Affinity of zinc and copper ions for insulin monomersGavrilova, Julia; Tõugu, Vello; Palumaa, PeepMetallomics2014 / p. 1296-1300 : ill https://doi.org/10.1039/c4mt00059e Journal metrics at Scopus Article at Scopus Journal metrics at WOS Article at WOS

Cu(II) partially protects three histidine residues and the N-terminus of amyloid-β peptide from diethyl pyrocarbonate (DEPC) modificationFriedemann, Merlin; Tõugu, Vello; Palumaa, PeepFEBS Open Bio2020 / p. 1072-1081 https://doi.org/10.1002/2211-5463.12857 Journal metrics at Scopus Article at Scopus Journal metrics at WOS Article at WOS

Effect of agitation on the peptide fibrillization: Alzheimer’s amyloid- b peptide 1-42 but not amylin and insulin fibrils can grow under quiescent conditionsTiiman, Ann; Noormägi, Andra; Friedemann, Merlin; Krištal, Jekaterina; Palumaa, Peep; Tõugu, VelloJournal of peptide science2013 / p. 386-391 : ill https://doi.org/10.1002/psc.2513 Journal metrics at Scopus Article at Scopus Journal metrics at WOS Article at WOS

Effects of Zn2+ ions and environmental conditions on the fibrillization of insulin = Zn2+ ioonide ja keskkonnatingimuste mõju insuliini fibrillisatsioonileNoormägi, Andra2018 https://digi.lib.ttu.ee/i/?10378 https://www.ester.ee/record=b5148492*est

INSL5 is a high affinity specific agonist for GPCR142(GPR100)Liu, C.; Kuei, C.; Sutton, S.; Chen, J.; Bonaventure, P.; Wu, J.; Nepomuceno, D.; Kamme, F.; Tran, D.T.; Zhu, J.; Wilkinson, T.; Bathgate, R.; Eriste, Elo; Sillard, Rannar; Lovenberg, T.W.Journal of biological chemistry2005 / 1, p. 292-300 https://www.sciencedirect.com/science/article/pii/S0021925820765919#:~:text=Insulin%2Dlike%20peptide%205%20(INSL5,receptor%20has%20not%20been%20identified.

Insulin fibrillization at acidic and physiological pH values is controlled by different molecular mechanismsNoormägi, Andra; Valmsen, Karin; Tõugu, Vello; Palumaa, PeepThe protein journal2015 / p. 398-403 : ill https://doi.org/10.1007/s10930-015-9634-x Journal metrics at Scopus Article at Scopus Journal metrics at WOS Article at WOS

Interference of low-molecular substances with the thioflavin-T fluorescence assay of amyloid fibrilsNoormägi, Andra; Primar, Kateryna; Tõugu, Vello; Palumaa, PeepJournal of peptide science2012 / p. 59-64 : ill https://pubmed.ncbi.nlm.nih.gov/22083646/

Role of metal ions in amyloidogenic properties of insulin and superoxide dismutase = Metallioonide roll insuliini ja superoksiidi dismutaasi amüloidogeensetes omadustesGavrilova, Julia2022 https://doi.org/10.23658/taltech.44/2022 https://digikogu.taltech.ee/et/Item/693de590-2d9f-43d6-989e-ebac0544151d https://www.ester.ee/record=b5511706*est

Zn(II) ions co-secreted with insulin suppress inherent amyloidogenic properties of monomeric insulinNoormägi, Andra; Gavrilova, Julia; Smirnova, Julia; Tõugu, Vello; Palumaa, PeepBiochemical journal2010 / p. 511-518 https://pubmed.ncbi.nlm.nih.gov/20632994/

Zn(II) ions inhibit fibrillization of monomeric insulinNoormägi, Andra; Gavrilova, Julia; Smirnova, Julia; Tõugu, Vello; Palumaa, PeepFEBS journal2010 / Suppl. 1, p. 256

The possible mechanisms by which phanoside stimulates insulin secretion from rat isletsHoa, Nquyen Kahanh; Norberg, Ake; Sillard, RannarJournal of endocrinology2007 / p. 389-394 https://pubmed.ncbi.nlm.nih.gov/17283239/