PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17254602-3	2007	In vitro, exposure of beta2m to equimolar Cu(2+) under near-physiological conditions can result in self-association leading to amyloid fiber formation.	cupric ion	42-48	beta-2-microglobulin	Homo sapiens	22-28	
23126476-10	2012	Interestingly, such structurally altered beta2m showed a specific affinity for divalent Cu(2+) ions, which is thought to be a candidate for initiating fibril formation.	cupric ion	88-94	beta-2-microglobulin	Homo sapiens	41-47	
22777780-5	2012	Protein engineering, or the addition of Cu(2+) ions, sodium dodecyl sulphate, trifluoroethanol, heparin, or protein stabilisers, was employed to perturb the conformational dynamics of beta(2)m.	cupric ion	40-46	beta-2-microglobulin	Homo sapiens	184-192	
19518133-0	2009	Delineating the conformational elements responsible for Cu(2+)-induced oligomerization of beta-2 microglobulin.	cupric ion	56-62	beta-2-microglobulin	Homo sapiens	90-110	
19377278-3	2009	Using Cu(2+) as a trigger, we have trapped, isolated, and crystallized a stable oligomer of beta2m that is populated under amyloidogenic solution conditions (Calabrese et al.	cupric ion	6-12	beta-2-microglobulin	Homo sapiens	92-98	
19377278-8	2009	A comparison of Cu(2+) binding to beta2m and PrP reveals common features.	cupric ion	16-22	beta-2-microglobulin	Homo sapiens	34-40	
19172750-3	2008	For beta2m, oligomerization into pre-amyloidogenic states occurs in specific response to coordination by Cu2+.	cupric ion	105-109	beta-2-microglobulin	Homo sapiens	4-10	
18383026-0	2008	The influence of Cu(2+) on the unfolding and refolding of intact and proteolytically processed beta(2)-microglobulin.	cupric ion	17-23	beta-2-microglobulin	Homo sapiens	95-116	
18383026-5	2008	The experiments provide both qualitative and quantitative data showing the specific destabilizing effects of Cu(2+)-ions on the folding of wt beta(2)m.	cupric ion	109-115	beta-2-microglobulin	Homo sapiens	142-150	
16513784-0	2006	Molecular basis for the Cu2+ binding-induced destabilization of beta2-microglobulin revealed by molecular dynamics simulation.	cupric ion	24-28	beta-2-microglobulin	Homo sapiens	64-83	
16513784-1	2006	According to experimental data, binding of the Cu(2+) ions destabilizes the native state of beta2-microglobulin (beta2m).	cupric ion	47-53	beta-2-microglobulin	Homo sapiens	92-111	
16513784-1	2006	According to experimental data, binding of the Cu(2+) ions destabilizes the native state of beta2-microglobulin (beta2m).	cupric ion	47-53	beta-2-microglobulin	Homo sapiens	113-119	
15196023-2	2004	In vitro, wild-type beta2m can be converted to amyloid under physiological conditions by exposure to biomedically relevant concentrations of Cu(2+).	cupric ion	141-147	beta-2-microglobulin	Homo sapiens	20-26	
12186550-3	2002	The basis for this effect is destabilization and incorporation of beta2m into amyloid fibers upon binding of Cu(2+).	cupric ion	109-115	beta-2-microglobulin	Homo sapiens	66-72	
12186550-4	2002	In this work, we demonstrate that while beta2m binds Cu(2+) specifically in the native state, it is binding of Cu(2+) by non-native states of beta2m which is responsible for destabilization.	cupric ion	53-59	beta-2-microglobulin	Homo sapiens	40-46	
12186550-4	2002	In this work, we demonstrate that while beta2m binds Cu(2+) specifically in the native state, it is binding of Cu(2+) by non-native states of beta2m which is responsible for destabilization.	cupric ion	111-117	beta-2-microglobulin	Homo sapiens	40-46	
12186550-4	2002	In this work, we demonstrate that while beta2m binds Cu(2+) specifically in the native state, it is binding of Cu(2+) by non-native states of beta2m which is responsible for destabilization.	cupric ion	111-117	beta-2-microglobulin	Homo sapiens	142-148	
12186550-8	2002	Binding of Cu(2+) in non-native states of beta2m is mediated by residues H13, H51, and H84, but not H31.	cupric ion	11-17	beta-2-microglobulin	Homo sapiens	42-48	
11371157-4	2001	Here, we present evidence for a novel interaction between beta2m and Cu(2+) at a concentration within institutionally recommended limits for this metal ion in dialysate solution.	cupric ion	69-75	beta-2-microglobulin	Homo sapiens	58-64