PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8601452-0 1996 Chemical modification of porcine kidney aminopeptidase P indicates the involvement of two critical histidine residues. Histidine 99-108 amyloid beta precursor protein Homo sapiens 40-56 34878265-3 2021 In this work, we found that a N-truncated Abeta analogue bearing a His-2 motif, Abeta5-9, forms a stable Ni(II) high-spin octahedral complex at a physiological pH of 7.4 with labile coordination sites and facilitates ternary interactions with phosphates and nucleotides. Histidine 67-70 amyloid beta precursor protein Homo sapiens 42-47 8245966-7 1993 The pH profile of heparin-induced aggregation of A beta(1-28) has a midpoint pH of approximately 6.5, suggesting that one or more histidine residues must be protonated for binding to occur. Histidine 130-139 amyloid beta precursor protein Homo sapiens 49-55 8245966-8 1993 Analysis of the A beta sequence reveals a consensus heparin-binding domain at residues 12-17, and this motif contains histidines at positions 13 and 14 that may be involved in the interaction with glycosaminoglycans. Histidine 118-128 amyloid beta precursor protein Homo sapiens 16-22 1283743-3 1992 As a result of this study a series of low-energy conformations were identified showing a common folding pattern with residues Val-3, Pro-4, His-5 and Lys-6 forming a beta turn. Histidine 140-143 amyloid beta precursor protein Homo sapiens 164-170 7510502-4 1993 The recently demonstrated presence of 4 basic amino acids (1 arginine, 3 histidine) in the cleaved fragment of the amyloid precursor protein (APP) suggest us to hypothesise that this APP portion may represent the common constitutive element of the many morphologically different alterations found in the brains of senile demented patients. Histidine 73-82 amyloid beta precursor protein Homo sapiens 115-140 34163842-6 2021 Both Ru1 and Ru2 contain an extended planar imidazo(4,5-f)(1,10)phenanthroline ligand, as compared to a 2,2"-bipyridine ligand for Ru3, and we show that the presence of the phenanthroline ligand promotes covalent binding to Abeta peptide His residues, and in addition, leads to a pronounced effect on peptide aggregation immediately after photoactivation. Histidine 238-241 amyloid beta precursor protein Homo sapiens 224-229 34371051-1 2021 One of the hallmarks of Alzheimer"s Disease (AD) is the anomalous binding involving amyloid-beta (Abeta) peptide and metal ions, such as copper, formed through histidine (His) residues. Histidine 160-169 amyloid beta precursor protein Homo sapiens 84-96 34371051-1 2021 One of the hallmarks of Alzheimer"s Disease (AD) is the anomalous binding involving amyloid-beta (Abeta) peptide and metal ions, such as copper, formed through histidine (His) residues. Histidine 160-169 amyloid beta precursor protein Homo sapiens 98-103 34371051-1 2021 One of the hallmarks of Alzheimer"s Disease (AD) is the anomalous binding involving amyloid-beta (Abeta) peptide and metal ions, such as copper, formed through histidine (His) residues. Histidine 171-174 amyloid beta precursor protein Homo sapiens 84-96 34371051-1 2021 One of the hallmarks of Alzheimer"s Disease (AD) is the anomalous binding involving amyloid-beta (Abeta) peptide and metal ions, such as copper, formed through histidine (His) residues. Histidine 171-174 amyloid beta precursor protein Homo sapiens 98-103 34343891-12 2021 The molecular docking and MD simulation results revealed that the active site residue Glu-538 of bacterial NEP along with Zn2+ interact with His-13 of Abeta peptide. Histidine 141-144 amyloid beta precursor protein Homo sapiens 151-156 33052996-7 2020 The results show that the oxidative capacity of OH coordinated Cu(ii)Abeta is significantly lower than that of the free OH radical and that propagation toward Abeta Asp and His residues is favoured over Tyr residues. Histidine 173-176 amyloid beta precursor protein Homo sapiens 69-74 35216047-0 2022 Mechanistic Insights into the Polymorphic Associations and Cross-Seeding of Abeta and hIAPP in the Presence of Histidine Tautomerism: An All-Atom Molecular Dynamic Study. Histidine 111-120 amyloid beta precursor protein Homo sapiens 76-81 32730791-1 2020 Histidine state (protonated or delta or epsilon tautomer) has been considered the origin of abnormal misfolding and aggregation of beta-amyloid (Abeta). Histidine 0-9 amyloid beta precursor protein Homo sapiens 145-150 31658742-7 2019 Iron and copper were coordinated by the same N-terminal region of Abeta, likely through histidine residues. Histidine 88-97 amyloid beta precursor protein Homo sapiens 66-71 32630528-1 2020 The coordination of zinc ions by histidine residues of amyloid-beta peptide (Abeta) plays a critical role in the zinc-induced Abeta aggregation implicated in Alzheimer"s disease (AD) pathogenesis. Histidine 33-42 amyloid beta precursor protein Homo sapiens 77-82 32630528-2 2020 The histidine to arginine substitution at position 6 of the Abeta sequence (H6R, English mutation) leads to an early onset of AD. Histidine 4-13 amyloid beta precursor protein Homo sapiens 60-65 31630339-1 2020 Alzheimer"s disease (AD) is related to the anomalous binding that occurs between amyloid-beta peptide (Abeta) and copper ion, through imidazole ring of histidine (His), as stated in the literature. Histidine 152-161 amyloid beta precursor protein Homo sapiens 103-108 31630339-1 2020 Alzheimer"s disease (AD) is related to the anomalous binding that occurs between amyloid-beta peptide (Abeta) and copper ion, through imidazole ring of histidine (His), as stated in the literature. Histidine 163-166 amyloid beta precursor protein Homo sapiens 103-108 32567070-8 2020 This "histidine trick" can be viewed as the Achilles" heel of Abeta in the fight against AD. Histidine 6-15 amyloid beta precursor protein Homo sapiens 62-67 32551634-2 2020 Mutation and histidine tautomerism are considered intrinsic origins in accumulation of Abeta. Histidine 13-22 amyloid beta precursor protein Homo sapiens 87-92 32255544-10 2020 These results allow us to elucidate the effect of DEPC modification on amyloidogenity of human Abeta and to speculate about the role of His residues in these processes. Histidine 136-139 amyloid beta precursor protein Homo sapiens 95-100 30813720-1 2019 As the intrinsic origin of the hypothesis for beta-amyloid (Abeta) from Alzheimer"s disease, histidine behaviors were found to play a crucial role in Abeta aggregation. Histidine 93-102 amyloid beta precursor protein Homo sapiens 46-66 31013069-4 2019 In isolated plaque cores, Cu(II) is bound to Abeta via histidine residues. Histidine 55-64 amyloid beta precursor protein Homo sapiens 45-50 30771375-2 2019 Despite the important role of histidine in stabilizing the fibrillar structure of the Abeta peptide at neutral pH, the effect of histidine tautomerism on Abeta peptide aggregation is still largely unknown. Histidine 30-39 amyloid beta precursor protein Homo sapiens 86-91 30771375-2 2019 Despite the important role of histidine in stabilizing the fibrillar structure of the Abeta peptide at neutral pH, the effect of histidine tautomerism on Abeta peptide aggregation is still largely unknown. Histidine 129-138 amyloid beta precursor protein Homo sapiens 154-159 30694660-6 2019 To this end, we studied the impact of widely used histidine to alanine mutations in amyloid-beta (Abeta). Histidine 50-59 amyloid beta precursor protein Homo sapiens 84-96 30694660-7 2019 We found that the secondary and tertiary contacts, salt bridge formations, and thermodynamic properties, as well as disorder propensities and aggregation predisposition of Abeta, are impacted by the single and triple point histidine to alanine mutations. Histidine 223-232 amyloid beta precursor protein Homo sapiens 172-177 29215101-1 2018 The extracellular domain E2 of the amyloid precursor protein (APP) features a His-rich metal-binding site (denoted as the M1 site). Histidine 78-81 amyloid beta precursor protein Homo sapiens 35-60 26118700-10 2015 Sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis and immunoblotting with anti-His antibody confirmed the identity of purified Abeta fusion protein and Abeta peptide. Histidine 96-99 amyloid beta precursor protein Homo sapiens 144-149 28096459-6 2017 We further demonstrate that the APP-C99 histidine residues His-6, His-13, and His-14 control the Zn2+-dependent APP-C99 dimerization and inhibition of Abeta production, whereas the increased Abeta43:Abeta40 ratio is substrate dimerization-independent and involves the known Zn2+ binding lysine Lys-28 residue that orientates the APP-C99 transmembrane domain within the lipid bilayer. Histidine 40-49 amyloid beta precursor protein Homo sapiens 151-156 28096459-6 2017 We further demonstrate that the APP-C99 histidine residues His-6, His-13, and His-14 control the Zn2+-dependent APP-C99 dimerization and inhibition of Abeta production, whereas the increased Abeta43:Abeta40 ratio is substrate dimerization-independent and involves the known Zn2+ binding lysine Lys-28 residue that orientates the APP-C99 transmembrane domain within the lipid bilayer. Histidine 59-62 amyloid beta precursor protein Homo sapiens 151-156 28096459-6 2017 We further demonstrate that the APP-C99 histidine residues His-6, His-13, and His-14 control the Zn2+-dependent APP-C99 dimerization and inhibition of Abeta production, whereas the increased Abeta43:Abeta40 ratio is substrate dimerization-independent and involves the known Zn2+ binding lysine Lys-28 residue that orientates the APP-C99 transmembrane domain within the lipid bilayer. Histidine 66-69 amyloid beta precursor protein Homo sapiens 151-156 28096459-6 2017 We further demonstrate that the APP-C99 histidine residues His-6, His-13, and His-14 control the Zn2+-dependent APP-C99 dimerization and inhibition of Abeta production, whereas the increased Abeta43:Abeta40 ratio is substrate dimerization-independent and involves the known Zn2+ binding lysine Lys-28 residue that orientates the APP-C99 transmembrane domain within the lipid bilayer. Histidine 66-69 amyloid beta precursor protein Homo sapiens 151-156 27687728-6 2016 We found that the H684R substitution within human Abeta, which replaces the histidine in the human protein with the arginine found at the corresponding position in mouse, facilitated beta" cleavage irrespective of the species origin of BACE1, thereby significantly increasing the level of Abeta(11-XX) and decreasing the level of Abeta(1-XX). Histidine 76-85 amyloid beta precursor protein Homo sapiens 50-55 28910862-7 2017 In addition, recombinant His-tagged Abeta42 was successfully expressed in Escherichia coli BL21 (DE3) and not only readily formed Abeta complexes, but also inhibited the proliferation of SH-SY5Y cells and E. coli. Histidine 25-28 amyloid beta precursor protein Homo sapiens 36-41 28682389-5 2017 Data suggest that the histidine needed to form the bis-histidine site in the low spin heme-Abeta complex is likely to be involved in the high affinity Cu binding site in the heme-Cu-Abeta complex. Histidine 22-31 amyloid beta precursor protein Homo sapiens 91-96 28682389-5 2017 Data suggest that the histidine needed to form the bis-histidine site in the low spin heme-Abeta complex is likely to be involved in the high affinity Cu binding site in the heme-Cu-Abeta complex. Histidine 22-31 amyloid beta precursor protein Homo sapiens 182-187 26252621-7 2015 The histidine residue binds heme, while the arginine and the tyrosine act as key second sphere residues of the heme-Abeta active site that play a crucial role in its reactivity. Histidine 4-13 amyloid beta precursor protein Homo sapiens 116-121 25969353-5 2015 The new Abeta construct expressed insoluble Abeta fused with an N-terminal histidine-tag connected by a linker harboring TEV protease cut site. Histidine 75-84 amyloid beta precursor protein Homo sapiens 8-13 25211009-2 2015 Recent studies show that heme binds to the His residue of Abeta with the iron center and subsequently forms an Abeta-heme complex, which can inhibit Abeta aggregation. Histidine 43-46 amyloid beta precursor protein Homo sapiens 58-63 25211009-2 2015 Recent studies show that heme binds to the His residue of Abeta with the iron center and subsequently forms an Abeta-heme complex, which can inhibit Abeta aggregation. Histidine 43-46 amyloid beta precursor protein Homo sapiens 111-116 25597800-1 2015 In this paper, a kind of gold nanoparticle (GNP)-based colorimetric assay has been developed for studying the reversible interaction of beta-amyloid peptide (Abeta) with Cu(2+) and Zn(2+), and quantitatively analyzing four inhibitors (i.e., EDTA, EGTA, histidine and clioquinol) of Cu(2+)/Zn(2+) induced Abeta assembly. Histidine 253-262 amyloid beta precursor protein Homo sapiens 136-156 25140899-5 2014 By modulating the amino acid sequence of alpha-synuclein at only two positions in which we introduced a pair of histidine residues found in Abeta, we created a chimeric alpha-synuclein/Abeta peptide with extended ganglioside-binding properties. Histidine 112-121 amyloid beta precursor protein Homo sapiens 140-145 25171714-0 2015 The histidine composition of the amyloid-beta domain, but not the E1 copper binding domain, modulates beta-secretase processing of amyloid-beta protein precursor in Alzheimer"s disease. Histidine 4-13 amyloid beta precursor protein Homo sapiens 33-45 25171714-0 2015 The histidine composition of the amyloid-beta domain, but not the E1 copper binding domain, modulates beta-secretase processing of amyloid-beta protein precursor in Alzheimer"s disease. Histidine 4-13 amyloid beta precursor protein Homo sapiens 131-143 25171714-2 2015 We have investigated the role of histidine residues within the extracellular E1 copper binding and Abeta domains of AbetaPP in its proteolysis. Histidine 33-42 amyloid beta precursor protein Homo sapiens 116-123 25171714-4 2015 Mutation of histidine 14 within the Abeta-domain specifically down-regulated beta-secretase processing without impacting on non-amyloidogenic proteolysis. Histidine 12-21 amyloid beta precursor protein Homo sapiens 36-41 25171714-5 2015 Understanding how histidine 14 participates in AbetaPP proteolysis may reveal new intervention points for AD treatments. Histidine 18-27 amyloid beta precursor protein Homo sapiens 47-54 25193696-4 2014 Our results indicated that both histidine residues (His(13), His(14)) in Abeta1-16 and free histidine enhanced the peroxidase activity of heme, hence His residues were essential in peroxidase activity of Abeta-heme complexes. Histidine 32-41 amyloid beta precursor protein Homo sapiens 73-78 25193696-4 2014 Our results indicated that both histidine residues (His(13), His(14)) in Abeta1-16 and free histidine enhanced the peroxidase activity of heme, hence His residues were essential in peroxidase activity of Abeta-heme complexes. Histidine 52-55 amyloid beta precursor protein Homo sapiens 73-78 25193696-4 2014 Our results indicated that both histidine residues (His(13), His(14)) in Abeta1-16 and free histidine enhanced the peroxidase activity of heme, hence His residues were essential in peroxidase activity of Abeta-heme complexes. Histidine 61-64 amyloid beta precursor protein Homo sapiens 73-78 25193696-4 2014 Our results indicated that both histidine residues (His(13), His(14)) in Abeta1-16 and free histidine enhanced the peroxidase activity of heme, hence His residues were essential in peroxidase activity of Abeta-heme complexes. Histidine 61-64 amyloid beta precursor protein Homo sapiens 73-78 25193696-8 2014 However, three of these residues (Arg(5), Tyr(10) and His(13)) identified in this study are all absent in rodents, where rodent Abeta-heme complex lacks peroxidase activity and it does not show AD, implicating the novel significance of these residues as well as human Abeta-heme peroxidase in the pathology of AD. Histidine 54-57 amyloid beta precursor protein Homo sapiens 128-133 25140899-5 2014 By modulating the amino acid sequence of alpha-synuclein at only two positions in which we introduced a pair of histidine residues found in Abeta, we created a chimeric alpha-synuclein/Abeta peptide with extended ganglioside-binding properties. Histidine 112-121 amyloid beta precursor protein Homo sapiens 185-190 24523414-7 2014 Both (13)C and (15)N SSNMR results show that Cu(+) coordinates to Abeta(1-40) fibrils primarily through the side chain Ndelta of both His-13 and His-14, suggesting major rearrangements from the Cu(2+) coordination via Nepsilon in the redox cycle. Histidine 134-137 amyloid beta precursor protein Homo sapiens 66-71 24858299-11 2014 At acidic pH (pH<6.5), ionic and hydrophobic interactions, created by histidine protonation and hydrophobic amino acids, appeared in the Abeta/HSPG binding. Histidine 73-82 amyloid beta precursor protein Homo sapiens 140-145 24523414-7 2014 Both (13)C and (15)N SSNMR results show that Cu(+) coordinates to Abeta(1-40) fibrils primarily through the side chain Ndelta of both His-13 and His-14, suggesting major rearrangements from the Cu(2+) coordination via Nepsilon in the redox cycle. Histidine 145-148 amyloid beta precursor protein Homo sapiens 66-71 24274576-1 2013 Recent evidence shows that metal coordination by amyloid beta peptides (Abeta) determines structural alterations of peptides, and His-13 from Abeta is crucial for Cu(2+) binding. Histidine 130-133 amyloid beta precursor protein Homo sapiens 142-147 24803226-5 2014 In addition to Abeta peptides starting with an Asp at position 1, a variety of different N-truncated Abeta peptides have been identified starting with amino residue Ala-2, pyroglutamylated Glu-3, Phe-4, Arg-5, His-6, Asp-7, Ser-8, Gly-9, Tyr-10 and pyroglutamylated Glu-11. Histidine 210-213 amyloid beta precursor protein Homo sapiens 101-106 24595206-5 2014 Here we show that our designed series of transition metal-functionalized POM derivatives with a defined histidine-chelated binding site have much better Abeta inhibition and peroxidase-like activity inhibition effects than the parent POM. Histidine 104-113 amyloid beta precursor protein Homo sapiens 153-158 23609990-4 2013 The structure demonstrates that Abeta residues 10-16, which are not in complex with the antibody, adopt a mixture of local polyproline II-helix and turn type conformations, enhancing cooperativity between the two adjacent histidine residues His13 and His14. Histidine 222-231 amyloid beta precursor protein Homo sapiens 32-37 24037720-8 2013 The Cu(2+) ligands in the most stable Cu(2+)-Abeta(1-16) structure involve Glu(3) , His(6) , His(13) and His(14) in terms of MM/3D-RISM (molecular mechanics/three-dimensional reference interaction site model). Histidine 84-87 amyloid beta precursor protein Homo sapiens 45-50 24037720-8 2013 The Cu(2+) ligands in the most stable Cu(2+)-Abeta(1-16) structure involve Glu(3) , His(6) , His(13) and His(14) in terms of MM/3D-RISM (molecular mechanics/three-dimensional reference interaction site model). Histidine 93-96 amyloid beta precursor protein Homo sapiens 45-50 24037720-8 2013 The Cu(2+) ligands in the most stable Cu(2+)-Abeta(1-16) structure involve Glu(3) , His(6) , His(13) and His(14) in terms of MM/3D-RISM (molecular mechanics/three-dimensional reference interaction site model). Histidine 93-96 amyloid beta precursor protein Homo sapiens 45-50 23289528-5 2013 Recent research has shown that heme binds preferentially to the His(13) residue of Abeta with the iron center, while the hydrophobic domain of Abeta is also able to bind to heme. Histidine 64-67 amyloid beta precursor protein Homo sapiens 83-88 23289528-5 2013 Recent research has shown that heme binds preferentially to the His(13) residue of Abeta with the iron center, while the hydrophobic domain of Abeta is also able to bind to heme. Histidine 64-67 amyloid beta precursor protein Homo sapiens 143-148 21491887-2 2011 At physiological pH, the Cu(II) coordination in Abeta is heterogeneous, and there exist at least two binding modes in which Cu(II) is coordinated by histidine residues. Histidine 149-158 amyloid beta precursor protein Homo sapiens 48-53 22558227-4 2012 Because the D7H mutant Abeta has an additional metal ion-coordinating residue, histidine, we speculate that this mutation may promote susceptibility of Abeta to ion. Histidine 79-88 amyloid beta precursor protein Homo sapiens 23-28 22558227-4 2012 Because the D7H mutant Abeta has an additional metal ion-coordinating residue, histidine, we speculate that this mutation may promote susceptibility of Abeta to ion. Histidine 79-88 amyloid beta precursor protein Homo sapiens 152-157 21341665-4 2011 Selective quenching observed in (13)C SSNMR of Cu(2+)-bound Abeta(1-40) suggested that primary Cu(2+) binding sites in Abeta(1-40) fibrils include N(epsilon) in His-13 and His-14 and carboxyl groups in Val-40 as well as in Glu sidechains (Glu-3, Glu-11, and/or Glu-22). Histidine 161-164 amyloid beta precursor protein Homo sapiens 60-65 21445432-3 2011 Proteins such as cytochrome c oxidase, a crucial enzyme in the respiratory chain, and beta-amyloid peptide, implicated in the pathology of Alzheimer"s disease, are examples of proteins containing histidines in their coordination sphere. Histidine 196-206 amyloid beta precursor protein Homo sapiens 86-106 20842634-12 2011 The mode of his-tag binding by C706 resembles the Abeta recognition by antibodies PFA1 and WO2. Histidine 12-15 amyloid beta precursor protein Homo sapiens 50-55 20842634-14 2011 By similarity, residues Phe-Arg-His of Abeta would be a major portion of the C706 epitope. Histidine 32-35 amyloid beta precursor protein Homo sapiens 39-44 21341665-4 2011 Selective quenching observed in (13)C SSNMR of Cu(2+)-bound Abeta(1-40) suggested that primary Cu(2+) binding sites in Abeta(1-40) fibrils include N(epsilon) in His-13 and His-14 and carboxyl groups in Val-40 as well as in Glu sidechains (Glu-3, Glu-11, and/or Glu-22). Histidine 172-175 amyloid beta precursor protein Homo sapiens 60-65 20061603-2 2010 While the mechanism(s) that modulate this toxicity are still widely debated, it has previously been demonstrated that modifications to the three histidine residues (6, 13, and 14) of Abeta are able to modulate the toxicity. Histidine 145-154 amyloid beta precursor protein Homo sapiens 183-188 19685013-4 2010 Here, we employed a mutant Abeta (Abeta H13R) in which a histidine residue was replaced by arginine. Histidine 57-66 amyloid beta precursor protein Homo sapiens 27-32 21187975-3 2010 The presence of the same consensus sequence, Val(12)-His-His-Gln(15), near the presumptive alpha-secretase cleavage site of the amyloid-beta (Abeta) peptide led us to hypothesize that NIa could possess activity against Abeta. Histidine 53-56 amyloid beta precursor protein Homo sapiens 142-147 21187975-3 2010 The presence of the same consensus sequence, Val(12)-His-His-Gln(15), near the presumptive alpha-secretase cleavage site of the amyloid-beta (Abeta) peptide led us to hypothesize that NIa could possess activity against Abeta. Histidine 53-56 amyloid beta precursor protein Homo sapiens 219-224 21187975-3 2010 The presence of the same consensus sequence, Val(12)-His-His-Gln(15), near the presumptive alpha-secretase cleavage site of the amyloid-beta (Abeta) peptide led us to hypothesize that NIa could possess activity against Abeta. Histidine 57-60 amyloid beta precursor protein Homo sapiens 142-147 21187975-3 2010 The presence of the same consensus sequence, Val(12)-His-His-Gln(15), near the presumptive alpha-secretase cleavage site of the amyloid-beta (Abeta) peptide led us to hypothesize that NIa could possess activity against Abeta. Histidine 57-60 amyloid beta precursor protein Homo sapiens 219-224 19685013-4 2010 Here, we employed a mutant Abeta (Abeta H13R) in which a histidine residue was replaced by arginine. Histidine 57-66 amyloid beta precursor protein Homo sapiens 34-39 20371992-7 2010 The Raman spectra demonstrate that three histidine residues in the N-terminal region of Abeta provide primary metal binding sites. Histidine 41-50 amyloid beta precursor protein Homo sapiens 88-93 19780898-2 2009 We found that a protein containing Asp-His-His-Cys (DHHC) domain, alcadein and APP interacting DHHC protein (AID)/DHHC-12, strongly inhibited APP metabolism, including amyloid beta-protein (Abeta) generation. Histidine 39-42 amyloid beta precursor protein Homo sapiens 190-195 18599641-7 2008 The novel distorted six-coordinated (3N3O) geometry around copper in the Abeta-Cu(2+) complexes include three histidines: glutamic, or/and aspartic acid, and axial water. Histidine 110-120 amyloid beta precursor protein Homo sapiens 73-78 19338344-8 2009 Electron paramagnetic resonance studies (EPR) with Abeta His/Ala analogues suggest a dynamic view of the tetragonal Cu(2+) complex, with axial as well as equatorial coordination of imidazole nitrogens creating an ensemble of coordination geometries in exchange between each other. Histidine 57-60 amyloid beta precursor protein Homo sapiens 51-56 18723589-2 2008 Peptide segments that include the characteristic histidine (His) diad, His(13) and His(14), efficiently block the Abeta channel activity, blocking Abeta cytotoxicity. Histidine 49-58 amyloid beta precursor protein Homo sapiens 114-119 18723589-2 2008 Peptide segments that include the characteristic histidine (His) diad, His(13) and His(14), efficiently block the Abeta channel activity, blocking Abeta cytotoxicity. Histidine 49-58 amyloid beta precursor protein Homo sapiens 147-152 18723589-2 2008 Peptide segments that include the characteristic histidine (His) diad, His(13) and His(14), efficiently block the Abeta channel activity, blocking Abeta cytotoxicity. Histidine 60-63 amyloid beta precursor protein Homo sapiens 114-119 18723589-2 2008 Peptide segments that include the characteristic histidine (His) diad, His(13) and His(14), efficiently block the Abeta channel activity, blocking Abeta cytotoxicity. Histidine 60-63 amyloid beta precursor protein Homo sapiens 147-152 18723589-2 2008 Peptide segments that include the characteristic histidine (His) diad, His(13) and His(14), efficiently block the Abeta channel activity, blocking Abeta cytotoxicity. Histidine 71-74 amyloid beta precursor protein Homo sapiens 114-119 18723589-2 2008 Peptide segments that include the characteristic histidine (His) diad, His(13) and His(14), efficiently block the Abeta channel activity, blocking Abeta cytotoxicity. Histidine 71-74 amyloid beta precursor protein Homo sapiens 147-152 18723589-2 2008 Peptide segments that include the characteristic histidine (His) diad, His(13) and His(14), efficiently block the Abeta channel activity, blocking Abeta cytotoxicity. Histidine 71-74 amyloid beta precursor protein Homo sapiens 114-119 18723589-2 2008 Peptide segments that include the characteristic histidine (His) diad, His(13) and His(14), efficiently block the Abeta channel activity, blocking Abeta cytotoxicity. Histidine 71-74 amyloid beta precursor protein Homo sapiens 147-152 18723589-3 2008 We hypothesize that the vicinal His-His peptides coordinate with the rings of His in the mouth of the pore, thus blocking the flow of calcium ions through the channel, with consequent blocking of Abeta cytotoxicity. Histidine 32-35 amyloid beta precursor protein Homo sapiens 196-201 18723589-3 2008 We hypothesize that the vicinal His-His peptides coordinate with the rings of His in the mouth of the pore, thus blocking the flow of calcium ions through the channel, with consequent blocking of Abeta cytotoxicity. Histidine 36-39 amyloid beta precursor protein Homo sapiens 196-201 18723589-3 2008 We hypothesize that the vicinal His-His peptides coordinate with the rings of His in the mouth of the pore, thus blocking the flow of calcium ions through the channel, with consequent blocking of Abeta cytotoxicity. Histidine 36-39 amyloid beta precursor protein Homo sapiens 196-201 18723589-7 2008 These data reinforce the premise that His residues within the Abeta channel sequence are in the pathway of ion flow. Histidine 38-41 amyloid beta precursor protein Homo sapiens 62-67 18847222-9 2008 In support of this, chemical modification of the Abeta peptide was examined using (1)H NMR, and specific oxidation sites within the peptide were identified at the histidine and methionine residues. Histidine 163-172 amyloid beta precursor protein Homo sapiens 49-54 16266835-6 2006 Perturbations in specific 1H NMR resonances between residues 6 and 14, and analysis of various Abeta analogues in which each of the three His residues have been replaced by alanine, indicates that His6, His13 and His14 residues are implicated in Zn-Abeta binding. Histidine 138-141 amyloid beta precursor protein Homo sapiens 249-254 17013614-0 2007 Ab initio modelling of the structure and redox behaviour of copper(I) bound to a His-His model peptide: relevance to the beta-amyloid peptide of Alzheimer"s disease. Histidine 81-84 amyloid beta precursor protein Homo sapiens 121-141 17106577-0 2006 Histidines 13 and 14 in the Abeta sequence are targets for inhibition of Alzheimer"s disease Abeta ion channel and cytotoxicity. Histidine 0-10 amyloid beta precursor protein Homo sapiens 28-33 17106577-4 2006 We found that the ability of peptides to block Abeta channel activity could be lost by replacement of histidines 13 and 14 by alanine or lysine. Histidine 102-112 amyloid beta precursor protein Homo sapiens 47-52 16271394-3 2005 The computed results based on a binuclear Cu complex predict that oxidation of cholesterol (yielding 4-cholesten-3-one as a specific product) proceeds at a slow rate when catalyzed by a Abeta/Cu(II) His- Cu(II)/Abeta) aggregate. Histidine 199-202 amyloid beta precursor protein Homo sapiens 186-191 16267663-0 2005 Ab initio model studies of copper binding to peptides containing a His-His sequence: relevance to the beta-amyloid peptide of Alzheimer"s disease. Histidine 67-70 amyloid beta precursor protein Homo sapiens 102-122 15964569-1 2005 The strong pH dependence of A beta oligomerization could arise from favorable intermolecular charge-charge interactions between His and carboxylate groups, or, alternatively, by mutual electrostatic repulsion of peptide molecules. Histidine 128-131 amyloid beta precursor protein Homo sapiens 28-34 15709480-4 2005 As revealed by atomic models of the Abeta protofilament, such as the nanotube beta-helix and parallel beta-sheet, the regular arrangement of histidines likely acts as a template for the end-to-end J-aggregation of CR molecules, which produces a red shift in UV/V is absorption. Histidine 141-151 amyloid beta precursor protein Homo sapiens 36-41 9516042-5 1998 We submit that histidine clusters, residing both in the Alzheimer"s beta-amyloid peptide and in most of the APP/APLP superfamily of proteins, constitute high-affinity binding sites for immobilized metal chelates. Histidine 15-24 amyloid beta precursor protein Homo sapiens 68-88 15263070-7 2004 A beta((1-40)) and A beta((1-42)) induced a redshift of 15-20 nm in the spectrum of heme-b and heme-a, suggesting that heme binds A beta, likely to one or more of the histidine residues. Histidine 167-176 amyloid beta precursor protein Homo sapiens 0-6 15263070-7 2004 A beta((1-40)) and A beta((1-42)) induced a redshift of 15-20 nm in the spectrum of heme-b and heme-a, suggesting that heme binds A beta, likely to one or more of the histidine residues. Histidine 167-176 amyloid beta precursor protein Homo sapiens 19-25 15263070-7 2004 A beta((1-40)) and A beta((1-42)) induced a redshift of 15-20 nm in the spectrum of heme-b and heme-a, suggesting that heme binds A beta, likely to one or more of the histidine residues. Histidine 167-176 amyloid beta precursor protein Homo sapiens 19-25 14978032-7 2004 Competition studies with glycine and l-histidine indicate that copper binds to Abeta-(1-28) at pH 7.4 with an affinity of K(a) approximately 10(7) m(-1). Histidine 37-48 amyloid beta precursor protein Homo sapiens 79-84 14978032-9 2004 Studies using analogues of Abeta-(1-28) in which each of the histidine residues have been replaced by alanine or in which the N terminus is acetylated suggest that the N terminus and His(13) are crucial for Cu(2+) binding and that His(6) and His(14) are also implicated. Histidine 61-70 amyloid beta precursor protein Homo sapiens 27-32 14978032-9 2004 Studies using analogues of Abeta-(1-28) in which each of the histidine residues have been replaced by alanine or in which the N terminus is acetylated suggest that the N terminus and His(13) are crucial for Cu(2+) binding and that His(6) and His(14) are also implicated. Histidine 183-186 amyloid beta precursor protein Homo sapiens 27-32 14978032-9 2004 Studies using analogues of Abeta-(1-28) in which each of the histidine residues have been replaced by alanine or in which the N terminus is acetylated suggest that the N terminus and His(13) are crucial for Cu(2+) binding and that His(6) and His(14) are also implicated. Histidine 231-234 amyloid beta precursor protein Homo sapiens 27-32 14978032-9 2004 Studies using analogues of Abeta-(1-28) in which each of the histidine residues have been replaced by alanine or in which the N terminus is acetylated suggest that the N terminus and His(13) are crucial for Cu(2+) binding and that His(6) and His(14) are also implicated. Histidine 231-234 amyloid beta precursor protein Homo sapiens 27-32 14717612-1 2004 We have previously reported that amyloid Abeta, the major component of senile plaques in Alzheimer"s disease (AD), binds Cu with high affinity via histidine and tyrosine residues [Atwood, C. S., et al. Histidine 147-156 amyloid beta precursor protein Homo sapiens 41-46 11274207-4 2001 Here we show that coordination of metal ions to Abeta is the same in both aqueous solution and lipid environments, with His(6), His(13), and His(14) all involved. Histidine 120-123 amyloid beta precursor protein Homo sapiens 48-53 11274207-4 2001 Here we show that coordination of metal ions to Abeta is the same in both aqueous solution and lipid environments, with His(6), His(13), and His(14) all involved. Histidine 128-131 amyloid beta precursor protein Homo sapiens 48-53 11274207-8 2001 These results suggest that metal binding to Abeta generated an allosterically ordered membrane-penetrating oligomer linked by superoxide dismutase-like bridging histidine residues. Histidine 161-170 amyloid beta precursor protein Homo sapiens 44-49 11029577-4 2000 Amyloid-beta peptide (Abeta) has a cluster of basic amino acids at the N-terminus (residues 13-16, His-His-Gln-Lys), which are considered critical for glycosaminoglycan interactions. Histidine 99-102 amyloid beta precursor protein Homo sapiens 22-27 11029577-4 2000 Amyloid-beta peptide (Abeta) has a cluster of basic amino acids at the N-terminus (residues 13-16, His-His-Gln-Lys), which are considered critical for glycosaminoglycan interactions. Histidine 103-106 amyloid beta precursor protein Homo sapiens 22-27 11029577-8 2000 The results demonstrate that the His-His-Gln-Lys region of Abeta, and in particular His13, is an important structural domain, as Ala substitution produces a dysfunctional folding mutant. Histidine 33-36 amyloid beta precursor protein Homo sapiens 59-64 11029577-8 2000 The results demonstrate that the His-His-Gln-Lys region of Abeta, and in particular His13, is an important structural domain, as Ala substitution produces a dysfunctional folding mutant. Histidine 37-40 amyloid beta precursor protein Homo sapiens 59-64 11019858-0 2000 Histidine residues underlie Congo red binding to A beta analogs. Histidine 0-9 amyloid beta precursor protein Homo sapiens 49-55 11019858-11 2000 That histidine residues underlie CR binding in A beta amyloid is consistent with previous findings that A beta peptides sediment as fibrillar assemblies at pH-3-7 and bind Congo red over the same pH range in aqueous medium. Histidine 5-14 amyloid beta precursor protein Homo sapiens 47-53 11019858-11 2000 That histidine residues underlie CR binding in A beta amyloid is consistent with previous findings that A beta peptides sediment as fibrillar assemblies at pH-3-7 and bind Congo red over the same pH range in aqueous medium. Histidine 5-14 amyloid beta precursor protein Homo sapiens 104-110 15693279-9 2000 Finally, the A beta peptide derived from the human sequence has a greater effect than the A beta peptide derived from the rat sequence, suggesting that histidine 13 may play a role in copper reduction. Histidine 152-161 amyloid beta precursor protein Homo sapiens 13-19 15693279-9 2000 Finally, the A beta peptide derived from the human sequence has a greater effect than the A beta peptide derived from the rat sequence, suggesting that histidine 13 may play a role in copper reduction. Histidine 152-161 amyloid beta precursor protein Homo sapiens 90-96 11580253-10 2001 Consistent with this idea, Abeta peptides containing Asp-->Asn or His-->Gln substitutions showed altered fibrillogenesis kinetics. Histidine 66-69 amyloid beta precursor protein Homo sapiens 27-32 10841784-4 2000 The Raman spectra clearly demonstrate that three histidine residues in the N-terminal hydrophilic region provide primary metal binding sites and the solubility of the metal-Abeta complex is correlated with the metal binding mode. Histidine 49-58 amyloid beta precursor protein Homo sapiens 173-178 10841784-9 2000 Under normal physiological conditions, Cu(II) is expected to protect Abeta against Zn(II)-induced aggregation by competing with Zn(II) for histidine residues of Abeta. Histidine 139-148 amyloid beta precursor protein Homo sapiens 69-74 10841784-9 2000 Under normal physiological conditions, Cu(II) is expected to protect Abeta against Zn(II)-induced aggregation by competing with Zn(II) for histidine residues of Abeta. Histidine 139-148 amyloid beta precursor protein Homo sapiens 161-166 10875439-3 2000 Human amyloid derived Abeta has an increased content of arginine (46%) and glutamate/glutamine residues (28%), but a decreased content of histidine residues (-32%) as compared to the expected amino acid content. Histidine 138-147 amyloid beta precursor protein Homo sapiens 22-27 10875439-6 2000 Our results suggest that the loss of histidine residues in human amyloid-derived Abeta may be a result of Cu oxidation, and that unidentified post-translational mechanisms operate to modify other amino acids of Abeta in vivo. Histidine 37-46 amyloid beta precursor protein Homo sapiens 81-86