statistiche ricercatore

Nome	#
A causative link between the structure of aberrant protein oligomers and their toxicity	241
Study of the early stages of HypN-N conversion intoamyloid-like aggregates: from the monomeric state tothe early-forming pre-fibrillar aggregates	175
The induction of α-helical structure in partially unfolded HypF-N does not affect its aggregation propensity	100
Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers	96
A comparison of the biochemical modifications caused by toxic and non-toxic protein oligomers in cells	90
Sequence and structural determinants of amyloid fibril formation	89
Salt anions promote the conversion of HypF-N into amyloid-like oligomers and modulate the structure of the oligomers and the monomeric precursor state.	70
Chaperones suppress protein oligomer toxicity: Insight into the molecular mechanism of action	46
Chaperones suppress the toxicity of aberrant protein aggregates. Molecular insight into the mechanism of action	41
Why proteins misfold?	35
Totale	983

	Totale	Lug	Ago	Sett	Ott	Nov	Dic	Gen	Feb	Mar	Apr	Mag	Giu
2019/2020	191	0	18	7	17	26	20	22	29	20	11	19	2
2020/2021	103	15	14	1	13	5	7	4	12	7	13	5	7
2021/2022	66	1	10	11	1	1	0	3	5	2	3	10	19
2022/2023	235	21	47	14	26	20	46	29	6	15	1	7	3
2023/2024	84	8	6	10	4	2	16	0	25	2	2	4	5
2024/2025	23	19	4	0	0	0	0	0	0	0	0	0	0
Totale													983