{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,23]],"date-time":"2026-06-23T23:52:24Z","timestamp":1782258744749,"version":"3.54.5"},"reference-count":116,"publisher":"Springer Science and Business Media LLC","issue":"5","license":[{"start":{"date-parts":[[2020,11,17]],"date-time":"2020-11-17T00:00:00Z","timestamp":1605571200000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2020,11,17]],"date-time":"2020-11-17T00:00:00Z","timestamp":1605571200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"funder":[{"name":"Italian Ministry of Foreign Affairs and International Cooperation","award":["PGR00963"],"award-info":[{"award-number":["PGR00963"]}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Cell. Mol. Life Sci."],"published-print":{"date-parts":[[2021,3]]},"DOI":"10.1007\/s00018-020-03697-3","type":"journal-article","created":{"date-parts":[[2020,11,17]],"date-time":"2020-11-17T05:34:33Z","timestamp":1605591273000},"page":"2059-2067","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":18,"title":["Intrinsically disordered features of carbonic anhydrase IX proteoglycan-like domain"],"prefix":"10.1007","volume":"78","author":[{"given":"Emma","family":"Langella","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martina","family":"Buonanno","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Giuseppina","family":"De Simone","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9647-7089","authenticated-orcid":false,"given":"Simona Maria","family":"Monti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2020,11,17]]},"reference":[{"key":"3697_CR1","first-page":"437","volume":"1","author":"P Romero","year":"1998","unstructured":"Romero P, Obradovic Z, Kissinger CR et al (1998) Thousands of proteins likely to have long disordered regions. Pac Symp Biocomput 1:437\u2013448","journal-title":"Pac Symp Biocomput"},{"key":"3697_CR2","doi-asserted-by":"publisher","first-page":"S7","DOI":"10.1186\/1471-2164-10-S1-S7","volume":"10","author":"VN Uversky","year":"2009","unstructured":"Uversky VN, Oldfield CJ, Midic U et al (2009) Unfoldomics of human diseases: linking protein intrinsic disorder with diseases. BMC Genomics 10:S7. https:\/\/doi.org\/10.1186\/1471-2164-10-S1-S7","journal-title":"BMC Genomics"},{"key":"3697_CR3","doi-asserted-by":"publisher","first-page":"756","DOI":"10.1016\/j.sbi.2008.10.002","volume":"18","author":"AK Dunker","year":"2008","unstructured":"Dunker AK, Silman I, Uversky VN, Sussman JL (2008) Function and structure of inherently disordered proteins. Curr Opin Struct Biol 18:756\u2013764. https:\/\/doi.org\/10.1016\/j.sbi.2008.10.002","journal-title":"Curr Opin Struct Biol"},{"key":"3697_CR4","doi-asserted-by":"publisher","first-page":"1989","DOI":"10.1021\/bi047993o","volume":"44","author":"CJ Oldfield","year":"2005","unstructured":"Oldfield CJ, Cheng Y, Cortese MS et al (2005) Comparing and combining predictors of mostly disordered proteins \u2020. Biochemistry 44:1989\u20132000. https:\/\/doi.org\/10.1021\/bi047993o","journal-title":"Biochemistry"},{"key":"3697_CR5","doi-asserted-by":"publisher","first-page":"137","DOI":"10.1007\/s00018-014-1661-9","volume":"72","author":"Z Peng","year":"2015","unstructured":"Peng Z, Yan J, Fan X et al (2015) Exceptionally abundant exceptions: comprehensive characterization of intrinsic disorder in all domains of life. Cell Mol Life Sci 72:137\u2013151. https:\/\/doi.org\/10.1007\/s00018-014-1661-9","journal-title":"Cell Mol Life Sci"},{"key":"3697_CR6","doi-asserted-by":"publisher","first-page":"371","DOI":"10.1016\/bs.pmbts.2019.05.006","volume":"166","author":"N Garg","year":"2019","unstructured":"Garg N, Kumar P, Gadhave K, Giri R (2019) The dark proteome of cancer: Intrinsic disorderedness and functionality of HIF-1\u03b1 along with its interacting proteins. Prog Mol Biol Transl Sci 166:371\u2013403. https:\/\/doi.org\/10.1016\/bs.pmbts.2019.05.006","journal-title":"Prog Mol Biol Transl Sci"},{"key":"3697_CR7","doi-asserted-by":"publisher","first-page":"1231","DOI":"10.1016\/j.bbapap.2010.01.017","volume":"1804","author":"VN Uversky","year":"2010","unstructured":"Uversky VN, Dunker AK (2010) Understanding protein non-folding. Biochim Biophys Acta Proteins Proteomics 1804:1231\u20131264. https:\/\/doi.org\/10.1016\/j.bbapap.2010.01.017","journal-title":"Biochim Biophys Acta Proteins Proteomics"},{"key":"3697_CR8","doi-asserted-by":"publisher","first-page":"161","DOI":"10.11234\/gi1990.11.161","volume":"11","author":"AK Dunker","year":"2000","unstructured":"Dunker AK, Obradovic Z, Romero P et al (2000) Intrinsic protein disorder in complete genomes. Genome Inform Ser Workshop Genome Inform 11:161\u2013171. https:\/\/doi.org\/10.11234\/gi1990.11.161","journal-title":"Genome Inform Ser Workshop Genome Inform"},{"key":"3697_CR9","doi-asserted-by":"publisher","first-page":"635","DOI":"10.1016\/j.jmb.2004.02.002","volume":"337","author":"JJ Ward","year":"2004","unstructured":"Ward JJ, Sodhi JS, McGuffin LJ et al (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 337:635\u2013645. https:\/\/doi.org\/10.1016\/j.jmb.2004.02.002","journal-title":"J Mol Biol"},{"key":"3697_CR10","doi-asserted-by":"publisher","first-page":"620","DOI":"10.1002\/pro.3348","volume":"27","author":"M Buonanno","year":"2018","unstructured":"Buonanno M, Coppola M, Di Lelio I et al (2018) Prosystemin, a prohormone that modulates plant defense barriers, is an intrinsically disordered protein. Protein Sci 27:620\u2013632. https:\/\/doi.org\/10.1002\/pro.3348","journal-title":"Protein Sci"},{"key":"3697_CR11","doi-asserted-by":"publisher","first-page":"215","DOI":"10.1146\/annurev.biophys.37.032807.125924","volume":"37","author":"U Vn","year":"2008","unstructured":"Vn U, Cj O, AK D, (2008) Intrinsically disordered proteins in human diseases: introducing the D 2 concept. Annu Rev Biophys 37:215\u2013246","journal-title":"Annu Rev Biophys"},{"key":"3697_CR12","doi-asserted-by":"publisher","first-page":"5129","DOI":"10.1111\/j.1742-4658.2005.04948.x","volume":"272","author":"AK Dunker","year":"2005","unstructured":"Dunker AK, Cortese MS, Romero P et al (2005) Flexible nets. The roles of intrinsic disorder in protein interaction networks. FEBS J 272:5129\u20135148. https:\/\/doi.org\/10.1111\/j.1742-4658.2005.04948.x","journal-title":"FEBS J"},{"key":"3697_CR13","doi-asserted-by":"publisher","first-page":"1899","DOI":"10.1021\/pr060393m","volume":"6","author":"S Vucetic","year":"2007","unstructured":"Vucetic S, Xie H, Iakoucheva LM et al (2007) Functional anthology of intrinsic disorder. 2. cellular components, domains, technical terms, developmental processes, and coding sequence diversities correlated with long disordered regions. J Proteome Res 6:1899\u20131916. https:\/\/doi.org\/10.1021\/pr060393m","journal-title":"J Proteome Res"},{"key":"3697_CR14","doi-asserted-by":"publisher","first-page":"1439","DOI":"10.1529\/biophysj.106.094045","volume":"92","author":"P Radivojac","year":"2007","unstructured":"Radivojac P, Iakoucheva LM, Oldfield CJ et al (2007) Intrinsic disorder and functional proteomics. Biophys J 92:1439\u20131456. https:\/\/doi.org\/10.1529\/biophysj.106.094045","journal-title":"Biophys J"},{"key":"3697_CR15","doi-asserted-by":"publisher","first-page":"197","DOI":"10.1038\/nrm1589","volume":"6","author":"HJ Dyson","year":"2005","unstructured":"Dyson HJ, Wright PE (2005) Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6:197\u2013208. https:\/\/doi.org\/10.1038\/nrm1589","journal-title":"Nat Rev Mol Cell Biol"},{"key":"3697_CR16","doi-asserted-by":"publisher","first-page":"1882","DOI":"10.1021\/pr060392u","volume":"6","author":"H Xie","year":"2007","unstructured":"Xie H, Vucetic S, Iakoucheva LM et al (2007a) Functional anthology of intrinsic disorder. 1. biological processes and functions of proteins with long disordered regions. J Proteome Res 6:1882\u20131898. https:\/\/doi.org\/10.1021\/pr060392u","journal-title":"J Proteome Res"},{"key":"3697_CR17","doi-asserted-by":"publisher","first-page":"1917","DOI":"10.1021\/pr060394e","volume":"6","author":"H Xie","year":"2007","unstructured":"Xie H, Vucetic S, Iakoucheva LM et al (2007b) Functional anthology of intrinsic disorder. 3. ligands, post-translational modifications, and diseases associated with intrinsically disordered proteins. J Proteome Res 6:1917\u20131932. https:\/\/doi.org\/10.1021\/pr060394e","journal-title":"J Proteome Res"},{"key":"3697_CR18","doi-asserted-by":"publisher","first-page":"343","DOI":"10.1002\/jmr.747","volume":"18","author":"VN Uversky","year":"2005","unstructured":"Uversky VN, Oldfield CJ, Dunker AK (2005) Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling. J Mol Recognit 18:343\u2013384. https:\/\/doi.org\/10.1002\/jmr.747","journal-title":"J Mol Recognit"},{"key":"3697_CR19","doi-asserted-by":"publisher","first-page":"8390","DOI":"10.1073\/pnas.0507916103","volume":"103","author":"PR Romero","year":"2006","unstructured":"Romero PR, Zaidi S, Fang YY et al (2006) Alternative splicing in concert with protein intrinsic disorder enables increased functional diversity in multicellular organisms. Proc Natl Acad Sci 103:8390\u20138395. https:\/\/doi.org\/10.1073\/pnas.0507916103","journal-title":"Proc Natl Acad Sci"},{"key":"3697_CR20","doi-asserted-by":"publisher","first-page":"805","DOI":"10.1038\/nbt0901-805","volume":"19","author":"AK Dunker","year":"2001","unstructured":"Dunker AK, Obradovic Z (2001) The protein trinity\u2014linking function and disorder. Nat Biotechnol 19:805\u2013806. https:\/\/doi.org\/10.1038\/nbt0901-805","journal-title":"Nat Biotechnol"},{"key":"3697_CR21","doi-asserted-by":"publisher","first-page":"S1","DOI":"10.1186\/1471-2164-9-S1-S1","volume":"9","author":"CJ Oldfield","year":"2008","unstructured":"Oldfield CJ, Meng J, Yang JY et al (2008) Flexible nets: disorder and induced fit in the associations of p53 and 14\u20133-3 with their partners. BMC Genomics 9:S1. https:\/\/doi.org\/10.1186\/1471-2164-9-S1-S1","journal-title":"BMC Genomics"},{"key":"3697_CR22","doi-asserted-by":"publisher","first-page":"1131","DOI":"10.1016\/j.jmb.2003.08.008","volume":"332","author":"R Dawson","year":"2003","unstructured":"Dawson R, M\u00fcller L, Dehner A et al (2003) The N-terminal domain of p53 is natively unfolded. J Mol Biol 332:1131\u20131141. https:\/\/doi.org\/10.1016\/j.jmb.2003.08.008","journal-title":"J Mol Biol"},{"key":"3697_CR23","doi-asserted-by":"publisher","first-page":"29426","DOI":"10.1074\/jbc.M003107200","volume":"275","author":"H Lee","year":"2000","unstructured":"Lee H, Mok KH, Muhandiram R et al (2000) Local structural elements in the mostly unstructured transcriptional activation domain of human p53. J Biol Chem 275:29426\u201329432. https:\/\/doi.org\/10.1074\/jbc.M003107200","journal-title":"J Biol Chem"},{"key":"3697_CR24","doi-asserted-by":"publisher","first-page":"573","DOI":"10.1016\/S0022-2836(02)00969-5","volume":"323","author":"LM Iakoucheva","year":"2002","unstructured":"Iakoucheva LM, Brown CJ, Lawson JD et al (2002) Intrinsic disorder in cell-signaling and cancer-associated proteins. J Mol Biol 323:573\u2013584. https:\/\/doi.org\/10.1016\/S0022-2836(02)00969-5","journal-title":"J Mol Biol"},{"key":"3697_CR25","doi-asserted-by":"publisher","first-page":"275","DOI":"10.1016\/j.jmb.2004.10.045","volume":"345","author":"W-Y Mark","year":"2005","unstructured":"Mark W-Y, Liao JCC, Lu Y et al (2005) Characterization of segments from the central region of BRCA1: an intrinsically disordered scaffold for multiple protein-protein and protein\u2013DNA interactions? J Mol Biol 345:275\u2013287. https:\/\/doi.org\/10.1016\/j.jmb.2004.10.045","journal-title":"J Mol Biol"},{"key":"3697_CR26","doi-asserted-by":"publisher","first-page":"3283","DOI":"10.1007\/s00018-018-2798-8","volume":"75","author":"E Langella","year":"2018","unstructured":"Langella E, Buonanno M, Vullo D et al (2018) Biochemical, biophysical and molecular dynamics studies on the proteoglycan-like domain of carbonic anhydrase IX. Cell Mol Life Sci 75:3283\u20133296. https:\/\/doi.org\/10.1007\/s00018-018-2798-8","journal-title":"Cell Mol Life Sci"},{"key":"3697_CR27","doi-asserted-by":"publisher","first-page":"4421","DOI":"10.1021\/cr200176r","volume":"112","author":"V Alterio","year":"2012","unstructured":"Alterio V, Di Fiore A, D\u2019Ambrosio K et al (2012) Multiple binding modes of inhibitors to carbonic anhydrases: how to design specific drugs targeting 15 different isoforms? Chem Rev 112:4421\u20134468. https:\/\/doi.org\/10.1021\/cr200176r","journal-title":"Chem Rev"},{"key":"3697_CR28","doi-asserted-by":"publisher","first-page":"27799","DOI":"10.1074\/jbc.M800938200","volume":"283","author":"M Hilvo","year":"2008","unstructured":"Hilvo M, Baranauskiene L, Salzano AM et al (2008) Biochemical characterization of CA IX, one of the most active carbonic anhydrase isozymes. J Biol Chem 283:27799\u201327809. https:\/\/doi.org\/10.1074\/jbc.M800938200","journal-title":"J Biol Chem"},{"key":"3697_CR29","doi-asserted-by":"publisher","first-page":"1784","DOI":"10.1097\/00005392-199805000-00146","volume":"159","author":"S-Y Liao","year":"1998","unstructured":"Liao S-Y, Aurelio ON, Jan K et al (1998) Identification of the MN\/CA9 protein as a reliable diagnostic biomarker of clear cell carcinoma of the kidney. J Urol 159:1784\u20131785. https:\/\/doi.org\/10.1097\/00005392-199805000-00146","journal-title":"J Urol"},{"key":"3697_CR30","first-page":"598","volume":"145","author":"SY Liao","year":"1994","unstructured":"Liao SY, Brewer C, Z\u00e1vada J et al (1994) Identification of the MN antigen as a diagnostic biomarker of cervical intraepithelial squamous and glandular neoplasia and cervical carcinomas. Am J Pathol 145:598\u2013609","journal-title":"Am J Pathol"},{"key":"3697_CR31","doi-asserted-by":"publisher","first-page":"282","DOI":"10.1021\/pr300565w","volume":"12","author":"P Buanne","year":"2013","unstructured":"Buanne P, Renzone G, Monteleone F et al (2013) Characterization of carbonic anhydrase IX interactome reveals proteins assisting its nuclear localization in hypoxic cells. J Proteome Res 12:282\u2013292. https:\/\/doi.org\/10.1021\/pr300565w","journal-title":"J Proteome Res"},{"key":"3697_CR32","doi-asserted-by":"publisher","first-page":"288","DOI":"10.1016\/j.radonc.2006.04.008","volume":"79","author":"RA Jonathan","year":"2006","unstructured":"Jonathan RA, Wijffels KIEM, Peeters W et al (2006) The prognostic value of endogenous hypoxia-related markers for head and neck squamous cell carcinomas treated with ARCON. Radiother Oncol 79:288\u2013297. https:\/\/doi.org\/10.1016\/j.radonc.2006.04.008","journal-title":"Radiother Oncol"},{"key":"3697_CR33","doi-asserted-by":"publisher","first-page":"806","DOI":"10.1034\/j.1399-3003.1999.14d14.x","volume":"14","author":"P Vermylen","year":"1999","unstructured":"Vermylen P, Roufosse C, Burny A et al (1999) Carbonic anhydrase IX antigen differentiates between preneoplastic malignant lesions in non-small cell lung carcinoma. Eur Respir J 14:806\u2013811. https:\/\/doi.org\/10.1034\/j.1399-3003.1999.14d14.x","journal-title":"Eur Respir J"},{"key":"3697_CR34","doi-asserted-by":"publisher","first-page":"279","DOI":"10.1016\/S0002-9440(10)65569-1","volume":"153","author":"J Saarnio","year":"1998","unstructured":"Saarnio J, Parkkila S, Parkkila A-K et al (1998) Immunohistochemical study of colorectal tumors for expression of a novel transmembrane carbonic anhydrase, MN\/CA IX, with potential value as a marker of cell proliferation. Am J Pathol 153:279\u2013285. https:\/\/doi.org\/10.1016\/S0002-9440(10)65569-1","journal-title":"Am J Pathol"},{"key":"3697_CR35","doi-asserted-by":"publisher","first-page":"740","DOI":"10.1016\/S0046-8177(97)90185-4","volume":"28","author":"J Turner","year":"1997","unstructured":"Turner J, Odze R, Crum C, Resnick M (1997) MN antigen expression in normal, preneoplastic, and neoplastic esophagus: a clinicopathological study of a new cancer-associated biomarker. Hum Pathol 28:740\u2013744. https:\/\/doi.org\/10.1016\/S0046-8177(97)90185-4","journal-title":"Hum Pathol"},{"key":"3697_CR36","doi-asserted-by":"publisher","first-page":"594","DOI":"10.1111\/j.1365-2559.2006.02523.x","volume":"49","author":"P Hynninen","year":"2006","unstructured":"Hynninen P, Vaskivuo L, Saarnio J et al (2006) Expression of transmembrane carbonic anhydrases IX and XII in ovarian tumours. Histopathology 49:594\u2013602. https:\/\/doi.org\/10.1111\/j.1365-2559.2006.02523.x","journal-title":"Histopathology"},{"key":"3697_CR37","doi-asserted-by":"publisher","first-page":"1483","DOI":"10.1016\/j.bmc.2012.09.018","volume":"21","author":"AJ Kivel\u00e4","year":"2013","unstructured":"Kivel\u00e4 AJ, Knuuttila A, R\u00e4s\u00e4nen J et al (2013) Carbonic anhydrase IX in malignant pleural mesotheliomas: a potential target for anti-cancer therapy. Bioorg Med Chem 21:1483\u20131488. https:\/\/doi.org\/10.1016\/j.bmc.2012.09.018","journal-title":"Bioorg Med Chem"},{"key":"3697_CR38","doi-asserted-by":"publisher","first-page":"465","DOI":"10.1215\/S1152851705000025","volume":"7","author":"MA Proescholdt","year":"2005","unstructured":"Proescholdt MA, Mayer C, Kubitza M et al (2005) Expression of hypoxia-inducible carbonic anhydrases in brain tumors. Neuro Oncol 7:465\u2013475. https:\/\/doi.org\/10.1215\/S1152851705000025","journal-title":"Neuro Oncol"},{"key":"3697_CR39","doi-asserted-by":"publisher","first-page":"1569","DOI":"10.2174\/09298673113209990227","volume":"21","author":"G Ilardi","year":"2014","unstructured":"Ilardi G, Zambrano N, Merolla F et al (2014) Histopathological determinants of tumor resistance: a special look to the immunohistochemical expression of carbonic anhydrase IX in human cancers. Curr Med Chem 21:1569\u20131582. https:\/\/doi.org\/10.2174\/09298673113209990227","journal-title":"Curr Med Chem"},{"key":"3697_CR40","doi-asserted-by":"publisher","first-page":"615","DOI":"10.1016\/j.oraloncology.2012.01.018","volume":"48","author":"NT Brockton","year":"2012","unstructured":"Brockton NT, Klimowicz AC, Bose P et al (2012) High stromal carbonic anhydrase IX expression is associated with nodal metastasis and decreased survival in patients with surgically-treated oral cavity squamous cell carcinoma. Oral Oncol 48:615\u2013622. https:\/\/doi.org\/10.1016\/j.oraloncology.2012.01.018","journal-title":"Oral Oncol"},{"key":"3697_CR41","doi-asserted-by":"publisher","first-page":"1791","DOI":"10.4161\/cc.24902","volume":"12","author":"T Fiaschi","year":"2013","unstructured":"Fiaschi T, Giannoni E, Taddei L et al (2013) Carbonic anhydrase IX from cancer-associated fibroblasts drives epithelial-mesenchymal transition in prostate carcinoma cells. Cell Cycle 12:1791\u20131801. https:\/\/doi.org\/10.4161\/cc.24902","journal-title":"Cell Cycle"},{"key":"3697_CR42","doi-asserted-by":"publisher","DOI":"10.1042\/BSR20200520","author":"G Wu","year":"2020","unstructured":"Wu G, Song X, Liu J et al (2020) Expression of CD44 and the survival in glioma: a meta-analysis. Biosci Rep. https:\/\/doi.org\/10.1042\/BSR20200520","journal-title":"Biosci Rep"},{"key":"3697_CR43","doi-asserted-by":"publisher","first-page":"21794","DOI":"10.18632\/oncotarget.15585","volume":"8","author":"M Chovanec","year":"2017","unstructured":"Chovanec M, Cierna Z, Miskovska V et al (2017) Prognostic role of programmed-death ligand 1 (PD-L1) expressing tumor infiltrating lymphocytes in testicular germ cell tumors. Oncotarget 8:21794\u201321805. https:\/\/doi.org\/10.18632\/oncotarget.15585","journal-title":"Oncotarget"},{"key":"3697_CR44","doi-asserted-by":"publisher","first-page":"13730","DOI":"10.18632\/oncotarget.14629","volume":"8","author":"I S\u00e1enz-de-Santa-Mar\u00eda","year":"2017","unstructured":"S\u00e1enz-de-Santa-Mar\u00eda I, Bernardo-Casti\u00f1eira C, Secades P et al (2017) Clinically relevant HIF-1\u03b1-dependent metabolic reprogramming in oropharyngeal squamous cell carcinomas includes coordinated activation of CAIX and the miR-210\/ISCU signaling axis, but not MCT1 and MCT4 upregulation. Oncotarget 8:13730\u201313746. https:\/\/doi.org\/10.18632\/oncotarget.14629","journal-title":"Oncotarget"},{"key":"3697_CR45","doi-asserted-by":"publisher","first-page":"164","DOI":"10.4161\/cc.3.2.618","volume":"3","author":"C Potter","year":"2004","unstructured":"Potter C, Harris AL (2004) Hypoxia inducible carbonic anhydrase IX, marker of tumor hypoxia, survival pathway and therapy target. Cell Cycle 3:164\u2013167","journal-title":"Cell Cycle"},{"key":"3697_CR46","doi-asserted-by":"publisher","first-page":"759","DOI":"10.3109\/14756366.2012.672983","volume":"27","author":"CT Supuran","year":"2012","unstructured":"Supuran CT (2012) Structure-based drug discovery of carbonic anhydrase inhibitors. J Enzyme Inhib Med Chem 27:759\u2013772. https:\/\/doi.org\/10.3109\/14756366.2012.672983","journal-title":"J Enzyme Inhib Med Chem"},{"key":"3697_CR47","doi-asserted-by":"publisher","first-page":"1896","DOI":"10.1021\/jm101541x","volume":"54","author":"F Pacchiano","year":"2011","unstructured":"Pacchiano F, Carta F, McDonald PC et al (2011) Ureido-substituted benzenesulfonamides potently inhibit carbonic anhydrase IX and show antimetastatic activity in a model of breast cancer metastasis. J Med Chem 54:1896\u20131902. https:\/\/doi.org\/10.1021\/jm101541x","journal-title":"J Med Chem"},{"key":"3697_CR48","doi-asserted-by":"publisher","first-page":"3364","DOI":"10.1158\/0008-5472.CAN-10-4261","volume":"71","author":"Y Lou","year":"2011","unstructured":"Lou Y, McDonald PC, Oloumi A et al (2011) Targeting tumor hypoxia: suppression of breast tumor growth and metastasis by novel carbonic anhydrase IX inhibitors. Cancer Res 71:3364\u20133376. https:\/\/doi.org\/10.1158\/0008-5472.CAN-10-4261","journal-title":"Cancer Res"},{"key":"3697_CR49","doi-asserted-by":"publisher","first-page":"1498","DOI":"10.1080\/14756366.2019.1653291","volume":"1","author":"E Langella","year":"2019","unstructured":"Langella E, Alterio V, D\u2019Ambrosio K et al (2019) Exploring benzoxaborole derivatives as carbonic anhydrase inhibitors: a structural and computational analysis reveals their conformational variability as a tool to increase enzyme selectivity. J Enzyme Inhib Med Chem 1:1498\u20131505. https:\/\/doi.org\/10.1080\/14756366.2019.1653291","journal-title":"J Enzyme Inhib Med Chem"},{"key":"3697_CR50","doi-asserted-by":"publisher","first-page":"1571","DOI":"10.3390\/ijms19061571","volume":"19","author":"M Buonanno","year":"2018","unstructured":"Buonanno M, Di Fiore A, Langella E et al (2018) The crystal structure of a hCA VII variant provides insights into the molecular determinants responsible for its catalytic behavior. Int J Mol Sci 19:1571. https:\/\/doi.org\/10.3390\/ijms19061571","journal-title":"Int J Mol Sci"},{"key":"3697_CR51","doi-asserted-by":"publisher","first-page":"1506","DOI":"10.1080\/14756366.2019.1653290","volume":"34","author":"G De Simone","year":"2019","unstructured":"De Simone G, Di Fiore A, Truppo E et al (2019) Exploration of the residues modulating the catalytic features of human carbonic anhydrase XIII by a site-specific mutagenesis approach. J Enzyme Inhib Med Chem 34:1506\u20131510. https:\/\/doi.org\/10.1080\/14756366.2019.1653290","journal-title":"J Enzyme Inhib Med Chem"},{"key":"3697_CR52","doi-asserted-by":"publisher","first-page":"168","DOI":"10.1038\/nrd2467","volume":"7","author":"CT Supuran","year":"2008","unstructured":"Supuran CT (2008) Carbonic anhydrases: novel therapeutic applications for inhibitors and activators. Nat Rev Drug Discov 7:168\u2013181. https:\/\/doi.org\/10.1038\/nrd2467","journal-title":"Nat Rev Drug Discov"},{"key":"3697_CR53","doi-asserted-by":"publisher","first-page":"1232","DOI":"10.1016\/j.biochi.2012.02.013","volume":"94","author":"V Alterio","year":"2012","unstructured":"Alterio V, Langella E, Viparelli F et al (2012) Structural and inhibition insights into carbonic anhydrase CDCA1 from the marine diatom Thalassiosira weissflogii. Biochimie 94:1232\u20131241. https:\/\/doi.org\/10.1016\/j.biochi.2012.02.013","journal-title":"Biochimie"},{"key":"3697_CR54","doi-asserted-by":"publisher","first-page":"1652","DOI":"10.1080\/14756366.2019.1664501","volume":"34","author":"S Akocak","year":"2019","unstructured":"Akocak S, Supuran CT (2019) Activation of \u03b1-, \u03b2-, \u03b3- \u03b4-, \u03b6- and \u03b7- class of carbonic anhydrases with amines and amino acids: a review. J Enzyme Inhib Med Chem 34:1652\u20131659. https:\/\/doi.org\/10.1080\/14756366.2019.1664501","journal-title":"J Enzyme Inhib Med Chem"},{"key":"3697_CR55","doi-asserted-by":"publisher","first-page":"1799","DOI":"10.1002\/med.21497","volume":"38","author":"CT Supuran","year":"2018","unstructured":"Supuran CT, Alterio V, Di Fiore A et al (2018) Inhibition of carbonic anhydrase IX targets primary tumors, metastases, and cancer stem cells: three for the price of one. Med Res Rev 38:1799\u20131836. https:\/\/doi.org\/10.1002\/med.21497","journal-title":"Med Res Rev"},{"key":"3697_CR56","doi-asserted-by":"publisher","first-page":"5","DOI":"10.1080\/14756366.2016.1225046","volume":"32","author":"DM Monti","year":"2017","unstructured":"Monti DM, De Simone G, Langella E et al (2017) Insights into the role of reactive sulfhydryl groups of carbonic anhydrase III and VII during oxidative damage. J Enzyme Inhib Med Chem 32:5\u201312","journal-title":"J Enzyme Inhib Med Chem"},{"key":"3697_CR57","doi-asserted-by":"publisher","first-page":"685","DOI":"10.2174\/138161208783877893","volume":"14","author":"J Pastorek","year":"2008","unstructured":"Pastorek J, Pastorekova S, Zatovicova M (2008) Cancer-associated carbonic anhydrases and their inhibition. Curr Pharm Des 14:685\u2013698. https:\/\/doi.org\/10.2174\/138161208783877893","journal-title":"Curr Pharm Des"},{"key":"3697_CR58","doi-asserted-by":"publisher","first-page":"66960","DOI":"10.18632\/oncotarget.16921","volume":"8","author":"HC Christianson","year":"2017","unstructured":"Christianson HC, Menard JA, Chandran VI et al (2017) Tumor antigen glycosaminoglycan modification regulates antibody-drug conjugate delivery and cytotoxicity. Oncotarget 8:66960\u201366974. https:\/\/doi.org\/10.18632\/oncotarget.16921","journal-title":"Oncotarget"},{"key":"3697_CR59","doi-asserted-by":"publisher","first-page":"7558","DOI":"10.1158\/0008-5472.CAN-11-2520","volume":"71","author":"P Ditte","year":"2011","unstructured":"Ditte P, Dequiedt F, Svastova E et al (2011) Phosphorylation of carbonic anhydrase IX controls its ability to mediate extracellular acidification in hypoxic tumors. Cancer Res 71:7558\u20137567. https:\/\/doi.org\/10.1158\/0008-5472.CAN-11-2520","journal-title":"Cancer Res"},{"key":"3697_CR60","doi-asserted-by":"publisher","first-page":"2935","DOI":"10.1016\/j.ejca.2005.09.011","volume":"41","author":"T Dorai","year":"2005","unstructured":"Dorai T, Sawczuk IS, Pastorek J et al (2005) The role of carbonic anhydrase IX overexpression in kidney cancer. Eur J Cancer 41:2935\u20132947. https:\/\/doi.org\/10.1016\/j.ejca.2005.09.011","journal-title":"Eur J Cancer"},{"key":"3697_CR61","doi-asserted-by":"publisher","first-page":"1460","DOI":"10.1021\/acschembio.7b00055","volume":"12","author":"M Buonanno","year":"2017","unstructured":"Buonanno M, Langella E, Zambrano N et al (2017) Disclosing the interaction of carbonic anhydrase IX with cullin-associated NEDD8-dissociated protein 1 by molecular modeling and integrated binding measurements. ACS Chem Biol 12:1460\u20131465. https:\/\/doi.org\/10.1021\/acschembio.7b00055","journal-title":"ACS Chem Biol"},{"key":"3697_CR62","doi-asserted-by":"publisher","first-page":"16233","DOI":"10.1073\/pnas.0908301106","volume":"106","author":"V Alterio","year":"2009","unstructured":"Alterio V, Hilvo M, Di Fiore A et al (2009) Crystal structure of the catalytic domain of the tumor-associated human carbonic anhydrase IX. Proc Natl Acad Sci U S A 106:16233\u201316238. https:\/\/doi.org\/10.1073\/pnas.0908301106","journal-title":"Proc Natl Acad Sci U S A"},{"key":"3697_CR63","doi-asserted-by":"publisher","first-page":"622","DOI":"10.1038\/s41416-018-0216-5","volume":"119","author":"S-H Lee","year":"2018","unstructured":"Lee S-H, McIntyre D, Honess D et al (2018) Carbonic anhydrase IX is a pH-stat that sets an acidic tumour extracellular pH in vivo. Br J Cancer 119:622\u2013630. https:\/\/doi.org\/10.1038\/s41416-018-0216-5","journal-title":"Br J Cancer"},{"key":"3697_CR64","doi-asserted-by":"publisher","first-page":"480","DOI":"10.1006\/geno.1996.0223","volume":"33","author":"R Opavsk\u00fd","year":"1996","unstructured":"Opavsk\u00fd R, Pastorekov\u00e1 S et al (1996) HumanMN\/CA9Gene, a novel member of the carbonic anhydrase family: structure and exon to protein domain relationships. Genomics 33:480\u2013487. https:\/\/doi.org\/10.1006\/geno.1996.0223","journal-title":"Genomics"},{"key":"3697_CR65","doi-asserted-by":"publisher","first-page":"27940","DOI":"10.18632\/oncotarget.25371","volume":"9","author":"S Ames","year":"2018","unstructured":"Ames S, Pastorekova S, Becker HM (2018) The proteoglycan-like domain of carbonic anhydrase IX mediates non-catalytic facilitation of lactate transport in cancer cells. Oncotarget 9:27940\u201327957","journal-title":"Oncotarget"},{"key":"3697_CR66","doi-asserted-by":"publisher","first-page":"5825","DOI":"10.1016\/j.bmcl.2009.08.088","volume":"19","author":"A Innocenti","year":"2009","unstructured":"Innocenti A, Pastorekova S, Pastorek J et al (2009) The proteoglycan region of the tumor-associated carbonic anhydrase isoform IX acts as anintrinsic buffer optimizing CO2 hydration at acidic pH values characteristic of solid tumors. Bioorg Med Chem Lett 19:5825\u20135828. https:\/\/doi.org\/10.1016\/j.bmcl.2009.08.088","journal-title":"Bioorg Med Chem Lett"},{"key":"3697_CR67","doi-asserted-by":"publisher","first-page":"439","DOI":"10.1016\/j.febslet.2004.10.043","volume":"577","author":"E \u0160vastova","year":"2004","unstructured":"\u0160vastova E, Hulikova A, Rafajova M et al (2004) Hypoxia activates the capacity of tumor-associated carbonic anhydrase IX to acidify extracellular pH. FEBS Lett 577:439\u2013445. https:\/\/doi.org\/10.1016\/j.febslet.2004.10.043","journal-title":"FEBS Lett"},{"key":"3697_CR68","doi-asserted-by":"publisher","first-page":"358","DOI":"10.1158\/0008-5472.CAN-08-2470","volume":"69","author":"J Chiche","year":"2009","unstructured":"Chiche J, Ilc K, Laferriere J et al (2009) Hypoxia-inducible carbonic anhydrase IX and XII promote tumor cell growth by counteracting acidosis through the regulation of the intracellular pH. Cancer Res 69:358\u2013368. https:\/\/doi.org\/10.1158\/0008-5472.CAN-08-2470","journal-title":"Cancer Res"},{"key":"3697_CR69","doi-asserted-by":"publisher","first-page":"407","DOI":"10.3390\/genes11040407","volume":"11","author":"M Delucchi","year":"2020","unstructured":"Delucchi M, Schaper E, Sachenkova O et al (2020) A new census of protein tandem repeats and their relationship with intrinsic disorder. Genes (Basel) 11:407. https:\/\/doi.org\/10.3390\/genes11040407","journal-title":"Genes (Basel)"},{"key":"3697_CR70","doi-asserted-by":"publisher","first-page":"2673","DOI":"10.1111\/j.1742-4658.2010.07684.x","volume":"277","author":"J Jorda","year":"2010","unstructured":"Jorda J, Xue B, Uversky VN, Kajava AV (2010) Protein tandem repeats - the more perfect, the less structured. FEBS J 277:2673\u20132682. https:\/\/doi.org\/10.1111\/j.1742-4658.2010.07684.x","journal-title":"FEBS J"},{"key":"3697_CR71","doi-asserted-by":"publisher","first-page":"415","DOI":"10.1002\/1097-0134(20001115)41:3<415::AID-PROT130>3.0.CO;2-7","volume":"41","author":"VN Uversky","year":"2000","unstructured":"Uversky VN, Gillespie JR, Fink AL (2000) Why are\u202f?natively unfolded? proteins unstructured under physiologic conditions? Proteins Struct Funct Genet 41:415\u2013427. https:\/\/doi.org\/10.1002\/1097-0134(20001115)41:3%3c415::AID-PROT130%3e3.0.CO;2-7","journal-title":"Proteins Struct Funct Genet"},{"key":"3697_CR72","doi-asserted-by":"publisher","first-page":"996","DOI":"10.1016\/j.bbapap.2010.01.011","volume":"1804","author":"B Xue","year":"2010","unstructured":"Xue B, Dunbrack RL, Williams RW et al (2010) PONDR-FIT: a meta-predictor of intrinsically disordered amino acids. Biochim Biophys Acta Proteins Proteomics 1804:996\u20131010. https:\/\/doi.org\/10.1016\/j.bbapap.2010.01.011","journal-title":"Biochim Biophys Acta Proteins Proteomics"},{"key":"3697_CR73","doi-asserted-by":"publisher","first-page":"3","DOI":"10.1007\/978-1-62703-691-7_1","volume":"1091","author":"YJ Huang","year":"2014","unstructured":"Huang YJ, Acton TB, Montelione GT (2014) DisMeta: a meta server for construct design and optimization. Methods Mol Biol 1091:3\u201316. https:\/\/doi.org\/10.1007\/978-1-62703-691-7_1","journal-title":"Methods Mol Biol"},{"key":"3697_CR74","doi-asserted-by":"publisher","first-page":"932","DOI":"10.1016\/j.bbapap.2012.12.008","volume":"1834","author":"VN Uversky","year":"2013","unstructured":"Uversky VN (2013) Unusual biophysics of intrinsically disordered proteins. Biochim Biophys Acta Proteins Proteomics 1834:932\u2013951. https:\/\/doi.org\/10.1016\/j.bbapap.2012.12.008","journal-title":"Biochim Biophys Acta Proteins Proteomics"},{"key":"3697_CR75","doi-asserted-by":"publisher","first-page":"309","DOI":"10.1002\/prot.20746","volume":"62","author":"GP Singh","year":"2005","unstructured":"Singh GP, Ganapathi M, Sandhu KS, Dash D (2005) Intrinsic unstructuredness and abundance of PEST motifs in eukaryotic proteomes. Proteins Struct Funct Bioinforma 62:309\u2013315. https:\/\/doi.org\/10.1002\/prot.20746","journal-title":"Proteins Struct Funct Bioinforma"},{"key":"3697_CR76","doi-asserted-by":"publisher","first-page":"9490","DOI":"10.1074\/jbc.271.16.9490","volume":"271","author":"K Takahashi","year":"1996","unstructured":"Takahashi K, Stamenkovic I, Cutler M et al (1996) Keratan sulfate modification of CD44 modulates adhesion to hyaluronate. J Biol Chem 271:9490\u20139496. https:\/\/doi.org\/10.1074\/jbc.271.16.9490","journal-title":"J Biol Chem"},{"key":"3697_CR77","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/S0304-4165(97)00119-0","volume":"1380","author":"M Nishimura","year":"1998","unstructured":"Nishimura M, Yan W, Mukudai Y et al (1998) Role of chondroitin sulfate\u2013hyaluronan interactions in the viscoelastic properties of extracellular matrices and fluids. Biochim Biophys Acta Gen Subj 1380:1\u20139. https:\/\/doi.org\/10.1016\/S0304-4165(97)00119-0","journal-title":"Biochim Biophys Acta Gen Subj"},{"key":"3697_CR78","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1111\/1523-1747.ep12319402","volume":"109","author":"A-L Tuhkanen","year":"1997","unstructured":"Tuhkanen A-L, Tammi M, Tammi R (1997) CD44 substituted with heparan sulfate and endo-\u03b2-galactosidase-sensitive oligosaccharides: a major proteoglycan in adult human epidermis. J Invest Dermatol 109:213\u2013218. https:\/\/doi.org\/10.1111\/1523-1747.ep12319402","journal-title":"J Invest Dermatol"},{"key":"3697_CR79","doi-asserted-by":"publisher","first-page":"295","DOI":"10.3390\/cells8040295","volume":"8","author":"C-J Lai","year":"2019","unstructured":"Lai C-J, Lin C-Y, Liao W-Y et al (2019) CD44 promotes migration and invasion of docetaxel-resistant prostate cancer cells likely via induction of hippo-yap signaling. Cells 8:295. https:\/\/doi.org\/10.3390\/cells8040295","journal-title":"Cells"},{"key":"3697_CR80","doi-asserted-by":"publisher","first-page":"1783","DOI":"10.3892\/ijmm.2020.4562","volume":"45","author":"J Yin","year":"2020","unstructured":"Yin J, Zhang H, Wu X et al (2020) CD44 inhibition attenuates EGFR signaling and enhances cisplatin sensitivity in human EGFR wild-type non-small-cell lung cancer cells. Int J Mol Med 45:1783\u20131792. https:\/\/doi.org\/10.3892\/ijmm.2020.4562","journal-title":"Int J Mol Med"},{"key":"3697_CR81","doi-asserted-by":"publisher","first-page":"1979","DOI":"10.1111\/jcmm.13118","volume":"21","author":"Y Liu","year":"2017","unstructured":"Liu Y, Yu C, Wu Y et al (2017) CD44 + fibroblasts increases breast cancer cell survival and drug resistance via IGF2BP3-CD44-IGF2 signalling. J Cell Mol Med 21:1979\u20131988. https:\/\/doi.org\/10.1111\/jcmm.13118","journal-title":"J Cell Mol Med"},{"key":"3697_CR82","doi-asserted-by":"publisher","first-page":"1808","DOI":"10.1054\/bjoc.2000.1111","volume":"82","author":"J Z\u00e1vada","year":"2000","unstructured":"Z\u00e1vada J, Z\u00e1vadov\u00e1 Z, Pastorek J et al (2000) Human tumour-associated cell adhesion protein MN\/CA IX: identification of M75 epitope and of the region mediating cell adhesion. Br J Cancer 82:1808\u20131813. https:\/\/doi.org\/10.1054\/bjoc.2000.1111","journal-title":"Br J Cancer"},{"key":"3697_CR83","doi-asserted-by":"publisher","DOI":"10.3389\/fphys.2013.00271","author":"L Csaderova","year":"2013","unstructured":"Csaderova L, Debreova M, Radvak P et al (2013) The effect of carbonic anhydrase IX on focal contacts during cell spreading and migration. Front Physiol. https:\/\/doi.org\/10.3389\/fphys.2013.00271","journal-title":"Front Physiol"},{"key":"3697_CR84","doi-asserted-by":"publisher","first-page":"2745","DOI":"10.3390\/ijms20112745","volume":"20","author":"M Debreova","year":"2019","unstructured":"Debreova M, Csaderova L, Burikova M et al (2019) CAIX regulates invadopodia formation through both a pH-dependent mechanism and interplay with actin regulatory proteins. Int J Mol Sci 20:2745. https:\/\/doi.org\/10.3390\/ijms20112745","journal-title":"Int J Mol Sci"},{"key":"3697_CR85","doi-asserted-by":"publisher","first-page":"52","DOI":"10.1016\/j.semcancer.2014.08.002","volume":"31","author":"J Pastorek","year":"2015","unstructured":"Pastorek J, Pastorekova S (2015) Hypoxia-induced carbonic anhydrase IX as a target for cancer therapy: from biology to clinical use. Semin Cancer Biol 31:52\u201364. https:\/\/doi.org\/10.1016\/j.semcancer.2014.08.002","journal-title":"Semin Cancer Biol"},{"key":"3697_CR86","doi-asserted-by":"publisher","first-page":"299","DOI":"10.1007\/s10555-007-9064-0","volume":"26","author":"P Swietach","year":"2007","unstructured":"Swietach P, Vaughan-Jones RD, Harris AL (2007) Regulation of tumor pH and the role of carbonic anhydrase 9. Cancer Meta Rev 26:299\u2013310. https:\/\/doi.org\/10.1007\/s10555-007-9064-0","journal-title":"Cancer Meta Rev"},{"key":"3697_CR87","first-page":"7075","volume":"60","author":"CC Wykoff","year":"2000","unstructured":"Wykoff CC, Beasley NJP, Watson PH et al (2000) Hypoxia-inducible expression of tumor-associated carbonic anhydrases. Cancer Res 60:7075\u20137083","journal-title":"Cancer Res"},{"key":"3697_CR88","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.22693","author":"AL Miles","year":"2017","unstructured":"Miles AL, Burr SP, Grice GL, Nathan JA (2017) The vacuolar-ATPase complex and assembly factors, TMEM199 and CCDC115, control HIF1\u03b1 prolyl hydroxylation by regulating cellular iron levels. Elife. https:\/\/doi.org\/10.7554\/eLife.22693","journal-title":"Elife"},{"key":"3697_CR89","doi-asserted-by":"publisher","first-page":"48","DOI":"10.1016\/j.molmet.2019.07.006","volume":"33","author":"VL Payen","year":"2020","unstructured":"Payen VL, Mina E, Van H\u00e9e VF et al (2020) Monocarboxylate transporters in cancer. Mol Metab 33:48\u201366. https:\/\/doi.org\/10.1016\/j.molmet.2019.07.006","journal-title":"Mol Metab"},{"key":"3697_CR90","doi-asserted-by":"publisher","first-page":"C1015","DOI":"10.1152\/ajpcell.1993.265.4.C1015","volume":"265","author":"R Martinez-Zaguilan","year":"1993","unstructured":"Martinez-Zaguilan R, Lynch RM, Martinez GM, Gillies RJ (1993) Vacuolar-type H(+)-ATPases are functionally expressed in plasma membranes of human tumor cells. Am J Physiol Physiol 265:C1015\u2013C1029. https:\/\/doi.org\/10.1152\/ajpcell.1993.265.4.C1015","journal-title":"Am J Physiol Physiol"},{"key":"3697_CR91","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1155\/2019\/3702783","volume":"19","author":"NCS Voss","year":"2019","unstructured":"Voss NCS, Kold-Petersen H, Henningsen MB et al (2019) Upregulated Na + \/H + -exchange protects human colon cancer tissue against intracellular acidification. Biomed Res Int 19:1\u20135. https:\/\/doi.org\/10.1155\/2019\/3702783","journal-title":"Biomed Res Int"},{"key":"3697_CR92","doi-asserted-by":"publisher","first-page":"2439","DOI":"10.1113\/JP273309","volume":"595","author":"SK Parks","year":"2017","unstructured":"Parks SK, Cormerais Y, Pouyss\u00e9gur J (2017) Hypoxia and cellular metabolism in tumour pathophysiology. J Physiol 595:2439\u20132450. https:\/\/doi.org\/10.1113\/JP273309","journal-title":"J Physiol"},{"key":"3697_CR93","doi-asserted-by":"publisher","first-page":"6509","DOI":"10.1038\/onc.2010.455","volume":"29","author":"P Swietach","year":"2010","unstructured":"Swietach P, Hulikova A, Vaughan-Jones RD, Harris AL (2010) New insights into the physiological role of carbonic anhydrase IX in tumour pH regulation. Oncogene 29:6509\u20136521. https:\/\/doi.org\/10.1038\/onc.2010.455","journal-title":"Oncogene"},{"key":"3697_CR94","doi-asserted-by":"publisher","first-page":"771","DOI":"10.1111\/j.1582-4934.2009.00994.x","volume":"14","author":"J Chiche","year":"2010","unstructured":"Chiche J, Brahimi-Horn MC, Pouyss\u00e9gur J (2010) Tumour hypoxia induces a metabolic shift causing acidosis: a common feature in cancer. J Cell Mol Med 14:771\u2013794. https:\/\/doi.org\/10.1111\/j.1582-4934.2009.00994.x","journal-title":"J Cell Mol Med"},{"key":"3697_CR95","doi-asserted-by":"publisher","first-page":"299","DOI":"10.1002\/jcp.22400","volume":"226","author":"SK Parks","year":"2011","unstructured":"Parks SK, Chiche J, Pouyssegur J (2011) pH control mechanisms of tumor survival and growth. J Cell Physiol 226:299\u2013308. https:\/\/doi.org\/10.1002\/jcp.22400","journal-title":"J Cell Physiol"},{"key":"3697_CR96","doi-asserted-by":"publisher","first-page":"C738","DOI":"10.1152\/ajpcell.00157.2007","volume":"293","author":"PE Morgan","year":"2007","unstructured":"Morgan PE, Pastorekov\u00e1 S, Stuart-Tilley AK et al (2007) Interactions of transmembrane carbonic anhydrase, CAIX, with bicarbonate transporters. Am J Physiol Physiol 293:C738\u2013C748. https:\/\/doi.org\/10.1152\/ajpcell.00157.2007","journal-title":"Am J Physiol Physiol"},{"issue":"2","key":"3697_CR97","doi-asserted-by":"publisher","first-page":"157","DOI":"10.1038\/s41416-019-0642-z","volume":"122","author":"HM Becker","year":"2020","unstructured":"Becker HM (2020) Carbonic anhydrase IX and acid transport in cancer. Br J Cancer 122(2):157\u2013167","journal-title":"Br J Cancer"},{"key":"3697_CR98","doi-asserted-by":"publisher","first-page":"19","DOI":"10.3390\/metabo8010019","volume":"8","author":"M Mboge","year":"2018","unstructured":"Mboge M, Mahon B, McKenna R, Frost S (2018) Carbonic anhydrases: role in pH control and cancer. Metabolites 8:19. https:\/\/doi.org\/10.3390\/metabo8010019","journal-title":"Metabolites"},{"key":"3697_CR99","doi-asserted-by":"publisher","DOI":"10.3389\/fphys.2013.00400","author":"O Sedlakova","year":"2014","unstructured":"Sedlakova O (2014) Carbonic anhydrase IX, a hypoxia-induced catalytic component of the pH regulating machinery in tumors. Front Physiol. https:\/\/doi.org\/10.3389\/fphys.2013.00400","journal-title":"Front Physiol"},{"key":"3697_CR100","doi-asserted-by":"publisher","first-page":"48","DOI":"10.3390\/metabo7030048","volume":"7","author":"CT Supuran","year":"2017","unstructured":"Supuran CT (2017) Carbonic anhydrase inhibition and the management of hypoxic tumors. Metabolites 7:48. https:\/\/doi.org\/10.3390\/metabo7030048","journal-title":"Metabolites"},{"key":"3697_CR101","doi-asserted-by":"publisher","first-page":"503","DOI":"10.1042\/BJ20061064","volume":"402","author":"S Monaco","year":"2007","unstructured":"Monaco S, Gioia M, Rodriguez J et al (2007) Modulation of the proteolytic activity of matrix metalloproteinase-2 (gelatinase A) on fibrinogen. Biochem J 402:503\u2013513. https:\/\/doi.org\/10.1042\/BJ20061064","journal-title":"Biochem J"},{"key":"3697_CR102","doi-asserted-by":"publisher","first-page":"2032","DOI":"10.1021\/mp200292c","volume":"8","author":"JW Wojtkowiak","year":"2011","unstructured":"Wojtkowiak JW, Verduzco D, Schramm KJ, Gillies RJ (2011) Drug Resistance and cellular adaptation to tumor acidic pH microenvironment. Mol Pharm 8:2032\u20132038. https:\/\/doi.org\/10.1021\/mp200292c","journal-title":"Mol Pharm"},{"key":"3697_CR103","doi-asserted-by":"publisher","first-page":"1391","DOI":"10.1016\/S0360-3016(00)01590-X","volume":"49","author":"T Ohtsubo","year":"2001","unstructured":"Ohtsubo T, Igawa H, Saito T et al (2001) Acidic environment modifies heat- or radiation-induced apoptosis in human maxillary cancer cells. Int J Radiat Oncol 49:1391\u20131398. https:\/\/doi.org\/10.1016\/S0360-3016(00)01590-X","journal-title":"Int J Radiat Oncol"},{"key":"3697_CR104","doi-asserted-by":"publisher","first-page":"3246","DOI":"10.2174\/138161210793429841","volume":"16","author":"TC Supuran","year":"2010","unstructured":"Supuran TC, Fiore A, Alterio V et al (2010) Recent advances in structural studies of the carbonic anhydrase family: the crystal structure of human CA IX and CA XIII. Curr Pharm Des 16:3246\u20133254. https:\/\/doi.org\/10.2174\/138161210793429841","journal-title":"Curr Pharm Des"},{"key":"3697_CR105","doi-asserted-by":"publisher","first-page":"767","DOI":"10.1038\/nrd3554","volume":"10","author":"D Neri","year":"2011","unstructured":"Neri D, Supuran CT (2011) Interfering with pH regulation in tumours as a therapeutic strategy. Nat Rev Drug Discov 10:767\u2013777. https:\/\/doi.org\/10.1038\/nrd3554","journal-title":"Nat Rev Drug Discov"},{"key":"3697_CR106","doi-asserted-by":"publisher","first-page":"737","DOI":"10.1517\/13543776.2013.798648","volume":"23","author":"SM Monti","year":"2013","unstructured":"Monti SM, Supuran CT, De Simone G (2013) Anticancer carbonic anhydrase inhibitors: a patent review (2008\u20132013). Expert Opin Ther Pat 23:737\u2013749. https:\/\/doi.org\/10.1517\/13543776.2013.798648","journal-title":"Expert Opin Ther Pat"},{"key":"3697_CR107","doi-asserted-by":"publisher","first-page":"620","DOI":"10.1016\/0042-6822(92)90464-Z","volume":"187","author":"S Pastorekov\u00e1","year":"1992","unstructured":"Pastorekov\u00e1 S, Z\u00e1vadov\u00e1 Z, Ko\u0161\u0165\u00e1l M et al (1992) A novel quasi-viral agent, MaTu, is a two-component system. Virology 187:620\u2013626. https:\/\/doi.org\/10.1016\/0042-6822(92)90464-Z","journal-title":"Virology"},{"key":"3697_CR108","doi-asserted-by":"publisher","first-page":"1448","DOI":"10.1002\/cncr.24163","volume":"115","author":"T Klatte","year":"2009","unstructured":"Klatte T, Seligson DB, Rao JY et al (2009) Carbonic anhydrase IX in bladder cancer. Cancer 115:1448\u20131458. https:\/\/doi.org\/10.1002\/cncr.24163","journal-title":"Cancer"},{"key":"3697_CR109","doi-asserted-by":"publisher","DOI":"10.1111\/j.1464-410x.2008.07649.x","author":"HK Jensen","year":"2008","unstructured":"Jensen HK, Nordsmark M, Donskov F et al (2008) Immunohistochemical expression of carbonic anhydrase IX assessed over time and during treatment in renal cell carcinoma. BJU Int Suppl. https:\/\/doi.org\/10.1111\/j.1464-410x.2008.07649.x","journal-title":"BJU Int Suppl"},{"key":"3697_CR110","doi-asserted-by":"publisher","first-page":"1275","DOI":"10.1002\/prot.21821","volume":"71","author":"V Kr\u00e1l","year":"2007","unstructured":"Kr\u00e1l V, Mader P, Collard R et al (2007) Stabilization of antibody structure upon association to a human carbonic anhydrase IX epitope studied by X-ray crystallography, microcalorimetry, and molecular dynamics simulations. Proteins Struct Funct Bioinforma 71:1275\u20131287. https:\/\/doi.org\/10.1002\/prot.21821","journal-title":"Proteins Struct Funct Bioinforma"},{"key":"3697_CR111","doi-asserted-by":"publisher","first-page":"304","DOI":"10.3390\/biom9080304","volume":"9","author":"D Stravinskiene","year":"2019","unstructured":"Stravinskiene D, Imbrasaite A, Petrikaite V et al (2019) New Monoclonal antibodies for a selective detection of membrane-associated and soluble forms of carbonic anhydrase IX in human cell lines and biological samples. Biomolecules 9:304. https:\/\/doi.org\/10.3390\/biom9080304","journal-title":"Biomolecules"},{"key":"3697_CR112","doi-asserted-by":"publisher","first-page":"1995","DOI":"10.1080\/07391102.2019.1623075","volume":"38","author":"A John","year":"2020","unstructured":"John A, Sivashanmugam M, Natarajan SK, Umashankar V (2020) Computational modeling of novel inhibitory peptides targeting proteoglycan like region of carbonic anhydrase IX and in vitro validation in HeLa cells. J Biomol Struct Dyn 38:1995\u20132006. https:\/\/doi.org\/10.1080\/07391102.2019.1623075","journal-title":"J Biomol Struct Dyn"},{"key":"3697_CR113","doi-asserted-by":"publisher","DOI":"10.1021\/acsomega.9b04203","author":"A John","year":"2020","unstructured":"John A, Vetrivel U, Sivashanmugam M, Natarajan SK (2020) Microsecond simulation of the proteoglycan-like region of carbonic anhydrase IX and design of chemical inhibitors targeting pH homeostasis in cancer cells. ACS Omega. https:\/\/doi.org\/10.1021\/acsomega.9b04203","journal-title":"ACS Omega"},{"key":"3697_CR114","doi-asserted-by":"publisher","first-page":"481","DOI":"10.1016\/j.cbpa.2010.06.169","volume":"14","author":"SJ Metallo","year":"2010","unstructured":"Metallo SJ (2010) Intrinsically disordered proteins are potential drug targets. Curr Opin Chem Biol 14:481\u2013488. https:\/\/doi.org\/10.1016\/j.cbpa.2010.06.169","journal-title":"Curr Opin Chem Biol"},{"key":"3697_CR115","doi-asserted-by":"publisher","first-page":"475","DOI":"10.1517\/17460441.2012.686489","volume":"7","author":"VN Uversky","year":"2012","unstructured":"Uversky VN (2012) Intrinsically disordered proteins and novel strategies for drug discovery. Expert Opin Drug Discov 7:475\u2013488. https:\/\/doi.org\/10.1517\/17460441.2012.686489","journal-title":"Expert Opin Drug Discov"},{"key":"3697_CR116","doi-asserted-by":"publisher","first-page":"782","DOI":"10.1016\/j.coph.2010.09.005","volume":"10","author":"AK Dunker","year":"2010","unstructured":"Dunker AK, Uversky VN (2010) Drugs for \u2018protein clouds\u2019: targeting intrinsically disordered transcription factors. Curr Opin Pharmacol 10:782\u2013788. https:\/\/doi.org\/10.1016\/j.coph.2010.09.005","journal-title":"Curr Opin Pharmacol"}],"container-title":["Cellular and Molecular Life Sciences"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s00018-020-03697-3.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/article\/10.1007\/s00018-020-03697-3\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s00018-020-03697-3.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,3,16]],"date-time":"2021-03-16T05:25:37Z","timestamp":1615872337000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/s00018-020-03697-3"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,11,17]]},"references-count":116,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2021,3]]}},"alternative-id":["3697"],"URL":"https:\/\/doi.org\/10.1007\/s00018-020-03697-3","relation":{},"ISSN":["1420-682X","1420-9071"],"issn-type":[{"value":"1420-682X","type":"print"},{"value":"1420-9071","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,11,17]]},"assertion":[{"value":"28 July 2020","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"26 September 2020","order":2,"name":"revised","label":"Revised","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"31 October 2020","order":3,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"17 November 2020","order":4,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Compliance with ethical standards"}},{"value":"The authors declare no conflict of interest.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interest"}},{"value":"Not applicable.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics approval"}},{"value":"Not applicable.","order":4,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent to participate"}},{"value":"All authors have read and agreed to the published version of the manuscript.","order":5,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent for publication"}},{"value":"Not applicable.","order":6,"name":"Ethics","group":{"name":"EthicsHeading","label":"Availability of data and material"}}]}}