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Entry version 131 (02 Jun 2021)
Sequence version 1 (01 Aug 1998)
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Protein

NAD(P)H coenzyme A polysulfide/persulfide reductase

Gene

PH0572

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the NAD(P)H-dependent reduction of polysulfide, CoA-polysulfides, and CoA persulfide, as well as the reduction of a range of other small persulfides, including TNB and glutathione persulfides. The likely in vivo substrates are di-, poly-, and persulfide derivatives of coenzyme A, although polysulfide itself is also efficiently reduced (PubMed:23530771).

Shows coenzyme A disulfide reductase (CoADR) activity with both NADH and NADPH, with a preference for NADPH (PubMed:15720393).

May also play a role in the reduction of elemental sulfur (PubMed:23530771).

2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

FAD2 PublicationsNote: Binds 1 FAD per subunit.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 1.11 sec(-1) with CoA persulfide as substrate (in the presence of NADH). kcat is 1.50 sec(-1) with CoA persulfide as substrate (in the presence of NADPH). kcat is 1.07 sec(-1) with NADH as substrate (in the presence of CoA persulfide). kcat is 2.08 sec(-1) with NADPH as substrate (in the presence of CoA persulfide). kcat is 6.56 sec(-1) with CoA polysulfide as substrate (in the presence of NADH). kcat is 8.86 sec(-1) with NADH as substrate (in the presence of CoA polysulfide). kcat is 16.1 sec(-1) with NADPH as substrate (in the presence of CoA polysulfide). kcat is 1.04 sec(-1) with polysulfide as substrate (in the presence of NADH). kcat is 3.37 sec(-1) with TNB persulfide as substrate (in the presence of NADH). kcat is 0.69 sec(-1) with DTNB as substrate (in the presence of NADH).1 Publication
  1. KM=73 µM for NADH1 Publication
  2. KM=20.5 µM for CoA persulfide (in the presence of NADH)1 Publication
  3. KM=56.2 µM for CoA persulfide (in the presence of NADPH)1 Publication
  4. KM=13.9 µM for NADH (in the presence of CoA persulfide)1 Publication
  5. KM=12.7 µM for NADPH (in the presence of CoA persulfide)1 Publication
  6. KM=94.9 µM for CoA polysulfide (in the presence of NADH)1 Publication
  7. KM=125 µM for NADH (in the presence of CoA polysulfide)1 Publication
  8. KM=14.1 µM for NADPH (in the presence of CoA polysulfide)1 Publication
  9. KM=12.3 µM for polysulfide (in the presence of NADH)1 Publication
  10. KM=25.1 µM for TNB persulfide (in the presence of NADH)1 Publication
  11. KM=129 µM for DTNB (in the presence of NADH)1 Publication

    Temperature dependencei

    Optimum temperature is 85 degrees Celsius. Thermostable.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei27Coenzyme ACombined sources2 Publications1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei48Redox-active1 Publication1
    Binding sitei75Coenzyme ACombined sources2 Publications1
    Binding sitei85FAD; via amide nitrogen and carbonyl oxygenCombined sources2 Publications1
    Binding sitei283FADCombined sources2 Publications1
    Binding sitei301FAD; via amide nitrogenCombined sources1 Publication1
    Binding sitei305Coenzyme ACombined sources2 Publications1
    Binding sitei361Coenzyme A; via carbonyl oxygenCombined sources2 Publications1
    Binding sitei425FAD; via carbonyl oxygenCombined sources2 Publications1
    Binding sitei433Coenzyme ACombined sources2 Publications1
    Binding sitei441Coenzyme ACombined sources2 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi16 – 17FADCombined sources2 Publications2
    Nucleotide bindingi38 – 39FADCombined sources2 Publications2
    Nucleotide bindingi45 – 47FADCombined sources2 Publications3

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionOxidoreductase
    LigandFAD, Flavoprotein, NAD, NADP

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.8.1.14, 5244

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    O58308

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    NAD(P)H coenzyme A polysulfide/persulfide reductaseCurated (EC:1.8.1.-1 Publication)
    Alternative name(s):
    Coenzyme A disulfide reductase2 Publications (EC:1.8.1.141 Publication)
    Short name:
    CoA-disulfide reductaseCurated
    Short name:
    CoADR1 Publication
    Polysulfide reductase1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Ordered Locus Names:PH0572
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri70601 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000752 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001846991 – 445NAD(P)H coenzyme A polysulfide/persulfide reductaseAdd BLAST445

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer (PubMed:23530771). Homotetramer (PubMed:15720393).

    2 Publications

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    70601.3256978

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1445
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    O58308

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    O58308

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni44 – 48Coenzyme A bindingCombined sources2 Publications5
    Regioni65 – 66Coenzyme A bindingCombined sources1 Publication2

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    When compared to homologous enzymes known to reduce CoA disulfide, this enzyme shows a narrower access channel for CoA substrates, which suggests that this restriction might be responsible for the enzyme's poor activity toward the bulky CoA disulfide substrate (PubMed:23530771). The substrate channel was widened by making four mutations along the channel wall (Y65A, Y66A, P67G, and H367G), leading to a fourfold increase in kcat for the NAD(P)H-dependent reduction of CoA disulfide and enhanced activity toward the substrate at lower temperatures (PubMed:29988575). It suggests that substrate channel morphology is an important determinant of substrate specificity for this family of pyridine nucleotide disulfide oxidoreductase (PNDOR) enzymes (PubMed:29988575).2 Publications

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    arCOG01069, Archaea

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    WVSHAPC

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.50.50.60, 3 hits

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR017758, CoA_disulphide_reductase
    IPR036188, FAD/NAD-bd_sf
    IPR023753, FAD/NAD-binding_dom
    IPR016156, FAD/NAD-linked_Rdtase_dimer_sf
    IPR004099, Pyr_nucl-diS_OxRdtase_dimer

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF07992, Pyr_redox_2, 1 hit
    PF02852, Pyr_redox_dim, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51905, SSF51905, 1 hit
    SSF55424, SSF55424, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR03385, CoA_CoA_reduc, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    O58308-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MGENMKKKVV IIGGGAAGMS AASRVKRLKP EWDVKVFEAT EWVSHAPCGI
    60 70 80 90 100
    PYVVEGLSTP DKLMYYPPEV FIKKRGIDLH LNAEVIEVDT GYVRVRENGG
    110 120 130 140 150
    EKSYEWDYLV FANGASPQVP AIEGVNLKGV FTADLPPDAL AIREYMEKYK
    160 170 180 190 200
    VENVVIIGGG YIGIEMAEAF AAQGKNVTMI VRGERVLRRS FDKEVTDILE
    210 220 230 240 250
    EKLKKHVNLR LQEITMKIEG EERVEKVVTD AGEYKAELVI LATGIKPNIE
    260 270 280 290 300
    LAKQLGVRIG ETGAIWTNEK MQTSVENVYA AGDVAETRHV ITGRRVWVPL
    310 320 330 340 350
    APAGNKMGYV AGSNIAGKEL HFPGVLGTAV TKFMDVEIGK TGLTEMEALK
    360 370 380 390 400
    EGYDVRTAFI KASTRPHYYP GGREIWLKGV VDNETNRLLG VQVVGSDILP
    410 420 430 440
    RIDTAAAMLM AGFTTKDAFF TDLAYAPPFA PVWDPLIVLA RVLKF
    Length:445
    Mass (Da):48,977
    Last modified:August 1, 1998 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i896A034000A0B233
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    BA000001 Genomic DNA Translation: BAA29661.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    H71171

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    BAA29661; BAA29661; BAA29661

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    pho:PH0572

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000001 Genomic DNA Translation: BAA29661.1
    PIRiH71171

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3KD9X-ray2.75A/B/C7-444[»]
    4FX9X-ray2.70A/B1-445[»]
    5L1NX-ray3.60A/B1-445[»]
    SMRiO58308
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi70601.3256978

    Genome annotation databases

    EnsemblBacteriaiBAA29661; BAA29661; BAA29661
    KEGGipho:PH0572

    Phylogenomic databases

    eggNOGiarCOG01069, Archaea
    OMAiWVSHAPC

    Enzyme and pathway databases

    BRENDAi1.8.1.14, 5244
    SABIO-RKiO58308

    Miscellaneous databases

    EvolutionaryTraceiO58308

    Family and domain databases

    Gene3Di3.50.50.60, 3 hits
    InterProiView protein in InterPro
    IPR017758, CoA_disulphide_reductase
    IPR036188, FAD/NAD-bd_sf
    IPR023753, FAD/NAD-binding_dom
    IPR016156, FAD/NAD-linked_Rdtase_dimer_sf
    IPR004099, Pyr_nucl-diS_OxRdtase_dimer
    PfamiView protein in Pfam
    PF07992, Pyr_redox_2, 1 hit
    PF02852, Pyr_redox_dim, 1 hit
    SUPFAMiSSF51905, SSF51905, 1 hit
    SSF55424, SSF55424, 1 hit
    TIGRFAMsiTIGR03385, CoA_CoA_reduc, 1 hit

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNCPPR_PYRHO
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O58308
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 27, 2005
    Last sequence update: August 1, 1998
    Last modified: June 2, 2021
    This is version 131 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
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