{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,28]],"date-time":"2025-09-28T20:10:19Z","timestamp":1759090219837,"version":"3.44.0"},"reference-count":42,"publisher":"Elsevier BV","issue":"10","license":[{"start":{"date-parts":[[2018,10,1]],"date-time":"2018-10-01T00:00:00Z","timestamp":1538352000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2018,10,1]],"date-time":"2018-10-01T00:00:00Z","timestamp":1538352000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2019,10,1]],"date-time":"2019-10-01T00:00:00Z","timestamp":1569888000000},"content-version":"vor","delay-in-days":365,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100001332","name":"CSIR","doi-asserted-by":"crossref","award":["miND BSC0115"],"award-info":[{"award-number":["miND BSC0115"]}],"id":[{"id":"10.13039\/501100001332","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100010218","name":"Department of Science and Technology","doi-asserted-by":"publisher","award":["SR\/CSI\/07\/2009(G)"],"award-info":[{"award-number":["SR\/CSI\/07\/2009(G)"]}],"id":[{"id":"10.13039\/501100010218","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],"published-print":{"date-parts":[[2018,10]]},"DOI":"10.1016\/j.bbamcr.2018.07.012","type":"journal-article","created":{"date-parts":[[2018,7,19]],"date-time":"2018-07-19T20:14:05Z","timestamp":1532031245000},"page":"1465-1478","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":2,"title":["Degradation of fibrin-\u03b2 amyloid co-aggregate: A novel function attributed to ubiquitin"],"prefix":"10.1016","volume":"1865","author":[{"given":"Payel","family":"Bhattacharjee","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Debashree","family":"De","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Debasish","family":"Bhattacharyya","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbamcr.2018.07.012_bb0005","series-title":"Aqueous Extract of Human Placenta, Recent Advances in Research on the Human Placenta","first-page":"77","author":"Chakraborty","year":"2012"},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0010","doi-asserted-by":"crossref","first-page":"2033","DOI":"10.1002\/jcp.22535","article-title":"Regulation of trypsin activity by peptide fraction of an aqueous extract of human placenta used as wound healer","volume":"226","author":"De","year":"2011","journal-title":"J. Cell. Physiol."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0015","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0059585","article-title":"Ubiquitin-like protein from human placental extract exhibits collagenase activity","volume":"8","author":"De","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0020","first-page":"732","article-title":"Cell adhesion by aqueous extract of human placenta used as wound healer","volume":"45","author":"Nath","year":"2007","journal-title":"Indian J. Exp. Biol."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0025","doi-asserted-by":"crossref","first-page":"873","DOI":"10.1016\/j.placenta.2010.07.010","article-title":"Anti-oxidative and anti-inflammatory activities of placental extracts in benzo[a] pyrene-exposed rats","volume":"31","author":"Park","year":"2010","journal-title":"Placenta"},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0030","doi-asserted-by":"crossref","first-page":"359","DOI":"10.5966\/sctm.2011-0021","article-title":"Original articles and reviews - fetal and neonatal stem cells: multipotent stromal stem cells from human placenta demonstrate high therapeutic potential","volume":"1","author":"Nazarov","year":"2012","journal-title":"Stem Cells Transl. Med."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0035","first-page":"770","article-title":"Fibrino(geno)lytic activity of the pregnant uterus, decidua, and placenta in rat","volume":"32","author":"Tympanidis","year":"1968","journal-title":"Obstet. Gynecol."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0040","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1055\/s-0038-1661167","article-title":"Haemostasis in normal pregnancy","volume":"52","author":"Stirling","year":"1984","journal-title":"Thromb. Haemost."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0045","first-page":"145","article-title":"The role of placental urokinase inhibitor in toxemia of pregnancy","volume":"4","author":"Terao","year":"1983","journal-title":"Biol. Res. Pregnancy Perinatol."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0050","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1055\/s-0038-1648672","article-title":"Alterations in the coagulation and fibrinolysis system in pregnancy, labour and puerperium, with special reference to a possible transitory state of intravascular coagulation during labour","volume":"40","author":"Gilabert","year":"1978","journal-title":"Thromb. Haemost."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0055","first-page":"1","article-title":"Hemostatic changes in normal pregnancy","volume":"1","author":"Prisco","year":"2005","journal-title":"Haematol. Rep."},{"year":"2014","series-title":"Evaluation of Bioactive Components from Natural Products for Prevention of Toxicity and Neurological Disorders","author":"Bhattacharjee","key":"10.1016\/j.bbamcr.2018.07.012_bb0060"},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0065","doi-asserted-by":"crossref","first-page":"3033","DOI":"10.1073\/pnas.84.9.3033","article-title":"Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer disease brains","volume":"84","author":"Perry","year":"1987","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0070","doi-asserted-by":"crossref","first-page":"1091","DOI":"10.1016\/S0731-7085(03)00654-X","article-title":"Spectroscopic and chromatographic evidences of NADPH in human placental extract used as wound healer","volume":"34","author":"Datta","year":"2004","journal-title":"J. Pharm. Biomed. Anal."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0075","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1016\/0003-9861(52)90121-5","article-title":"The fibrin plate method for estimating fibrino(geno)lytic activity","volume":"40","author":"Astrup","year":"1952","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0080","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1006\/abio.1998.2816","article-title":"Fibrin zymography: a direct analysis of fibrino(geno)lytic enzymes on gels","volume":"263","author":"Kim","year":"1998","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0085","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1016\/j.toxicon.2011.02.008","article-title":"Thermal detoxification of the venom from Daboiarussellirusselli of Eastern India with restoration of fibrino(geno)lytic activity","volume":"57","author":"Maity","year":"2007","journal-title":"Toxicon"},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0090","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1016\/j.jep.2012.10.056","article-title":"Characterization of the aqueous extract of the root of Aristolochiaindica: evaluation of its traditional use as an antidote for snakebites","volume":"145","author":"Bhattacharjee","year":"2013","journal-title":"J. Ethnopharmacol."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0095","doi-asserted-by":"crossref","first-page":"181","DOI":"10.4269\/ajtmh.1988.38.181","article-title":"A rapid dot immunoassay for the detection of serum antibodies to Eastern equine encephalomyelitis and St. Louis encephalitis viruses in sentinel chickens","volume":"38","author":"Oprandy","year":"1988","journal-title":"Am. J. Trop. Med. Hyg."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0100","doi-asserted-by":"crossref","first-page":"21812","DOI":"10.1073\/pnas.1010373107","article-title":"Alzheimer's disease peptide \u03b2-amyloid interacts with fibrinogen and induces its oligomerization","volume":"107","author":"Ahn","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0105","series-title":"Fibrinolysis and Thrombolysis","first-page":"3","article-title":"An insight into the abnormal fibrin clots: its pathophysiological roles","author":"Bhattacharjee","year":"2014"},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0110","doi-asserted-by":"crossref","first-page":"30559","DOI":"10.1074\/jbc.M113.511410","article-title":"Factor V activator from Daboiarussellirusselli venom destabilizes \u03b2-amyloid aggregate, the hallmark of Alzheimer disease","volume":"288","author":"Bhattacharjee","year":"2013","journal-title":"J. Biol. Chem."},{"year":"2008","series-title":"University of Colorado Denver, Biophysics Core Facility","author":"Biacore Tutorial","key":"10.1016\/j.bbamcr.2018.07.012_bb0115"},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0120","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1046\/j.1471-4159.1995.65010218.x","article-title":"The intracellular component of cellular 3-(4,5-dimethylthiazol-2-yl)-2, 5-diphenyltetrazolium bromide (MTT) reduction is specifically inhibited by beta amyloid peptides","volume":"65","author":"Shearman","year":"1995","journal-title":"J. Neurochem."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0125","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1161\/ATVBAHA.110.213389","article-title":"Molecular mechanisms affecting fibrin structure and stability","volume":"31","author":"Lord","year":"2011","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0130","doi-asserted-by":"crossref","first-page":"3342","DOI":"10.1182\/blood-2011-11-389668","article-title":"A\u03b2 delays fibrin clot lysis by altering fibrin structure and attenuating plasminogen binding to fibrin","volume":"119","author":"Zamolodchikov","year":"2012","journal-title":"Blood"},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0135","doi-asserted-by":"crossref","first-page":"3685","DOI":"10.1073\/pnas.84.11.3685","article-title":"Ubiquitin has intrinsic proteolytic activity: implications for cellular regulation","volume":"84","author":"Fried","year":"1987","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0140","first-page":"303","article-title":"Ubiquitin with a non-ATP-dependent slow intrinsic protelolytic activity: a mild and rapid purification procedure","volume":"29","author":"Parakh","year":"1992","journal-title":"Indian J. Biochem. Biophys."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0145","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1016\/j.preghy.2014.10.295","article-title":"[289-POS]: placental heparin sulphateglycosaminoglycans in pre-eclampsia","volume":"5","author":"Gunatillake","year":"2015","journal-title":"Pregnancy Hypertens."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0150","doi-asserted-by":"crossref","DOI":"10.1161\/CIRCULATIONAHA.109.853127","article-title":"Preeclampsia, a disease of the maternal endothelium: the role of anti-angiogenic factors and implications for later cardiovascular disease","volume":"123","author":"Powe","year":"2011","journal-title":"Circulation"},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0155","first-page":"253","article-title":"Increased placental antifibrino(geno)lytic potential and fibrin deposits in pregnancy-induced hypertension and preeclampsia","volume":"74","author":"Kanfer","year":"1996","journal-title":"Lab. Investig."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0160","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1515\/JPM.2009.060","article-title":"Coagulation and fibrinolysis related cytokine imbalance in preeclampsia: the role of placental trophoblasts","volume":"37","author":"Teng","year":"2009","journal-title":"J. Perinat. Med."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0165","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1186\/alzrt6","article-title":"Cerebral amyloid angiopathy in the aetiology and immunotherapy of Alzheimer disease","volume":"1","author":"Weller","year":"2009","journal-title":"Alzheimers Res. Ther."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0170","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1111\/j.1750-3639.1996.tb00798.x","article-title":"Peripheral nerve amyloidosis","volume":"6","author":"Reilly","year":"1996","journal-title":"Brain Pathol."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0175","doi-asserted-by":"crossref","first-page":"976","DOI":"10.3390\/ijms10030976","article-title":"Molecular pathology of human prion diseases","volume":"10","author":"Kovacs","year":"2009","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0180","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1007\/s00401-009-0501-8","article-title":"Genetics and molecular pathogenesis of sporadic and hereditary cerebral amyloid angiopathies","volume":"118","author":"Revesz","year":"2009","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0185","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1161\/01.STR.18.2.311","article-title":"Cerebral amyloid angiopathy. A critical review","volume":"18","author":"Vinters","year":"1987","journal-title":"Stroke"},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0190","doi-asserted-by":"crossref","first-page":"2637","DOI":"10.1161\/01.STR.0000189721.31432.26","article-title":"Fibrinogen is associated with an increased risk of Alzheimer disease and vascular dementia","volume":"36","author":"van Oijen","year":"2005","journal-title":"Stroke"},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0195","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1016\/j.neuron.2010.05.014","article-title":"Fibrinogen and beta-amyloid association alters thrombosis and fibrinolysis: a possible contributing factor to Alzheimer's disease","volume":"66","author":"Cortes-Canteli","year":"2010","journal-title":"Neuron"},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0200","doi-asserted-by":"crossref","first-page":"134","DOI":"10.17925\/ENR.2012.07.02.134","article-title":"Advances in our understanding of the pathophysiology, detection and management of cerebral amyloid angiopathy","volume":"7","author":"Pontes-Neto","year":"2012","journal-title":"Eur. Neurol. Rev."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0205","doi-asserted-by":"crossref","first-page":"1251","DOI":"10.1038\/jcbfm.2013.76","article-title":"The APOE \u025b4\/\u025b4 genotype potentiates vascular fibrin(ogen) deposition in amyloid-laden vessels in the brains of Alzheimer's disease patients","volume":"33","author":"Hultman","year":"2013","journal-title":"J. Cereb. Blood Flow Metab."},{"key":"10.1016\/j.bbamcr.2018.07.012_bb0210","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.1084\/jem.20131751","article-title":"A novel A\u03b2-fibrinogen interaction inhibitor rescues altered thrombosis and cognitive decline in Alzheimer's disease mice","volume":"211","author":"Ahn","year":"2014","journal-title":"J. Exp. Med."}],"container-title":["Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0167488918301873?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0167488918301873?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,28]],"date-time":"2025-09-28T19:46:43Z","timestamp":1759088803000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0167488918301873"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,10]]},"references-count":42,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2018,10]]}},"alternative-id":["S0167488918301873"],"URL":"https:\/\/doi.org\/10.1016\/j.bbamcr.2018.07.012","relation":{},"ISSN":["0167-4889"],"issn-type":[{"type":"print","value":"0167-4889"}],"subject":[],"published":{"date-parts":[[2018,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Degradation of fibrin-\u03b2 amyloid co-aggregate: A novel function attributed to ubiquitin","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - Molecular Cell Research","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbamcr.2018.07.012","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 Published by Elsevier B.V.","name":"copyright","label":"Copyright"}]}}