Title : Urea titration of a lipase from Pseudomonas sp. reveals four different conformational states, with a stable partially folded state explaining its high aggregation propensity - Qafary_2021_Int.J.Biol.Macromol_174_32 |
Author(s) : Qafary M , Khajeh K , Ramazzotti M , Moosavi-Movahedi AA , Chiti F |
Ref : Int J Biol Macromol , 174 :32 , 2021 |
Abstract : |
PubMedSearch : Qafary_2021_Int.J.Biol.Macromol_174_32 |
PubMedID: 33508357 |
Title : Insight into the aggregation of lipase from Pseudomonas sp. using mutagenesis: protection of aggregation prone region by adoption of alpha-helix structure - Rashno_2018_Protein.Eng.Des.Sel_31_419 |
Author(s) : Rashno F , Khajeh K , Dabirmanesh B , Sajedi RH , Chiti F |
Ref : Protein Engineering Des Sel , 31 :419 , 2018 |
Abstract : |
PubMedSearch : Rashno_2018_Protein.Eng.Des.Sel_31_419 |
PubMedID: 31083708 |
Gene_locus related to this paper: 9psed-c7e3f2 |
Title : Very rapid amyloid fibril formation by a bacterial lipase in the absence of a detectable lag phase - Rashno_2017_Biochim.Biophys.Acta_1865_652 |
Author(s) : Rashno F , Khajeh K , Capitini C , Sajedi RH , Shokri MM , Chiti F |
Ref : Biochimica & Biophysica Acta , 1865 :652 , 2017 |
Abstract : |
PubMedSearch : Rashno_2017_Biochim.Biophys.Acta_1865_652 |
PubMedID: 28315735 |
Title : Amyloid fibril formation by a normally folded protein in the absence of denaturants and agitation - Monsef_2013_Amyloid_20_226 |
Author(s) : Monsef Shokri M , Ahmadian S , Bemporad F , Khajeh K , Chiti F |
Ref : Amyloid , 20 :226 , 2013 |
Abstract : |
PubMedSearch : Monsef_2013_Amyloid_20_226 |
PubMedID: 24053331 |