{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,27]],"date-time":"2026-01-27T14:44:51Z","timestamp":1769525091748,"version":"3.49.0"},"publisher-location":"New York, NY","reference-count":15,"publisher":"Springer US","isbn-type":[{"value":"9781493998838","type":"print"},{"value":"9781493998845","type":"electronic"}],"license":[{"start":{"date-parts":[[2019,11,10]],"date-time":"2019-11-10T00:00:00Z","timestamp":1573344000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2020]]},"DOI":"10.1007\/978-1-4939-9884-5_13","type":"book-chapter","created":{"date-parts":[[2019,11,9]],"date-time":"2019-11-09T11:02:42Z","timestamp":1573297362000},"page":"193-208","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Immunohistochemistry (IHC): Chromogenic Detection of 3-Phosphohistidine Proteins in Formaldehyde-Fixed, Frozen Mouse Liver Tissue Sections"],"prefix":"10.1007","author":[{"given":"Natalie","family":"Luhtala","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tony","family":"Hunter","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2019,11,10]]},"reference":[{"issue":"1","key":"13_CR1","doi-asserted-by":"publisher","first-page":"198","DOI":"10.1016\/j.cell.2015.05.046","volume":"162","author":"SR Fuhs","year":"2015","unstructured":"Fuhs SR, Meisenhelder J, Aslanian A, Ma L, Zagorska A, Stankova M, Binnie A, Al-Obeidi F, Mauger J, Lemke G, Yates JR 3rd, Hunter T (2015) Monoclonal 1- and 3-phosphohistidine antibodies: new tools to study histidine phosphorylation. Cell 162(1):198\u2013210. \nhttps:\/\/doi.org\/10.1016\/j.cell.2015.05.046","journal-title":"Cell"},{"issue":"2","key":"13_CR2","doi-asserted-by":"publisher","first-page":"187","DOI":"10.1021\/ol503320p","volume":"17","author":"JM Kee","year":"2015","unstructured":"Kee JM, Oslund RC, Couvillon AD, Muir TW (2015) A second-generation phosphohistidine analog for production of phosphohistidine antibodies. Org Lett 17(2):187\u2013189. \nhttps:\/\/doi.org\/10.1021\/ol503320p","journal-title":"Org Lett"},{"issue":"7","key":"13_CR3","doi-asserted-by":"publisher","first-page":"416","DOI":"10.1038\/nchembio.1259","volume":"9","author":"JM Kee","year":"2013","unstructured":"Kee JM, Oslund RC, Perlman DH, Muir TW (2013) A pan-specific antibody for direct detection of protein histidine phosphorylation. Nat Chem Biol 9(7):416\u2013421. \nhttps:\/\/doi.org\/10.1038\/nchembio.1259","journal-title":"Nat Chem Biol"},{"issue":"41","key":"13_CR4","doi-asserted-by":"publisher","first-page":"14327","DOI":"10.1021\/ja104393t","volume":"132","author":"JM Kee","year":"2010","unstructured":"Kee JM, Villani B, Carpenter LR, Muir TW (2010) Development of stable phosphohistidine analogues. J Am Chem Soc 132(41):14327\u201314329. \nhttps:\/\/doi.org\/10.1021\/ja104393t","journal-title":"J Am Chem Soc"},{"issue":"7698","key":"13_CR5","doi-asserted-by":"publisher","first-page":"678","DOI":"10.1038\/nature26140","volume":"555","author":"SK Hindupur","year":"2018","unstructured":"Hindupur SK, Colombi M, Fuhs SR, Matter MS, Guri Y, Adam K, Cornu M, Piscuoglio S, Ng CKY, Betz C, Liko D, Quagliata L, Moes S, Jenoe P, Terracciano LM, Heim MH, Hunter T, Hall MN (2018) The protein histidine phosphatase LHPP is a tumour suppressor. Nature 555(7698):678\u2013682. \nhttps:\/\/doi.org\/10.1038\/nature26140","journal-title":"Nature"},{"issue":"8","key":"13_CR6","doi-asserted-by":"publisher","first-page":"1244","DOI":"10.1091\/mbc.E13-04-0180","volume":"25","author":"X Cai","year":"2014","unstructured":"Cai X, Srivastava S, Surindran S, Li Z, Skolnik EY (2014) Regulation of the epithelial Ca(2)(+) channel TRPV5 by reversible histidine phosphorylation mediated by NDPK-B and PHPT1. Mol Biol Cell 25(8):1244\u20131250. \nhttps:\/\/doi.org\/10.1091\/mbc.E13-04-0180","journal-title":"Mol Biol Cell"},{"issue":"12","key":"13_CR7","doi-asserted-by":"publisher","first-page":"10185","DOI":"10.18632\/oncotarget.23796","volume":"9","author":"I Khan","year":"2018","unstructured":"Khan I, Steeg PS (2018) The relationship of NM23 (NME) metastasis suppressor histidine phosphorylation to its nucleoside diphosphate kinase, histidine protein kinase and motility suppression activities. Oncotarget 9(12):10185\u201310202. \nhttps:\/\/doi.org\/10.18632\/oncotarget.23796","journal-title":"Oncotarget"},{"issue":"3","key":"13_CR8","doi-asserted-by":"publisher","first-page":"457","DOI":"10.1016\/j.molcel.2016.06.021","volume":"63","author":"S Panda","year":"2016","unstructured":"Panda S, Srivastava S, Li Z, Vaeth M, Fuhs SR, Hunter T, Skolnik EY (2016) Identification of PGAM5 as a mammalian protein histidine phosphatase that plays a central role to negatively regulate CD4(+) T cells. Mol Cell 63(3):457\u2013469. \nhttps:\/\/doi.org\/10.1016\/j.molcel.2016.06.021","journal-title":"Mol Cell"},{"issue":"5","key":"13_CR9","doi-asserted-by":"publisher","first-page":"849","DOI":"10.2337\/db17-1433","volume":"67","author":"S Srivastava","year":"2018","unstructured":"Srivastava S, Li Z, Soomro I, Sun Y, Wang J, Bao L, Coetzee WA, Stanley CA, Li C, Skolnik EY (2018) Regulation of KATP channel trafficking in pancreatic beta-cells by protein histidine phosphorylation. Diabetes 67(5):849\u2013860. \nhttps:\/\/doi.org\/10.2337\/db17-1433","journal-title":"Diabetes"},{"key":"13_CR10","doi-asserted-by":"publisher","unstructured":"Srivastava S, Panda S, Li Z, Fuhs SR, Hunter T, Thiele DJ, Hubbard SR, Skolnik EY (2016) Histidine phosphorylation relieves copper inhibition in the mammalian potassium channel KCa3.1. eLife 5. \nhttps:\/\/doi.org\/10.7554\/eLife.16093","DOI":"10.7554\/eLife.16093"},{"issue":"38","key":"13_CR11","doi-asserted-by":"publisher","first-page":"14442","DOI":"10.1073\/pnas.0803678105","volume":"105","author":"S Srivastava","year":"2008","unstructured":"Srivastava S, Zhdanova O, Di L, Li Z, Albaqumi M, Wulff H, Skolnik EY (2008) Protein histidine phosphatase 1 negatively regulates CD4 T cells by inhibiting the K+ channel KCa3.1. Proc Natl Acad Sci U S A 105(38):14442\u201314446. \nhttps:\/\/doi.org\/10.1073\/pnas.0803678105","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"1","key":"13_CR12","doi-asserted-by":"publisher","first-page":"51","DOI":"10.1016\/0014-5793(95)00353-B","volume":"364","author":"HR Matthews","year":"1995","unstructured":"Matthews HR, MacKintosh C (1995) Protein histidine phosphatase activity in rat liver and spinach leaves. FEBS Lett 364(1):51\u201354","journal-title":"FEBS Lett"},{"issue":"6","key":"13_CR13","doi-asserted-by":"publisher","first-page":"433","DOI":"10.1042\/BSR20090167","volume":"30","author":"K Kowalewska","year":"2010","unstructured":"Kowalewska K, Stefanowicz P, Ruman T, Fraczyk T, Rode W, Szewczuk Z (2010) Electron capture dissociation mass spectrometric analysis of lysine-phosphorylated peptides. Biosci Rep 30(6):433\u2013443. \nhttps:\/\/doi.org\/10.1042\/BSR20090167","journal-title":"Biosci Rep"},{"issue":"1","key":"13_CR14","doi-asserted-by":"publisher","first-page":"20","DOI":"10.3109\/03009734.2014.996720","volume":"120","author":"P Ek","year":"2015","unstructured":"Ek P, Ek B, Zetterqvist O (2015) Phosphohistidine phosphatase 1 (PHPT1) also dephosphorylates phospholysine of chemically phosphorylated histone H1 and polylysine. Ups J Med Sci 120(1):20\u201327. \nhttps:\/\/doi.org\/10.3109\/03009734.2014.996720","journal-title":"Ups J Med Sci"},{"key":"13_CR15","doi-asserted-by":"publisher","first-page":"388","DOI":"10.1016\/0076-6879(91)00156-Q","volume":"200","author":"YF Wei","year":"1991","unstructured":"Wei YF, Matthews HR (1991) Identification of phosphohistidine in proteins and purification of protein-histidine kinases. Methods Enzymol 200:388\u2013414","journal-title":"Methods Enzymol"}],"container-title":["Methods in Molecular Biology","Histidine Phosphorylation"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/978-1-4939-9884-5_13","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2019,11,9]],"date-time":"2019-11-09T11:04:48Z","timestamp":1573297488000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/978-1-4939-9884-5_13"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,11,10]]},"ISBN":["9781493998838","9781493998845"],"references-count":15,"URL":"https:\/\/doi.org\/10.1007\/978-1-4939-9884-5_13","relation":{},"ISSN":["1064-3745","1940-6029"],"issn-type":[{"value":"1064-3745","type":"print"},{"value":"1940-6029","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,11,10]]},"assertion":[{"value":"10 November 2019","order":1,"name":"first_online","label":"First Online","group":{"name":"ChapterHistory","label":"Chapter History"}}]}}