A novel form of neurotensin post-translationally modified by arginylationEriste, Elo; Norberg, Ake; Nepomuceno, D.; Kuei, C.; Kamme, F.; Tran, D.T.; Strupat, K.; Jörnvall, Hans; Liu, C.; Lovenberg, T.W.; Sillard, RannarJournal of biological chemistry2005 / 42, p. 35089-35097 Cox17, a copper chaperone for cytochrome c oxidase : expression, purification and formation of mixed disulphide adducts with thiol reagentsVoronova, Anastassia; Kazantseva, Jekaterina; Tuuling, Marina; Sokolova, Niina; Sillard, Rannar; Palumaa, PeepProtein expression and purification2007 / 1, p. 138-144 : ill Human Sco1 functional studies and pathological implications of P174L mutantBanci, Lucia; Bertini, Ivano; Palumaa, Peep; Sillard, RannarProceedings of the National Academy of Sciences of the United States of America2007 / 1, p. 15-20 https://www.researchgate.net/publication/6617178_Human_Sco1_functional_studies_and_pathological_implications_of_the_P174L_mutant 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 Lysophosphatidic acid binds to and activates GPR92, a G protein-coupled receptor highly expressed in gastrointestinal lymphocytesKotarsky, K.; Boketoft, A.; Sillard, RannarJournal of pharmacology and experimental therapeutics2006 / p. 619-628 https://pubmed.ncbi.nlm.nih.gov/16651401/ Mammalian copper chaperone Cox17 exist in two metalloforms linked by oxydative switchPalumaa, Peep; Voronova, Anastassia; Kangur, Liina; Sillard, Rannar; Meyer-Klauke, W.; Meyer, Thomas; Rompel, AnetteThe FEBS journal2005 / Supplement 1, p. 386-387 Metal binding of metallothionein-3 versus metallothionein-2 : lower affinity and higher plasticityPalumaa, Peep; Tammiste, Indrek; Kruusel, Keiu; Kangur, Liina; Jörnvall, Hans; Sillard, RannarBiochimica et biophysica acta : proteins and proteomics2005 / 2, p. 205-211 : ill https://www.sciencedirect.com/science/article/pii/S1570963904003164 Metal-binding mechanism of Cox17, a copper chaperone for cytochrome c oxidasePalumaa, Peep; Kangur, Liina; Voronova, Anastassia; Sillard, RannarBiochemical journal2004 / 1, p. 307-314 Metallothionein induces a regenerative reactive astrocyte phenotype via JAK/STAT and RhoA signalling pathwaysLeung, Y.; Pankhurst, M.; Palumaa, Peep; Sillard, RannarExperimental neurology2010 / 1, p. 98-106 : ill Novel, efficient and regiospecific alkylation/arylation/heteroarylation of unsymmetrical azo compoundsTšubrik, Olga; Sillard, Rannar; Mäeorg, UnoSynthesis2006 / p. 843-846 https://www.researchgate.net/publication/239239897_Novel_Efficient_and_Regiospecific_AlkylationArylationHeteroarylation_of_Unsymmetrical_Azo_Compounds Oxidative switches in functioning of mammalian copper chaperone Cox17Voronova, Anastassia; Meyer-Klaucke, Wolfram; Meyer, Thomas; Rompel, Anette; Krebs, Bernt; Kazantseva, Jekaterina; Sillard, Rannar; Palumaa, PeepBiochemical journal2007 / p. 139-148 Pharmacological characterization of relaxin-3/INSL7 receptors GPCR135 and GPCR142 from different mammalian speciesChen, J.; Kuei, C.; Sutton, S.W.; Bonaventure, P.; Nepomuceno, D.; Eriste, Elo; Sillard, Rannar; Lovenberg, T.W.; Liu, C.Journal of pharmacology and experimental therapeutics2005 / 1, p. 83-95 Proteins in the insulin-secreting cell line MIN6 bind the imidazoline compound BL11282Shafqat, Jawed; Ishrat, Moin; Jägerbrink, Theres; Sillard, Rannar; Mäeorg, Uno; Efendic, Suad; Berggren, Per-Olof; Zaitsev, Sergei V.; Jörnvall, HansFEBS letters2008 / 11, p. 1613-1617 The native copper- and zinc- binding protein metallothionein blocks copper-mediated A[beeta] aggregation and toxicity in rat cortical neuronsChung, Roger S.; Howells, Claire; Zovo, Kairit; Palumaa, Peep; Sillard, RannarPLoS ONE2010 / 8, p. e12030 [11 p.] The possible mechanisms by which phanoside stimulates insulin secretion from rat isletsHoa, Nquyen Kahanh; Norberg, Ake; Sillard, RannarJournal of endocrinology2007 / p. 389-394