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DeCure for Finnish type amyloidosis

DeCure's autonomous Rare AI scientist is researching a drug-repurposing hypothesis for Finnish type amyloidosis — screening already-approved drugs against its 1-gene Open Targets disease module to publish open-access research. Research is fast; the path to publication is funded in milestone stages.

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The disease map

Disease moduleFinnish type amyloidosis maps to a 1-gene Open Targets module — the target space DeCure's AI scientist screens approved drugs against.
DeCure.ai methodSignature reversal (LINCS) plus network proximity (STRING) rank already-approved drugs likely to perturb this module — the same engine that produces DeCure.ai's repurposing hypotheses.
Repurposing thesisScreening approved medicines against this disease module, then publishing the evidence for the strongest candidate. Known pharmacology and human exposure data make the first question sharper — they do not establish safety or efficacy in a new indication.

Research record

01
ResearchComing soon
Candidate research + dossier — target rationale, drug-repurposing thesis and evidence pack.proof: Published dossier + on-chain hash
02
ValidationComing soon
In-vitro biological validation at a contract research org (CRO).proof: CRO contract + in-vitro report
03
Peer review & paperComing soon
Peer-reviewed paper published open-access (preprint + journal).proof: DOI + open-access link + on-chain hash

Current lead

No approved-drug candidate for finnish type amyloidosis is corroborated in the literature DeepSearch retrieved. Some conditions are managed with non-pharmacological care — a device, surgery or physical therapy — rather than a medicine; that may be the case here, or the literature we found may simply be too sparse yet to support a drug-repurposing angle.

Molecular view

gelsolin (GSN) — GSN is one of the genes genetically linked to this disease in Open Targets — shown as context, not as a drug target we're pursuing: no approved-drug candidate for this disease is yet corroborated in the literature we found.

Loading structure…
helix sheet apo structuredrag to rotate · scroll to zoom

RCSB Protein Data Bank · entry 6Q9R · 2.73 Å · ligand none (apo structure). Experimental structure, not a prediction.

What the evidence adds up to

In a nationwide Finnish series of 1666 subjects with rheumatoid arthritis who died in 1989, amyloidosis was listed as an immediate or intervening antecedent cause of death in 64 cases (3.8%) and as a contributory cause in 33 cases (2%), giving a combined prevalence of 5.8%. Amyloidosis had been diagnosed during life in 89 instances and was detected only at autopsy in eight. The lifespan of subjects with amyloidosis was shortened by 7.7 years compared with the rest of the series. The authors concluded that this prevalence was lower than most earlier studies had suggested.

A 2018 review of systemic amyloidosis in Western countries states that the most common form is light chain amyloidosis, caused by a misfolded light chain produced by a small B-cell clone. The review describes biomarker-based staging systems and a risk-adapted treatment approach. It notes that the cornerstone of treatment is rapid chemotherapy targeting the underlying plasma cell clone, and that novel approaches targeting other steps of the amyloid cascade are expected. The review says currently available treatments can alter the natural history if an early diagnosis is made.

A 2025 paper describes amyloidosis as a group of diseases characterised by abnormal extracellular deposition of amyloid proteins that disrupt organ function and can lead to organ failure. It states that amyloidosis may be systemic or localised, with several biochemical types, and that early diagnosis and treatment are crucial to improving outcomes. The paper provides no new data on Finnish type amyloidosis specifically.

What is still missing: no trial has tested a specific drug for Finnish type amyloidosis; no patient stratification or biomarker-based staging system has been validated for this hereditary form; funding for a dedicated clinical trial is absent.

Evidence

Retrieved by DeepSearch across 234,678,978 indexed works and resolved on OpenAlex — ranked by citations, including the results that did not work.

Lara D. Veeken · 1999 · 66 citations · open access

Amyloidosis in a nationwide series of 1666 subjects with rheumatoid arthritis who died during 1989 in Finland

AbstractOBJECTIVES: Virtually all studies dealing with the occurrence of amyloidosis in subjects with rheumatoid arthritis (RA) have been based on selected series collected from university clinics. The purpose of the study was to obtain information on the true prevalence of amyloidosis and the role of amyloidosis as a cause of death. METHODS: The study included all 1666 subjects (480 men and 1186 women) who had died in 1989 and had been entitled under the national sickness insurance scheme to receive specially reimbursed medication for RA. RESULTS: Amyloidosis was regarded as an immediate cause or an intervening antecedent cause of death in 64 cases (3.8%) and as a contributory cause of death in 33 cases (2%), corresponding to a prevalence of 5.8%. Amyloidosis had been diagnosed during life in 89 instances and was detected at autopsy in eight instances. Twenty-three (4.8%) of the subjects were men and 74 (6.2%) were women (P = 0.25). Compared with the remaining subjects in the study series, the lifespan of the subjects with amyloidosis was shortened by 7.7 yr. CONCLUSIONS: The prevalence of amyloidosis was lower than apparent from most earlier studies. Monitoring information derived from the Finnish sickness insurance system is a useful way of following trends in the occurrence of amyloidosis complicating RA.

https://doi.org/10.1093/rheumatology/38.6.499
Plastic & Reconstructive Surgery · 2011 · 33 citations

Gelsolin Amyloidosis as a Cause of Early Aging and Progressive Bilateral Facial Paralysis

AbstractBACKGROUND: Gelsolin amyloidosis, or Meretoja disease, is a dominantly inherited syndrome in which the collection of amyloid leads to early aging, bilateral progressive facial paralysis, and corneal lattice dystrophy. Characteristically, the major symptoms appear in the fifth decade of life, with brow ptosis and blepharochalasis, drooping of the facial tissues, and oral disturbances. Indications and methods, as well as the results of plastic surgical treatment, seem varied. To better understand and operate on this challenging group of patients, the authors evaluated the surgical experience of their department. METHODS: From the surgical database, all patients operated on in the authors' department for gelsolin amyloidosis from 1986 to 2004 were included. Disease severity was evaluated, together with data on the course of surgery, complications, and results. RESULTS: During 1986 through 2004, 35 gelsolin amyloidosis patients underwent surgery, totaling 67 operations and 95 procedures; 89 percent consulted a plastic surgeon for brow ptosis or blepharochalasis, 15 percent for problems in oral function, and 21 percent for ocular dryness or corneal ulcers. Total bilateral forehead palsy was noted in 63 percent, total unilateral palsy in 14 percent, and weakness of the frontal branch in 23 percent. The buccal branch was affected in 40 percent. Postoperative complications were observed in 31 percent and minor complaints in 60 percent. Two-thirds, however, seemed satisfied with the results. The majority required reoperations. CONCLUSIONS: Operative treatment of gelsolin amyloidosis is symptomatic. Due to relentless disease progression, a good functional and aesthetic result seems to require selected techniques and repeated surgery. Recognizing this underdiagnosed syndrome is essential.

https://doi.org/10.1097/prs.0b013e318213a0a2
Annals of Internal Medicine · 1938 · 24 citations

SECONDARY AMYLOIDOSIS: RESULTS OF THERAPY WITH DESICCATED WHOLE LIVER POWDER

AbstractArticle1 July 1938SECONDARY AMYLOIDOSIS: RESULTS OF THERAPY WITH DESICCATED WHOLE LIVER POWDERHAROLD G. GRAYZEL, M.D., MENDEL JACOBI, M.D.HAROLD G. GRAYZEL, M.D.Search for more papers by this author, MENDEL JACOBI, M.D.Search for more papers by this authorAuthor, Article, and Disclosure Informationhttps://doi.org/10.7326/0003-4819-12-1-39 SectionsAboutPDF ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinkedInRedditEmail ExcerptAmyloidosis secondary to a chronic infection is a complication of serious prognostic significance. In human beings presenting clinical signs of amyloidosis, the condition usually progresses to a fatal termination because the underlying cause remains active. Very few reported cases of recovery appear in the literature.1-13The majority of these recover only after an extensive operation which eradicates the primary disease provided the operative procedure is carried out early. This method of treatment can be employed with success only in a limited number of instances. The treatment of secondary amyloidosis in the majority of patients is therefore directed towards mitigating the...Bibliography1. KRETZSCHMARWESTBROOK PHBF: A case of chronic empyema with extensive amyloid degeneration—recovery, Proc. Med. Soc. County Kings, 1880, v, 343. Google Scholar2. OWEN I: Recovery from advanced lardaceous disease, Proc. Med. Soc. London, 1886, ix, 18. Google Scholar3. GAIRDNER WP: In discussion of F. Delafield's paper "On the diseases of the kidneys, popularly called Bright's disease," Trans. Assoc. Am. Phys., 1891, vi, 149. Google Scholar4. HARRINGHAM WP: Kidney diseases, 1912, Oxford University Press, Oxford, page 353. Google Scholar5. NATHAN M: Ueber die klinische Diagnose mittels Kongorotinjectionen, Munchen. med. Wchnschr., 1928, lxxv, 1883. Google Scholar6. WALDENSTROM H: On the formation and disappearance of amyloid in man, Acta chir. Scandinav., 1928, lxiii, 479. Google Scholar7. WALKER GF: A case of recovery from amyloid disease, Lancet, 1928, ii, 120. CrossrefGoogle Scholar8. GRAYZELJACOBIMASLOWWARSHALL HGMHHB: Experimental studies in amyloidosis, Proc. Soc. Exper. Biol. and Med., 1930, xxviii, 172. CrossrefGoogle Scholar9. WHITBECK BH: Liver meal in the treatment of amyloidosis in surgical tuberculosis, Jr. Bone and Joint Surg., 1932, xiv, 85. Google Scholar10. HABEIN HC: Amyloidosis: report of a case in which the patient recovered, Proc. Staff. Meet., Mayo Clinic, 1934, ix, 261. Google Scholar11. REIMANN HA: Case of amyloidosis with recovery, Jr. Am. Med. Assoc., 1935, civ, 1070. CrossrefGoogle Scholar12. KENNEDY WR: Renal amyloidosis, Canad. Med. Assoc. Jr., 1935, xxxiii, 385. Google Scholar13. ROSENBLATT MD: Recovery from generalized amyloidosis secondary to pulmonary tuberculosis—report of a case, Arch. Int. Med., 1936, lvii, 562. CrossrefGoogle Scholar14. GRAYZELJACOBI HGM: Generalized amyloidosis secondary to tuberculosis. (To be published.) Google Scholar15. GRAYZELJACOBIWARSHALLBOGINKRAMER HGMHBMB: Clinical and experimental studies in amyloidosis, Acta Paediat., 1933, xxvi, 177. Google Scholar16. GRAYZELJACOBIWARSHALLBOGINBOLKER HGMHBMH: Amyloidosis: experimental studies, Arch. Path., 1934, xvii, 50. Google Scholar17. LIPSTEINAUERBACH SO: Congo Red test, Quart. Bull. Sea View Hosp., 1937, ii, 120. Google Scholar18. WELLS HG: Chemical pathology, ed. 5, 1925, W. B. Saunders Company, Philadelphia. Google Scholar19. GRAYZELJACOBIMILLER HGMP: (To be published). Google Scholar20. RUTTGERSKAMSLER PA: Über Milzdiät bei Tuberkulösen, Beitr. z. Klin. d. Tuberk., 1929, lxxii, 68. CrossrefGoogle Scholar21. LOEFFLER F: Milzverfütterung bei eitrigen Knochen- und Gelenkerkrankungen, Zentralbl. f. Chir., 1929, lvi, 2946. Google Scholar22. ROPSCHITZ A: Über eine bequeme Durchführungstechnik der Rohmilztherapie bei destruktiver Gelenkstuberkulose, Med. Klin., 1930, xxvi, 166. Google Scholar23. KUSS H: Milztherapie bei Knochen- und Gelenktuberkulose, Med. Welt, 1929, iii, 1334. Google Scholar24. FLIEGEL O: Calf spleen diet in treatment of suppurative tuberculosis of joints, Jr. Bone and Joint Surg., 1930, xii, 788. Google Scholar25. ARMAND-DELLILE PF: Action favorable d'extraits spléniques sur certaines formes évolutives de la tuberculose pulmonaire chez l'enfant, Rev. d. l. Tuberc., 1928, ix, 256. Google Scholar26. BAYLE JC: L'Opothérapie splénique. Traitement de choix de la tuberculose, Presse Med., 1925, lxxvi, 1266. Google Scholar27. DUNHAM RW: The effect of splenic extract and bone marrow on the blood picture in pulmonary tuberculosis, Am. Jr. Med. Sci., 1925, clxx, 394. CrossrefGoogle Scholar28. DEJUST-DEFIVES S: Étude clinique de l'action simultanée des extraits foie, rein, rate sue diverses anémies (Anémies post-hemorragiques. Anémies de la tuberculose), Progres Med., 1930, lviii, 189. Google Scholar29. WATSON GF: Raw spleen extract in tuberculosis, Am. Rev. Tuberc., 1935, xxxii, 312. Google Scholar30. NEWTON HF: Über die Beeinflussung sekundärer Anämien bei Tuberkulösen durch Leberextrakte, Klin. Wchnschr., 1928, vii, 1062. CrossrefGoogle Scholar31. FAUSTSWARTZWELDER ECJC: Use of liver extract intramuscularly in the course of acute amebiasis in dogs, Proc. Soc. Exper. Biol. and Med., 1936, xxxiii, 514. CrossrefGoogle Scholar32. BECKERMOREHOUSE ERNF: Liver as a source of vitamin G, Science, 1936, lxxxiii, 530. CrossrefGoogle Scholar33. WEDEKIND T: Die Bedeutung des Reticuloendothels für die Tuberkulosetherapie, Klin. Wchnschr., 1930, ix, 822. CrossrefGoogle Scholar34. SCHURER-WALDHEIM F: Milzbestrahlung und retikulo-endothelialer Apparat, Wien. klin. Wchnschr., 1930, xliii, 201. Google Scholar35. SCHLIEPHAKESINCKE EG: Über die Wirkung von Milzextrakten auf das reticulo-endotheliale System, Gezeigt an der Trypanblauspeicherung, Klin. Wchnschr., 1931, x, 346. CrossrefGoogle Scholar36. HEROSE K: Experiments in the artificial production of amyloid, Bull. Johns Hopkins Hosp., 1918, xxix, 40. Google Scholar37. KUCZYNSKI MH: Neue Beiträge zur Lehre vom Amyloid, Klin. Wchnschr., 1923, i, 727. CrossrefGoogle Scholar38. SMETANA H: The relation of the reticulo-endothelial system to the formation of amyloid, Jr. Exper. Med., 1927, xlv, 619. CrossrefGoogle Scholar39. JAFFEE RH: Amyloidosis produced by injections of proteins, Arch. Path. and Lab. Med., 1926, i, 26. Google Scholar40. LETTERER E: Experimentelle Studien über Art und Entstehung des Amyloids, Zentralbl. f. inn. Med., 1926, xlvii, 417. Google Scholar41. EKLUNDREIMANN CMHA: The etiology of amyloid disease, Arch. Path., 1936, xxi, 1. Google Scholar42. CAVALLACCI G: Osservazioni sull' amiloidosi sperimentale, Pathologica, 1934, xxvi, 303. Google Scholar This content is PDF only. To continue reading please click on the PDF icon. Author, Article, and Disclosure InformationAffiliations: Brooklyn, New York*Received for publication June 29, 1937.From the pediatric service of the Neponsit Beach Hospital, the department of pathology of the Beth-El Hospital and the pediatric research laboratory of the Jewish Hospital, Brooklyn, N. Y. PreviousarticleNextarticle Advertisement FiguresReferencesRelatedDetails Metrics Cited byTreatmentResponse of systemic amyloidosis to dimethyl sulfoxidePATHOLOGICAL STUDY ON AMYLOIDOSIS A NEW INDUCTION METHOD OF AMYLOIDOSIS TRYPAN BLUE*Experimentelle Grundlagen einer Therapie der AmyloidosenAmyloidosis in childhoodAmyloidosis Associated with Rheumatoid ArthritisAmyloidosisSenile cardiac amyloidosisDie ParamyloidosePERIODIC DISEASE: A CLINICOPATHOLOGIC STUDY*NIMR A. TUQAN, M.D.AMYLOIDOSIS: ITS CLINICAL AND PATHOLOGIC MANIFESTATIONS, WITH A REPORT OF 12 CASES*GEORGE L. BERO, M.D.SECONDARY AMYLOIDOSIS IN LEPROSY*JOHN S. SHUTTLEWORTH, M.D., HILARY ROSS, B.S.“Primary” amyloidosisPRIMARY SYSTEMIC AMYLOIDOSISH. J. L. M.Beitrag zum Heilverlauf der AmyloidnephrosePrimary Systemic Amyloidosis: Report of 2 CasesAMYLOIDOSIS IN RHEUMATOID ARTHRITISThe heart in primary systemic amyloidosisThe Association of Hypernephroma With Amyloidosis of the Kidney 1 July 1938Volume 12, Issue 1Page: 39-58KeywordsAmyloidosisLiverPediatric infectionsResearch laboratoriesSurgery ePublished: 1 December 2008 Issue Published: 1 July 1938 PDF downloadLoading ...

https://doi.org/10.7326/0003-4819-12-1-39
Expert Review of Hematology · 2018 · 19 citations

New concepts in the treatment and diagnosis of amyloidosis

AbstractINTRODUCTION: The most common form of systemic amyloidosis in Western countries is light chain amyloidosis. It is characterized by the deposition of a misfolded light chain in target organs. This amyloid precursor is produced by a usually small but dangerous B-cell clone. Areas covered: This review examines the diagnostic workup of this disease and current knowledge of biomarker-based staging systems. In addition, a risk-adapted treatment approach is presented, as well as an overview of the new treatment strategies. Expert commentary: The cornerstone of treatment is rapid and effective chemotherapy targeting the underlying plasma cell clone. In the near future, this will probably be associated with novel approaches targeting other steps of the amyloid cascade that result in amyloid deposits. Currently available effective treatments can alter its natural history if an early diagnosis is made. The availability of novel, more powerful drugs, and identification of the cellular mechanisms of organ damage and of the characteristics of the amyloidogenic plasma-cell clone all give grounds to hope that a dramatic improvement in the treatment of this disease will be seen in the near future.

https://doi.org/10.1080/17474086.2018.1424534
Zenodo (CERN European Organization for Nuclear Research) · 2025 · 0 citations · open access

FEATURES OF THE PATHOLOGICAL AND ANATOMICAL MANIFESTATION OF AMYLOIDOSIS

AbstractAmyloidosis is a group of diseases characterized by the abnormal extracellular deposition of amyloid proteins in various tissues and organs. These deposits disrupt normal function and can lead to organ failure. Amyloidosis may be systemic or localized, with several biochemical types. Early diagnosis and treatment are crucial to improving outcomes. Key words: abnormal, proteins, organ, eosinophilic, pathological anatomy, myloidosis, diagnosis.

https://doi.org/10.5281/zenodo.15708925
IntechOpen eBooks · 2019 · 0 citations · open access

Amyloidosis: Systems-Based Therapies

AbstractIn this chapter, the authors will discuss the epidemiology and clinical presentations of amyloidosis. The main body of this chapter will concentrate on treatment options, both FDA-approved and experimental, specific to the various forms of amyloidosis. Since this set of diseases can affect multiple organ systems, we tackle the therapeutic avenues and the current challenges in each system under clinical investigation, including neurological, psychiatric, gastrointestinal, cardiovascular, endocrine, renal and hematologic, in addition to options for palliative treatment for severe symptom management and improved quality of life. Several recent groundbreaking discoveries have opened up the potential for successful treatment of peripheral and central neurological amyloidoses making this an exciting and evolving field.

https://doi.org/10.5772/intechopen.85201

Disease module: DeepOracle (Open Targets). Structures: RDKit from PubChem SMILES. Literature: retrieved by DeepSearch across 234,678,978 indexed works (targeted per-candidate search), resolved on OpenAlex.

DeCure is a research and publication project, not medical advice and not a treatment. "DeCure for X" describes a research goal, not a claim that a cure exists. Backing a cure is a contribution to fund the research — it is not an investment, and confers no yield, royalty, equity or IP ownership. Papers are published open-access by the DeCure.ai DAO.