ArticleBiochemistry2012
Characterization of a cobalt-specific P(1B)-ATPase.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 32 citations in OpenAlex.
- Effluxosomes and the evolution of metal resistance inInfection and immunity · 2026Review
- Non-hyperbolic enzyme kinetics: the case of P-type ATPases.Biophysical reviews · 2025Review
- Reconsidering theACS bio & med chem Au · 2022Article
- A Novel Zinc Exporter CtpG Enhances Resistance to Zinc Toxicity and Survival in Mycobacterium bovis.Microbiology spectrum · 2022Article
- Structure and ion-release mechanism of PeLife · 2021Article
- Genomic Insights Into Cadmium Resistance of a Newly Isolated, Plasmid-FreeFrontiers in microbiology · 2021Article
- Asymmetric functions of a binuclear metal center within the transport pathway of a human zinc transporter ZIP4.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Cobalt in athletes: hypoxia and doping - new crossroads.Journal of applied biomedicine · 2019Review
- CuProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Ferrous iron efflux systems in bacteria.Metallomics : integrated biometal science · 2017Review
- A novel heavy metal ATPase peptide from Prosopis juliflora is involved in metal uptake in yeast and tobacco.Transgenic research · 2017Article
- Metal Selectivity of a Cd-, Co-, and Zn-Transporting PBiochemistry · 2017Article
- The Listeria monocytogenes Fur-regulated virulence protein FrvA is an Fe(II) efflux P1B4 -type ATPase.Molecular microbiology · 2016Article
- Fine-tuning of Substrate Affinity Leads to Alternative Roles of Mycobacterium tuberculosis Fe2+-ATPases.The Journal of biological chemistry · 2016Article
- A new metal binding domain involved in cadmium, cobalt and zinc transport.Nature chemical biology · 2015Article
- A sulfur-based transport pathway in Cu+-ATPases.EMBO reports · 2015Article
- Diversity of the metal-transporting P1B-type ATPases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- Differential roles for the Co(2+) /Ni(2+) transporting ATPases, CtpD and CtpJ, in Mycobacterium tuberculosis virulence.Molecular microbiology · 2014Article
- Sinorhizobium meliloti Nia is a P(1B-5)-ATPase expressed in the nodule during plant symbiosis and is involved in Ni and Fe transport.Metallomics : integrated biometal science · 2013Article
- A novel P(1B)-type Mn2+-transporting ATPase is required for secreted protein metallation in mycobacteria.The Journal of biological chemistry · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The P(1B)-type ATPases are a ubiquitous family of P-type ATPases involved in the transport of transition metal ions. Divided into subclasses based on sequence characteristics and substrate specificity, these integral membrane transporters play key roles in metal homeostasis, metal tolerance, and the biosynthesis of metalloproteins. The P(1B-4)-ATPases have the simplest architecture of the five P(1B)-ATPase families and have been suggested to play a role in Co(2+) transport. A P(1B-4)-ATPase from Sulfitobacter sp. NAS-14.1, designated sCoaT, has been cloned, expressed, and purified. Activity assays indicate that sCoaT is specific for Co(2+). A single Co(2+) binding site is present, and optical, electron paramagnetic resonance, and X-ray absorption spectroscopic data are consistent with tetrahedral coordination by oxygen and nitrogen ligands, including a histidine and likely a water. Surprisingly, there is no evidence for coordination by sulfur. Mutation of a conserved cysteine residue, Cys 327, in the signature transmembrane Ser-Pro-Cys metal binding motif does not abolish the ATP hydrolysis activity or affect the spectroscopic analysis, establishing that this residue is not involved in the initial Co(2+) binding by sCoaT. In contrast, replacements of conserved transmembrane residues Ser 325, His 657, Glu 658, and Thr 661 with alanine abolish ATP hydrolysis activity and Co(2+) binding, indicating that these residues are necessary for Co(2+) transport. These data represent the first in vitro characterization of a P(1B-4)-ATPase and its Co(2+) binding site.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.