P1889
SOD1 and amyotrophic lateral sclerosis: mutations and oligomerizationAn electron-transfer path through an extended disulfide relay system: the case of the redox protein ALRMolecular chaperone function of Mia40 triggers consecutive induced folding steps of the substrate in mitochondrial protein importStructural interplay between calcium(II) and copper(II) binding to S100A13 proteinMIA40 is an oxidoreductase that catalyzes oxidative protein folding in mitochondriaSolution structure and dynamics of S100A5 in the apo and Ca2+-bound statesAn NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes proteinA hint for the function of human Sco1 from different structuresSolution structure of the B form of oxidized rat microsomal cytochrome b5 and backbone dynamics via 15N rotating-frame NMR-relaxation measurements. Biological implicationsThe crystal structure of the monomeric human SOD mutant F50E/G51E/E133Q at atomic resolution. The enzyme mechanism revisitedThe solution structure of oxidized Escherichia coli cytochrome b562Solution structure of reduced horse heart cytochrome cA proton-NMR investigation of the fully reduced cytochrome c7 from Desulfuromonas acetoxidans. Comparison between the reduced and the oxidized formsThe solution structure of a monomeric, reduced form of human copper,zinc superoxide dismutase bearing the same charge as the native proteinSolution structure of oxidized microsomal rabbit cytochrome b5. Factors determining the heterogeneous binding of the hemeHigh resolution solution structure of the protein part of Cu7 metallothioneinStructural consequences of b- to c-type heme conversion in oxidized Escherichia coli cytochrome b562Solution structure of the yeast copper transporter domain Ccc2a in the apo and Cu(I)-loaded statesSolution structure of the Cu(I) and apo forms of the yeast metallochaperone, Atx1The first solution structure of a paramagnetic copper(II) protein: the case of oxidized plastocyanin from the cyanobacterium Synechocystis PCC6803Dimethyl propionate ester heme-containing cytochrome b5: structure and stabilityEffects of extrinsic imidazole ligation on the molecular and electronic structure of cytochrome cBackbone dynamics of plastocyanin in both oxidation states. Solution structure of the reduced form and comparison with the oxidized stateParamagnetism-based versus classical constraints: an analysis of the solution structure of Ca Ln calbindin D9kA quick solution structure determination of the fully oxidized double mutant K9-10A cytochrome c7 from Desulfuromonas acetoxidans and mechanistic implicationsNMR solution structure, backbone mobility, and homology modeling of c-type cytochromes from gram-positive bacteriaSolution structure of the unbound, oxidized Photosystem I subunit PsaC, containing [4Fe-4S] clusters F(A) and F(B): a conformational change occurs upon binding to photosystem IThe solution structure of reduced dimeric copper zinc superoxide dismutase. The structural effects of dimerizationThe metal reductase activity of some multiheme cytochromes c: NMR structural characterization of the reduction of chromium(VI) to chromium(III) by cytochrome c(7).Structure and dynamics of copper-free SOD: The protein before binding copperSolution structure of CopC: a cupredoxin-like protein involved in copper homeostasisA new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118)Solution structure and characterization of the heme chaperone CcmEStructure and dynamics of reduced Bacillus pasteurii cytochrome c: oxidation state dependent properties and implications for electron transfer processesStructural model for an alkaline form of ferricytochrome CA redox switch in CopC: An intriguing copper trafficking protein that binds copper(I) and copper(II) at different sitesHuman Sco1 functional studies and pathological implications of the P174L mutantA strategy for the NMR characterization of type II copper(II) proteins: the case of the copper trafficking protein CopC from Pseudomonas SyringaeX-ray structures of binary and ternary enzyme-product-inhibitor complexes of matrix metalloproteinasesA core mutation affecting the folding properties of a soluble domain of the ATPase protein CopA from Bacillus subtilis
P50
Q21090100-1157D769-B5D8-4648-B898-9B1923527D90Q24301115-1C2B240A-4E03-4799-8FFA-AA5F06BCD6E2Q24306303-780DE2C5-8FEC-4E1A-A593-F4FC127275C4Q24321123-A6D20BCB-137E-4B37-A34A-C5E926AFAC75Q24324109-28886BE9-84BD-42CA-9690-B26B6650F820Q24338739-08B09E81-F611-4D57-95A7-1084B50883A4Q24338842-1C43F3B5-97AB-42C7-A448-B0F7BCB4001EQ24548538-DEFDC320-24E9-4A38-90F1-C6C9C6382544Q27617771-36F6EF90-4DDD-4740-A62A-A6171F1E6D9EQ27618186-BAE9D48C-051A-42D3-A36C-A79AB1305C70Q27618942-9CD220E1-29F5-427C-A145-CE7210D9AFC4Q27619745-12D76A6D-D980-409B-8221-6B996DC51D07Q27620382-0BD7E420-01E1-40E2-9CC4-25DB8134C213Q27620947-AC0E219A-F40F-45DA-BF57-57B9C81B5F53Q27621113-B1574EEE-4E9C-4E45-95A2-15E1962DD81FQ27621330-A196E6B5-EA1F-4CB0-887C-C60AB68B94BBQ27621510-326C4F91-A7B8-426C-9057-0E87F6E3096EQ27628454-B13C8250-9F2C-49FC-98A4-435DE04B69E4Q27631460-55EAA73C-C1D7-49EF-9769-9B78E2DCA30BQ27633313-75E95728-43E3-4E33-8531-00D826950F33Q27633621-744E8037-2458-46CC-A899-C54484C5E8B7Q27633628-4AB42E10-D3F7-4AB9-A086-84A0C7FE8FB6Q27634152-A92647D5-4474-420C-A094-B93DEBEDF4A2Q27636498-4F71D224-1F48-4443-8FC3-1CE372819516Q27638211-64D60CA2-4D81-4832-8D66-749375AA66F9Q27638732-6C5191B4-74B0-43EC-ACA5-8F908A752B4BQ27638821-0BC7FD26-F47B-4427-B08B-45D051A2FD99Q27638847-4B790683-BDAC-44BD-95FD-9270A96FCBA0Q27639360-81CF22D5-1FA0-4F8A-A3B0-F8F46A6FA529Q27639669-4538D911-7BDA-4CDC-9136-D63A5516956EQ27639769-8AA473DC-CC1B-454F-853C-57214C0E941EQ27639912-DED1561A-2263-40E7-9D44-3496A56284B8Q27639941-8929D4BF-6EE5-4A17-B41F-EF86F840AD5BQ27640328-198B7C0B-D997-4A8D-9F15-9FD0F650C148Q27640621-D88E1A06-77CF-476A-8C1F-8AD29A56EEFAQ27640760-3FD1010F-E57C-4E77-901C-14285463C035Q27640878-F88F4820-38C3-4C25-B8BE-4D74E7761087Q27641422-88D4604D-C693-4B68-A945-299B36D2BB24Q27641449-487BF280-644C-4C9D-A044-306DD84D405EQ27641755-58C7BEC3-625D-4D91-B304-A844DAAA99D9
P50
description
Itaalia keemik
@et
Italiaans scheikundige (1940-2012)
@nl
Italian chemist
@en
Italian chemist
@en-ca
Italian chemist
@en-gb
ceimiceoir Iodálach
@ga
chimico italiano
@it
chimist italian
@ro
chimiste italien
@fr
italienischer Chemiker
@de
name
Ivano Bertini
@ast
Ivano Bertini
@ca
Ivano Bertini
@da
Ivano Bertini
@de
Ivano Bertini
@en
Ivano Bertini
@es
Ivano Bertini
@fr
Ivano Bertini
@ga
Ivano Bertini
@it
Ivano Bertini
@nb
type
label
Ivano Bertini
@ast
Ivano Bertini
@ca
Ivano Bertini
@da
Ivano Bertini
@de
Ivano Bertini
@en
Ivano Bertini
@es
Ivano Bertini
@fr
Ivano Bertini
@ga
Ivano Bertini
@it
Ivano Bertini
@nb
prefLabel
Ivano Bertini
@ast
Ivano Bertini
@ca
Ivano Bertini
@da
Ivano Bertini
@de
Ivano Bertini
@en
Ivano Bertini
@es
Ivano Bertini
@fr
Ivano Bertini
@ga
Ivano Bertini
@it
Ivano Bertini
@nb
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