here we explored the biophysical characteristics of the C-terminal region of Isu1, the segment of the protein that is truncated on the human ortholog during the disease ISCU Myopathy. We characterized the role of this region in relation to iron binding, protein stability, assembly of the ISC multiprotein complex required to accomplish Fe-S cluster assembly, and finally on overall cell viability. We determined the Isu1 C-terminus is essential for the completion of the Fe-S cluster assembly but serves a function independent of protein iron binding.
MeSH term(s)	Humans ; Iron-Sulfur Proteins/metabolism ; Saccharomyces cerevisiae/metabolism ; Iron/metabolism ; Muscular Diseases ; Mitochondrial Proteins/chemistry ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	sulofenur (Z45N070N3S) ; Iron-Sulfur Proteins ; Iron (E1UOL152H7) ; ISCU protein, human ; ISU1 protein, S cerevisiae ; Mitochondrial Proteins ; Saccharomyces cerevisiae Proteins
Language	English
Publishing date	2022-10-30
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, N.I.H., Extramural
ZDB-ID	1464026-0
ISSN	1432-1327 ; 0949-8257
ISSN (online)	1432-1327
ISSN	0949-8257
DOI	10.1007/s00775-022-01964-1
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

Order via subito

Details ▾
- Full text online
- Order with fees

Article ; Online: Mitochondria Export Sulfur Species Required for Cytosolic tRNA Thiolation.

Pandey, Alok / Pain, Jayashree / Dziuba, Nathaniel / Pandey, Ashutosh K / Dancis, Andrew / Lindahl, Paul A / Pain, Debkumar

Cell chemical biology

2018 Volume 25, Issue 6, Page(s) 738–748.e3

Abstract: In eukaryotes, mitochondria have been hypothesized to generate sulfur species required for tRNA thiolation in the cytosol, although no direct evidence thus far exists. Here we have detected these sulfur species, making use of our observation that ... ...

Abstract	In eukaryotes, mitochondria have been hypothesized to generate sulfur species required for tRNA thiolation in the cytosol, although no direct evidence thus far exists. Here we have detected these sulfur species, making use of our observation that isolated yeast cytosol alone is unable to thiolate tRNAs but can do so upon addition of mitochondria. Mitochondria were found to utilize the cysteine desulfurase Nfs1 to produce sulfur-containing species with masses ranging from 700 to 1,100 Da. Mitochondria exported these species via the Atm1 transporter in the inner membrane. Once exported to the cytosol, these sulfur species promoted cytosolic tRNA thiolation with no further requirement of mitochondria. Furthermore, we found that the Isu1/2 scaffolds but not the Ssq1 chaperone of the mitochondrial iron-sulfur cluster machinery were required for cytosolic tRNA thiolation, and thus the sulfur utilization pathway bifurcates at the Isu1/2 site for intra-organellar use in mitochondria or export to the cytosol.
MeSH term(s)	Carbon-Sulfur Lyases/chemistry ; Carbon-Sulfur Lyases/metabolism ; Cytosol/chemistry ; Cytosol/metabolism ; Humans ; Mitochondria/chemistry ; Mitochondria/metabolism ; RNA, Transfer/chemistry ; RNA, Transfer/metabolism ; Sulfhydryl Compounds/chemistry ; Sulfhydryl Compounds/metabolism ; Sulfur/chemistry ; Sulfur/metabolism
Chemical Substances	Sulfhydryl Compounds ; Sulfur (70FD1KFU70) ; RNA, Transfer (9014-25-9) ; Carbon-Sulfur Lyases (EC 4.4.-) ; NFS1 protein, human (EC 4.4.1.-)
Language	English
Publishing date	2018-04-26
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	2451-9448
ISSN (online)	2451-9448
DOI	10.1016/j.chembiol.2018.04.002
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article: Nfs1 cysteine desulfurase protein complexes and phosphorylation sites as assessed by mass spectrometry.

Rocha, Agostinho G / Knight, Simon A B / Pandey, Alok / Yoon, Heeyong / Pain, Jayashree / Pain, Debkumar / Dancis, Andrew

Data in brief

2017 Volume 15, Page(s) 775–799

Abstract: Fe-S clusters are cofactors that participate in diverse and essential biological processes. Mitochondria contain a complete machinery for Fe-S cluster assembly. Cysteine desulfurase (Nfs1) is required generation of a form of activated sulfur and is ... ...

Abstract	Fe-S clusters are cofactors that participate in diverse and essential biological processes. Mitochondria contain a complete machinery for Fe-S cluster assembly. Cysteine desulfurase (Nfs1) is required generation of a form of activated sulfur and is essential for the initial Fe-S cluster assembly step. Using mass-spectometry we identified proteins that were copurified with Nfs1 using a pull-down strategy, including a novel protein kinase. Furthermore, we were able to identify phosphorylation sites on the Nfs1 protein. These data and analyses support the research article "Cysteine desulfurase is regulated by phosphorylation of Nfs1 in yeast mitochondria" by Rocha et al. (in press) [1].
Language	English
Publishing date	2017-10-06
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2786545-9
ISSN	2352-3409
ISSN	2352-3409
DOI	10.1016/j.dib.2017.09.068
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Persulfide formation on mitochondrial cysteine desulfurase: enzyme activation by a eukaryote-specific interacting protein and Fe-S cluster synthesis.

Pandey, Alok / Golla, Ramesh / Yoon, Heeyong / Dancis, Andrew / Pain, Debkumar

The Biochemical journal

2015 Volume 448, Issue 2, Page(s) 171–187

Abstract: Cysteine desulfurases abstract sulfur from the substrate cysteine, generate a covalent persulfide on the active site cysteine of the enzyme, and then donate the persulfide sulfur to various recipients such as Fe-S clusters. In Saccharomyces cerevisiae, ... ...

Abstract	Cysteine desulfurases abstract sulfur from the substrate cysteine, generate a covalent persulfide on the active site cysteine of the enzyme, and then donate the persulfide sulfur to various recipients such as Fe-S clusters. In Saccharomyces cerevisiae, the Nfs1p protein is the only known cysteine desulfurase, and it forms a complex with Isd11p (Nfs1p·Isd11p). Both of these proteins are found primarily in mitochondria and both are essential for cell viability. In the present study we show, using the results of experiments with isolated mitochondria and purified proteins, that Isd11p is required for the cysteine desulfurase activity of Nfs1p. Whereas Nfs1p by itself was inactive, the Nfs1p·Isd11p complex formed persulfide and was active as a cysteine desulfurase. In the absence of Isd11p, Nfs1p was able to bind the substrate cysteine but failed to form a persulfide. Addition of Isd11p allowed Nfs1p with bound substrate to generate a covalent persulfide. We suggest that Isd11p induces an activating conformational change in Nfs1p to bring the bound substrate and the active site cysteine in proximity for persulfide formation. Thus mitochondrial Nfs1p is different from bacterial cysteine desulfurases that are active in the absence of accessory proteins. Isd11p may serve to regulate cysteine desulfurase activity in mitochondria.
MeSH term(s)	Alleles ; Carbon-Sulfur Lyases/genetics ; Carbon-Sulfur Lyases/metabolism ; Enzyme Activation ; Genes, Fungal ; Iron-Sulfur Proteins/genetics ; Iron-Sulfur Proteins/metabolism ; Mitochondria/metabolism ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Models, Biological ; Multienzyme Complexes/genetics ; Multienzyme Complexes/metabolism ; Mutation ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Sulfides/metabolism ; Sulfurtransferases/genetics ; Sulfurtransferases/metabolism
Chemical Substances	Iron-Sulfur Proteins ; Isd11 protein, S cerevisiae ; Mitochondrial Proteins ; Multienzyme Complexes ; Recombinant Proteins ; Saccharomyces cerevisiae Proteins ; Sulfides ; persulfides ; Sulfurtransferases (EC 2.8.1.-) ; NFS1 protein, S cerevisiae (EC 2.8.1.7) ; Carbon-Sulfur Lyases (EC 4.4.-) ; cysteine desulfurase (EC 4.4.1.-)
Language	English
Publishing date	2015-05-05
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2969-5
ISSN	1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
ISSN (online)	1470-8728
ISSN	0006-2936 ; 0306-3275 ; 0264-6021
DOI	10.1042/BJ20120951
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.110: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito