Chiti F

References (4)

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 : Qafary_2021_Int.J.Biol.Macromol_174_32
ESTHER : Qafary_2021_Int.J.Biol.Macromol_174_32
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 : Rashno_2018_Protein.Eng.Des.Sel_31_419
ESTHER : Rashno_2018_Protein.Eng.Des.Sel_31_419
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 : Rashno_2017_Biochim.Biophys.Acta_1865_652
ESTHER : Rashno_2017_Biochim.Biophys.Acta_1865_652
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 : Monsef_2013_Amyloid_20_226
ESTHER : Monsef_2013_Amyloid_20_226
PubMedSearch : Monsef_2013_Amyloid_20_226
PubMedID: 24053331