{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2022,4,2]],"date-time":"2022-04-02T21:51:33Z","timestamp":1648936293125},"reference-count":54,"publisher":"American Society of Hematology","issue":"13","content-domain":{"domain":["ashpublications.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2001,12,15]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Fanconi anemia (FA) is an autosomal recessive disease with congenital anomalies, bone marrow failure, and susceptibility to leukemia. Patient cells show chromosome instability and hypersensitivity to DNA cross-linking agents. At least 8 complementation groups (A-G) have been identified and 6 FAgenes (for subtypes A, C, D2, E, F, and G) have been cloned. Increasing evidence indicates that a protein complex assembly of multiple FA proteins, including FANCA and FANCG, plays a crucial role in the FA pathway. Previously, it was reported that FANCA was phosphorylated in lymphoblasts from normal controls, whereas the phosphorylation was defective in those derived from patients with FA of multiple complementation groups. The present study examined phosphorylation of FANCA ectopically expressed in FANCA\u2212 cells. Several patient-derived mutations abrogated in vivo phosphorylation of FANCA in this system, suggesting that FANCA phosphorylation is associated with its function. In vitro phosphorylation studies indicated that a physiologic protein kinase for FANCA (FANCA-PK) forms a complex with the substrate. Furthermore, at least a part of FANCA-PK as well as phosphorylated FANCA were included in the FANCA\/FANCG complex. Thus, FANCA-PK appears to be another component of the FA protein complex and may regulate function of FANCA. FANCA-PK was characterized as a cytoplasmic serine kinase sensitive to wortmannin. Identification of the protein kinase is expected to elucidate regulatory mechanisms that control the FA pathway.<\/jats:p>","DOI":"10.1182\/blood.v98.13.3650","type":"journal-article","created":{"date-parts":[[2002,10,28]],"date-time":"2002-10-28T20:44:12Z","timestamp":1035837852000},"page":"3650-3657","update-policy":"http:\/\/dx.doi.org\/10.1182\/blood.2019cm0000","source":"Crossref","is-referenced-by-count":14,"title":["A cytoplasmic serine protein kinase binds and may regulate the Fanconi anemia protein FANCA"],"prefix":"10.1182","volume":"98","author":[{"given":"Hiroshi","family":"Yagasaki","sequence":"first","affiliation":[{"name":"From the Division of Genetic Diagnosis, Institute of Medical Science; and the Department of Molecular Therapy, Advanced Clinical Research Center, Institute of Medical Science, University of Tokyo, Japan; and the Department of Pediatric Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Daiki","family":"Adachi","sequence":"additional","affiliation":[{"name":"From the Division of Genetic Diagnosis, Institute of Medical Science; and the Department of Molecular Therapy, Advanced Clinical Research Center, Institute of Medical Science, University of Tokyo, Japan; and the Department of Pediatric Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tsukasa","family":"Oda","sequence":"additional","affiliation":[{"name":"From the Division of Genetic Diagnosis, Institute of Medical Science; and the Department of Molecular Therapy, Advanced Clinical Research Center, Institute of Medical Science, University of Tokyo, Japan; and the Department of Pediatric Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Irene","family":"Garcia-Higuera","sequence":"additional","affiliation":[{"name":"From the Division of Genetic Diagnosis, Institute of Medical Science; and the Department of Molecular Therapy, Advanced Clinical Research Center, Institute of Medical Science, University of Tokyo, Japan; and the Department of Pediatric Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nii","family":"Tetteh","sequence":"additional","affiliation":[{"name":"From the Division of Genetic Diagnosis, Institute of Medical Science; and the Department of Molecular Therapy, Advanced Clinical Research Center, Institute of Medical Science, University of Tokyo, Japan; and the Department of Pediatric Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alan D.","family":"D'Andrea","sequence":"additional","affiliation":[{"name":"From the Division of Genetic Diagnosis, Institute of Medical Science; and the Department of Molecular Therapy, Advanced Clinical Research Center, Institute of Medical Science, University of Tokyo, Japan; and the Department of Pediatric Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Makoto","family":"Futaki","sequence":"additional","affiliation":[{"name":"From the Division of Genetic Diagnosis, Institute of Medical Science; and the Department of Molecular Therapy, Advanced Clinical Research Center, Institute of Medical Science, University of Tokyo, Japan; and the Department of Pediatric Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shigetaka","family":"Asano","sequence":"additional","affiliation":[{"name":"From the Division of Genetic Diagnosis, Institute of Medical Science; and the Department of Molecular Therapy, Advanced Clinical Research Center, Institute of Medical Science, University of Tokyo, Japan; and the Department of Pediatric Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Takayuki","family":"Yamashita","sequence":"additional","affiliation":[{"name":"From the Division of Genetic Diagnosis, Institute of Medical Science; and the Department of Molecular Therapy, Advanced Clinical Research Center, Institute of Medical Science, University of Tokyo, Japan; and the Department of Pediatric Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"234","reference":[{"key":"2020021218060797700_B1","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/S0921-8777(98)00024-X","article-title":"Is Fanconi anemia caused by a defect in the processing of DNA damage?","volume":"408","author":"Buchwald","year":"1998","journal-title":"Mutat Res."},{"key":"2020021218060797700_B2","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1097\/00062752-199903000-00005","article-title":"The molecular and cellular biology of Fanconi anemia.","volume":"6","author":"Garcia-Higuera","year":"1999","journal-title":"Curr Opin Hematol."},{"key":"2020021218060797700_B3","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1038\/ng0692-196","article-title":"Evidence for at least four Fanconi anaemia genes including FACC on chromosome 9.","volume":"1","author":"Strathdee","year":"1992","journal-title":"Nat Genet."},{"key":"2020021218060797700_B4","doi-asserted-by":"crossref","first-page":"2156","DOI":"10.1182\/blood.V86.6.2156.bloodjournal8662156","article-title":"Classification of Fanconi anemia patients by complementation analysis: evidence for a fifth genetic subtype.","volume":"86","author":"Joenje","year":"1995","journal-title":"Blood."},{"key":"2020021218060797700_B5","doi-asserted-by":"crossref","first-page":"940","DOI":"10.1086\/514881","article-title":"Evidence for at least eight Fanconi anemia genes.","volume":"61","author":"Joenje","year":"1997","journal-title":"Am J Hum Genet."},{"key":"2020021218060797700_B6","doi-asserted-by":"crossref","first-page":"759","DOI":"10.1086\/303067","article-title":"Complementation analysis in Fanconi anemia: assignment of the reference FA-H patient to group A.","volume":"67","author":"Joenje","year":"2000","journal-title":"Am J Hum Genet."},{"key":"2020021218060797700_B7","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/S1097-2765(01)00172-1","article-title":"Positional cloning of a novel Fanconi anemia gene, FANCD2.","volume":"7","author":"Timmers","year":"2001","journal-title":"Mol Cell."},{"key":"2020021218060797700_B8","doi-asserted-by":"crossref","first-page":"763","DOI":"10.1038\/356763a0","article-title":"Cloning of cDNAs for Fanconi's anaemia by functional complementation.","volume":"356","author":"Strathdee","year":"1992","journal-title":"Nature."},{"key":"2020021218060797700_B9","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1038\/ng1196-320","article-title":"Expression cloning of a cDNA for the major Fanconi anaemia gene, FAA.","volume":"14","author":"Lo Ten Foe","year":"1996","journal-title":"Nat Genet."},{"key":"2020021218060797700_B10","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1038\/ng1196-324","article-title":"Positional cloning of the Fanconi anaemia group A gene. the Fanconi anaemia\/breast cancer consortium.","volume":"14","year":"1996","journal-title":"Nat Genet."},{"key":"2020021218060797700_B11","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1038\/3093","article-title":"The Fanconi anaemia group G gene FANCG is identical with XRCC9.","volume":"20","author":"de Winter","year":"1998","journal-title":"Nat Genet."},{"key":"2020021218060797700_B12","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1038\/71626","article-title":"The Fanconi anaemia gene FANCF encodes a novel protein with homology to ROM.","volume":"24","author":"de Winter","year":"2000","journal-title":"Nat Genet."},{"key":"2020021218060797700_B13","doi-asserted-by":"crossref","first-page":"1306","DOI":"10.1016\/S0002-9297(07)62959-0","article-title":"Isolation of a cDNA representing the Fanconi anemia complementation group E gene.","volume":"67","author":"de Winter","year":"2000","journal-title":"Am J Hum Genet."},{"key":"2020021218060797700_B14","doi-asserted-by":"crossref","first-page":"6712","DOI":"10.1073\/pnas.91.14.6712","article-title":"The Fanconi anemia polypeptide FACC is localized to the cytoplasm.","volume":"91","author":"Yamashita","year":"1994","journal-title":"Proc Natl Acad Sci U S A."},{"key":"2020021218060797700_B15","doi-asserted-by":"crossref","first-page":"7975","DOI":"10.1073\/pnas.91.17.7975","article-title":"Localization of Fanconi anemia C protein to the cytoplasm of mammalian cells.","volume":"91","author":"Youssoufian","year":"1994","journal-title":"Proc Natl Acad Sci U S A."},{"key":"2020021218060797700_B16","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1038\/ng1297-487","article-title":"The Fanconi anaemia proteins, FAA and FAC, interact to form a nuclear complex.","volume":"17","author":"Kupfer","year":"1997","journal-title":"Nat Genet."},{"key":"2020021218060797700_B17","doi-asserted-by":"crossref","first-page":"1418","DOI":"10.1182\/blood.V91.4.1418","article-title":"The Fanconi anemia group C gene product is located in both the nucleus and cytoplasm of human cells.","volume":"91","author":"Hoatlin","year":"1998","journal-title":"Blood."},{"key":"2020021218060797700_B18","doi-asserted-by":"crossref","first-page":"13085","DOI":"10.1073\/pnas.95.22.13085","article-title":"The Fanconi anemia pathway requires FAA phosphorylation and FAA\/FAC nuclear accumulation.","volume":"95","author":"Yamashita","year":"1998","journal-title":"Proc Natl Acad Sci U S A."},{"key":"2020021218060797700_B19","doi-asserted-by":"crossref","first-page":"1007","DOI":"10.1093\/hmg\/8.6.1007","article-title":"Characterization of regions functional in the nuclear localization of the Fanconi anemia group A protein.","volume":"8","author":"Lightfoot","year":"1999","journal-title":"Hum Mol Genet."},{"key":"2020021218060797700_B20","doi-asserted-by":"crossref","first-page":"9232","DOI":"10.1073\/pnas.94.17.9232","article-title":"The human XRCC9 gene corrects chromosomal instability and mutagen sensitivities in CHO UV40 cells.","volume":"94","author":"Liu","year":"1997","journal-title":"Proc Natl Acad Sci U S A."},{"key":"2020021218060797700_B21","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/S1097-2765(01)00173-3","article-title":"Interaction of the Fanconi anemia proteins and BRCA1 in a common pathway.","volume":"7","author":"Garcia-Higuera","year":"2001","journal-title":"Mol Cell."},{"key":"2020021218060797700_B22","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1016\/S0301-472X(99)00022-3","article-title":"A patient-derived mutant form of the Fanconi anemia protein, FANCA, is defective in nuclear accumulation.","volume":"27","author":"Kupfer","year":"1999","journal-title":"Exp Hematol."},{"key":"2020021218060797700_B23","doi-asserted-by":"crossref","first-page":"3224","DOI":"10.1182\/blood.V96.9.3224","article-title":"The Fanconi anemia proteins, FANCA and FANCG, stabilize each other and promote the nuclear accumulation of the FA complex.","volume":"96","author":"Garcia-Higuera","year":"2000","journal-title":"Blood."},{"key":"2020021218060797700_B24","doi-asserted-by":"crossref","first-page":"5952","DOI":"10.1128\/MCB.18.10.5952","article-title":"Functional activity of the Fanconi anemia protein FAA requires FAC binding and nuclear localization.","volume":"18","author":"Naf","year":"1998","journal-title":"Mol Cell Biol."},{"key":"2020021218060797700_B25","doi-asserted-by":"crossref","first-page":"4866","DOI":"10.1128\/MCB.19.7.4866","article-title":"Fanconi anemia proteins FANCA, FANCC, and FANCG\/XRCC9 interact in a functional nuclear complex.","volume":"19","author":"Garcia-Higuera","year":"1999","journal-title":"Mol Cell Biol."},{"key":"2020021218060797700_B26","doi-asserted-by":"crossref","first-page":"10320","DOI":"10.1073\/pnas.96.18.10320","article-title":"A physical complex of the Fanconi anemia proteins FANCG\/XRCC9 and FANCA.","volume":"96","author":"Waisfisz","year":"1999","journal-title":"Proc Natl Acad Sci U S A."},{"key":"2020021218060797700_B27","doi-asserted-by":"crossref","first-page":"32904","DOI":"10.1074\/jbc.274.46.32904","article-title":"Human alpha spectrin II and the Fanconi anemia proteins FANCA and FANCC interact to form a nuclear complex.","volume":"274","author":"McMahon","year":"1999","journal-title":"J Biol Chem."},{"key":"2020021218060797700_B28","doi-asserted-by":"crossref","first-page":"34212","DOI":"10.1074\/jbc.274.48.34212","article-title":"Resistance to mitomycin C requires direct interaction between the Fanconi anemia proteins FANCA and FANCG in the nucleus through an arginine-rich domain.","volume":"274","author":"Kruyt","year":"1999","journal-title":"J Biol Chem."},{"key":"2020021218060797700_B29","doi-asserted-by":"crossref","first-page":"2665","DOI":"10.1093\/hmg\/9.18.2665","article-title":"The Fanconi anemia protein FANCF forms a nuclear complex with FANCA, FANCC and FANCG.","volume":"9","author":"de Winter","year":"2000","journal-title":"Hum Mol Genet."},{"key":"2020021218060797700_B30","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.1182\/blood.V90.3.1047","article-title":"The Fanconi anemia polypeptide, FAC, binds to the cyclin-dependent kinase, cdc2.","volume":"90","author":"Kupfer","year":"1997","journal-title":"Blood."},{"key":"2020021218060797700_B31","doi-asserted-by":"crossref","first-page":"4379","DOI":"10.1182\/blood.V91.11.4379","article-title":"Molecular chaperone GRP94 binds to the Fanconi anemia group C protein and regulates its intracellular expression.","volume":"91","author":"Hoshino","year":"1998","journal-title":"Blood."},{"key":"2020021218060797700_B32","doi-asserted-by":"crossref","first-page":"3050","DOI":"10.1182\/blood.V92.9.3050","article-title":"Abnormal microsomal detoxification implicated in Fanconi anemia group C by interaction of the FAC protein with NADPH cytochrome P450 reductase.","volume":"92","author":"Kruyt","year":"1998","journal-title":"Blood."},{"key":"2020021218060797700_B33","doi-asserted-by":"crossref","first-page":"630","DOI":"10.1006\/bbrc.1999.1731","article-title":"SNX5, a new member of the sorting nexin family, binds to the Fanconi anemia complementation group A protein.","volume":"265","author":"Otsuki","year":"1999","journal-title":"Biochem Biophys Res Commun."},{"key":"2020021218060797700_B34","doi-asserted-by":"crossref","first-page":"4724","DOI":"10.1128\/MCB.20.13.4724-4735.2000","article-title":"The Fanconi anemia protein FANCC binds to and facilitates the activation of STAT1 by gamma interferon and hematopoietic growth factors.","volume":"20","author":"Pang","year":"2000","journal-title":"Mol Cell Biol."},{"key":"2020021218060797700_B35","doi-asserted-by":"crossref","first-page":"20090","DOI":"10.1074\/jbc.M002193200","article-title":"Regulatory mechanism of Ca2+\/calmodulin-dependent protein kinase kinase.","volume":"275","author":"Tokumitsu","year":"2000","journal-title":"J Biol Chem."},{"key":"2020021218060797700_B36","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/S0092-8674(00)80406-7","article-title":"The I\u03baB kinase complex (IKK) contains two kinase subunits, IKK\u03b1 and IKK\u03b2, necessary for I\u03baB phosphorylation and NF-\u03baB activation.","volume":"91","author":"Zandi","year":"1997","journal-title":"Cell."},{"key":"2020021218060797700_B37","doi-asserted-by":"crossref","first-page":"1407","DOI":"10.1128\/MCB.20.4.1407-1418.2000","article-title":"A novel TATA-binding protein-binding protein, ABT1, activates basal transcription and has a yeast homolog that is essential for growth.","volume":"20","author":"Oda","year":"2000","journal-title":"Mol Cell Biol."},{"key":"2020021218060797700_B38","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1016\/0076-6879(83)99075-4","article-title":"Detection and quantification of phosphotyrosine proteins.","volume":"99","author":"Cooper","year":"1983","journal-title":"Methods in Enzymology."},{"key":"2020021218060797700_B39","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1016\/S0076-6879(83)96020-2","article-title":"Peptide mapping in one dimension by limited proteolysis of sodium dodecyl sulfate-solubilized proteins.","volume":"96","author":"Cleveland","year":"1983","journal-title":"Methods in Enzymology."},{"key":"2020021218060797700_B40","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1016\/0003-2697(87)90587-2","article-title":"Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa.","volume":"166","author":"Schagger","year":"1987","journal-title":"Anal Biochem."},{"key":"2020021218060797700_B41","doi-asserted-by":"crossref","first-page":"13051","DOI":"10.1073\/pnas.94.24.13051","article-title":"Sequence variation in the Fanconi anemia gene FAA.","volume":"94","author":"Levran","year":"1997","journal-title":"Proc Natl Acad Sci U S A."},{"key":"2020021218060797700_B42","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1146\/annurev.biochem.67.1.481","article-title":"Phosphoinositide kinases.","volume":"67","author":"Fruman","year":"1998","journal-title":"Annu Rev Biochem."},{"key":"2020021218060797700_B43","first-page":"692a","article-title":"The Fanconi anemia group A gene product is a component of the I\u03baB kinase signalsome complex involved in NF-\u03baB activation [abstract].","volume":"92(suppl 1)","author":"Otsuki","year":"1998","journal-title":"Blood."},{"key":"2020021218060797700_B44","doi-asserted-by":"crossref","first-page":"27339","DOI":"10.1074\/jbc.274.39.27339","article-title":"The beginning of the end: I\u03baB kinase (IKK) and NF-\u03baB activation.","volume":"274","author":"Karin","year":"1999","journal-title":"J Biol Chem."},{"key":"2020021218060797700_B45","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1038\/23948","article-title":"The anti-inflammatory agents aspirin and salicylate inhibit the activity of I\u03baB kinase-\u03b2.","volume":"396","author":"Yin","year":"1998","journal-title":"Nature."},{"key":"2020021218060797700_B46","doi-asserted-by":"crossref","first-page":"R329","DOI":"10.1016\/S0960-9822(99)80205-X","article-title":"Protein modification: docking sites for kinases.","volume":"9","author":"Holland","year":"1999","journal-title":"Curr Biol."},{"key":"2020021218060797700_B47","doi-asserted-by":"crossref","first-page":"448","DOI":"10.1016\/S0968-0004(00)01627-3","article-title":"Docking domains and substrate-specificity determination for MAP kinases.","volume":"25","author":"Sharrocks","year":"2000","journal-title":"Trends Biochem Sci."},{"key":"2020021218060797700_B48","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1101\/gad.13.2.163","article-title":"Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase.","volume":"13","author":"Jacobs","year":"1999","journal-title":"Genes Dev."},{"key":"2020021218060797700_B49","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/S0955-0674(99)00078-2","article-title":"Signal transduction: hanging on a scaffold.","volume":"12","author":"Burack","year":"2000","journal-title":"Curr Opin Cell Biol."},{"key":"2020021218060797700_B50","first-page":"4375","article-title":"Inhibition of phosphoinositide 3-kinase related kinases by the radiosensitizing agent wortmannin.","volume":"58","author":"Sarkaria","year":"1998","journal-title":"Cancer Res."},{"key":"2020021218060797700_B51","doi-asserted-by":"crossref","first-page":"5256","DOI":"10.1002\/j.1460-2075.1996.tb00911.x","article-title":"Direct inhibition of the signaling functions of the mammalian target of rapamycin by the phosphoinositide 3-kinase inhibitors, wortmannin and LY294002.","volume":"15","author":"Brunn","year":"1996","journal-title":"EMBO J."},{"key":"2020021218060797700_B52","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1002\/j.1460-2075.1994.tb06290.x","article-title":"PI 3-kinase is a dual specificity enzyme: autoregulation by an intrinsic protein-serine kinase activity.","volume":"13","author":"Dhand","year":"1994","journal-title":"EMBO J."},{"key":"2020021218060797700_B53","doi-asserted-by":"crossref","first-page":"1292","DOI":"10.1093\/emboj\/18.5.1292","article-title":"Autophosphorylation of p110 phosphoinositide 3-kinase: a new paradigm for the regulation of lipid kinases in vitro and in vivo.","volume":"18","author":"Vanhaesebroeck","year":"1999","journal-title":"EMBO J."},{"key":"2020021218060797700_B54","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1038\/377441a0","article-title":"Control of p70 S6 kinase by kinase activity of FRAP in vivo.","volume":"377","author":"Brown","year":"1995","journal-title":"Nature."}],"container-title":["Blood"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/ashpublications.org\/blood\/article-pdf\/98\/13\/3650\/1679380\/h8240103650.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"http:\/\/ashpublications.org\/blood\/article-pdf\/98\/13\/3650\/1679380\/h8240103650.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,2,13]],"date-time":"2020-02-13T00:07:56Z","timestamp":1581552476000},"score":1,"resource":{"primary":{"URL":"https:\/\/ashpublications.org\/blood\/article\/98\/13\/3650\/90249\/A-cytoplasmic-serine-protein-kinase-binds-and-may"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2001,12,15]]},"references-count":54,"journal-issue":{"issue":"13","published-print":{"date-parts":[[2001,12,15]]}},"URL":"https:\/\/doi.org\/10.1182\/blood.v98.13.3650","relation":{},"ISSN":["1528-0020","0006-4971"],"issn-type":[{"value":"1528-0020","type":"electronic"},{"value":"0006-4971","type":"print"}],"subject":[],"published":{"date-parts":[[2001,12,15]]}}}