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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Escherichia coli (strain K12)
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

Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.UniRule annotation3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activity is optimum in the presence of Mg2+ and K+.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

  1. KM=13.5 µM for 10-formyltetrahydrofolate1 Publication
  2. KM=0.35 µM for L-methionyl-tRNA(fMet)1 Publication

    <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

    • methionyl-tRNA formyltransferase activity Source: EcoCyc

    GO - Biological processi

    • charged-tRNA amino acid modification Source: EcoCyc
    • conversion of methionyl-tRNA to N-formyl-methionyl-tRNA Source: GO_Central

    <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 functionTransferase
    Biological processProtein biosynthesis

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:EG11268-MONOMER
    MetaCyc:EG11268-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.1.2.9 2026

    <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_and_taxonomy_section">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:
    Methionyl-tRNA formyltransferaseUniRule annotationCurated (EC:2.1.2.9UniRule annotation2 Publications)
    Alternative name(s):
    Met-tRNA(fMet) formyltransferase1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
    Name:fmt1 PublicationUniRule annotation
    Synonyms:yhdD
    Ordered Locus Names:b3288, JW3249
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiEscherichia coli (strain K12)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri83333 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
    • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    Escherichia coli strain K12 genome database

    More...
    EcoGenei
    EG11268 fmt

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB04464 N-Formylmethionine

    <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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000829592 – 315Methionyl-tRNA formyltransferaseAdd BLAST314

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P23882

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P23882

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P23882

    2D gel databases

    Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

    More...
    SWISS-2DPAGEi
    P23882

    <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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4263429, 45 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-9668N

    Protein interaction database and analysis system

    More...
    IntActi
    P23882, 12 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    316385.ECDH10B_3462

    <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

    1315
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P23882

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

    More...
    SMRi
    P23882

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P23882

    <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>Regioni2 – 189N-terminal domain2 PublicationsAdd BLAST188
    Regioni113 – 116Tetrahydrofolate (THF) bindingUniRule annotation4
    Regioni210 – 315C-terminal domain2 PublicationsAdd BLAST106

    <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

    Composed of an N- and a C-terminal domain. The N-terminal domain carries the tetrahydrofolate (THF)-binding site and the C-terminal domain is presumably involved in positioning the Met-tRNA substrate for the formylation reaction.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

    Belongs to the Fmt family.UniRule annotationCurated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105CAE Bacteria
    COG0223 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000261177

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P23882

    KEGG Orthology (KO)

    More...
    KOi
    K00604

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P23882

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.10.25.10, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00182 Formyl_trans, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR005794 Fmt
    IPR005793 Formyl_trans_C
    IPR037022 Formyl_trans_C_sf
    IPR002376 Formyl_transf_N
    IPR036477 Formyl_transf_N_sf
    IPR011034 Formyl_transferase-like_C_sf
    IPR001555 GART_AS

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02911 Formyl_trans_C, 1 hit
    PF00551 Formyl_trans_N, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF50486 SSF50486, 1 hit
    SSF53328 SSF53328, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00460 fmt, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00373 GART, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P23882-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSESLRIIFA GTPDFAARHL DALLSSGHNV VGVFTQPDRP AGRGKKLMPS
    60 70 80 90 100
    PVKVLAEEKG LPVFQPVSLR PQENQQLVAE LQADVMVVVA YGLILPKAVL
    110 120 130 140 150
    EMPRLGCINV HGSLLPRWRG AAPIQRSLWA GDAETGVTIM QMDVGLDTGD
    160 170 180 190 200
    MLYKLSCPIT AEDTSGTLYD KLAELGPQGL ITTLKQLADG TAKPEVQDET
    210 220 230 240 250
    LVTYAEKLSK EEARIDWSLS AAQLERCIRA FNPWPMSWLE IEGQPVKVWK
    260 270 280 290 300
    ASVIDTATNA APGTILEANK QGIQVATGDG ILNLLSLQPA GKKAMSAQDL
    310
    LNSRREWFVP GNRLV
    Length:315
    Mass (Da):34,168
    Last modified:January 23, 2007 - v4
    <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:i1AE14C808F04A126
    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
    X63666 Genomic DNA Translation: CAA45207.1
    X77091 Genomic DNA Translation: CAA54368.1
    U18997 Genomic DNA Translation: AAA58085.1
    U00096 Genomic DNA Translation: AAC76313.1
    AP009048 Genomic DNA Translation: BAE78004.1
    X00767 Genomic DNA Translation: CAA25339.1 Sequence problems.
    Y10307 Genomic DNA Translation: CAA71358.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S23108

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_417746.1, NC_000913.3
    WP_000004473.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC76313; AAC76313; b3288
    BAE78004; BAE78004; BAE78004

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    947779

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW3249
    eco:b3288

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.3444

    <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
    X63666 Genomic DNA Translation: CAA45207.1
    X77091 Genomic DNA Translation: CAA54368.1
    U18997 Genomic DNA Translation: AAA58085.1
    U00096 Genomic DNA Translation: AAC76313.1
    AP009048 Genomic DNA Translation: BAE78004.1
    X00767 Genomic DNA Translation: CAA25339.1 Sequence problems.
    Y10307 Genomic DNA Translation: CAA71358.1
    PIRiS23108
    RefSeqiNP_417746.1, NC_000913.3
    WP_000004473.1, NZ_LN832404.1

    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
    1FMTX-ray2.00A/B2-315[»]
    2FMTX-ray2.80A/B2-315[»]
    ProteinModelPortaliP23882
    SMRiP23882
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4263429, 45 interactors
    DIPiDIP-9668N
    IntActiP23882, 12 interactors
    STRINGi316385.ECDH10B_3462

    Chemistry databases

    DrugBankiDB04464 N-Formylmethionine

    2D gel databases

    SWISS-2DPAGEiP23882

    Proteomic databases

    EPDiP23882
    PaxDbiP23882
    PRIDEiP23882

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76313; AAC76313; b3288
    BAE78004; BAE78004; BAE78004
    GeneIDi947779
    KEGGiecj:JW3249
    eco:b3288
    PATRICifig|1411691.4.peg.3444

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...
    EchoBASEi
    EB1247
    EcoGeneiEG11268 fmt

    Phylogenomic databases

    eggNOGiENOG4105CAE Bacteria
    COG0223 LUCA
    HOGENOMiHOG000261177
    InParanoidiP23882
    KOiK00604
    PhylomeDBiP23882

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11268-MONOMER
    MetaCyc:EG11268-MONOMER
    BRENDAi2.1.2.9 2026

    Miscellaneous databases

    EvolutionaryTraceiP23882

    Protein Ontology

    More...
    PROi
    PR:P23882

    Family and domain databases

    Gene3Di3.10.25.10, 1 hit
    HAMAPiMF_00182 Formyl_trans, 1 hit
    InterProiView protein in InterPro
    IPR005794 Fmt
    IPR005793 Formyl_trans_C
    IPR037022 Formyl_trans_C_sf
    IPR002376 Formyl_transf_N
    IPR036477 Formyl_transf_N_sf
    IPR011034 Formyl_transferase-like_C_sf
    IPR001555 GART_AS
    PfamiView protein in Pfam
    PF02911 Formyl_trans_C, 1 hit
    PF00551 Formyl_trans_N, 1 hit
    SUPFAMiSSF50486 SSF50486, 1 hit
    SSF53328 SSF53328, 1 hit
    TIGRFAMsiTIGR00460 fmt, 1 hit
    PROSITEiView protein in PROSITE
    PS00373 GART, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    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 nameiFMT_ECOLI
    <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: P23882
    Secondary accession number(s): P77040, Q2M6V2
    <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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: January 23, 2007
    Last modified: December 5, 2018
    This is version 166 of the entry and version 4 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, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
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