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Ines Antunes Cardoso Pereira
AuthID:
R-000-63S
Publications
Confirmed
To Validate
Document Source:
All
Document Type:
All Document Types
Article (66)
Review (4)
Erratum (2)
Correction (1)
Editorial Material (1)
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Order:
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IF WOS Dsc
Cit. Scopus Dsc
IF Scopus Dsc
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Confirmed Publications: 74
41
TITLE:
The [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough is a bacterial lipoprotein lacking a typical lipoprotein signal peptide
Full Text
AUTHORS:
Filipa M A Valente
;
Patricia M Pereira
;
Sofia S Venceslau
; Manuela Regalla;
Ana V Coelho
;
Ines A C Pereira
;
PUBLISHED:
2007
,
SOURCE:
FEBS LETTERS,
VOLUME:
581,
ISSUE:
18
INDEXED IN:
Scopus
WOS
CrossRef
IN MY:
ORCID
|
ResearcherID
42
TITLE:
Characterization of the Desulfovibrio desulfuricans ATCC 27774 DsrMKJOP complex - A membrane-bound redox complex involved in the sulfate respiratory pathway
Full Text
AUTHORS:
Pires, RH
;
Venceslau, SS
;
Morais, F
;
Teixeira, M
;
Xavier, AV
;
Pereira, IAC
;
PUBLISHED:
2006
,
SOURCE:
BIOCHEMISTRY,
VOLUME:
45,
ISSUE:
1
INDEXED IN:
Scopus
WOS
CrossRef
IN MY:
ORCID
|
ResearcherID
43
TITLE:
Crystallization and preliminary structure determination of the membrane-bound complex cytochrome c nitrite reductase from Desulfovibrio vulgaris Hildenborough
Full Text
AUTHORS:
Rodrigues, ML
;
Oliveira, T
;
Matias, PM
;
Martins, IC
;
Valente, FMA
;
Pereira, IAC
;
Archer, M
;
PUBLISHED:
2006
,
SOURCE:
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS,
VOLUME:
62,
ISSUE:
6
INDEXED IN:
Scopus
WOS
CrossRef
IN MY:
ORCID
|
ResearcherID
44
TITLE:
Resonance Raman fingerprinting of multiheme cytochromes from the cytochrome c(3) family
Full Text
AUTHORS:
Di Paolo, RE
;
Pereira, PM
;
Gomes, I
;
Valente, FMA
;
Pereira, IAC
;
Franco, R
;
PUBLISHED:
2006
,
SOURCE:
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY,
VOLUME:
11,
ISSUE:
2
INDEXED IN:
Scopus
WOS
CrossRef
IN MY:
ORCID
|
ResearcherID
45
TITLE:
Selenium is involved in regulation of periplasmic hydrogenase gene expression in Desulfovibrio vulgaris Hildenborough
AUTHORS:
Valente, FAA; Almeida, CC; Pacheco, I; Carita, J;
Saraiva, LM
;
Pereira, IAC
;
PUBLISHED:
2006
,
SOURCE:
JOURNAL OF BACTERIOLOGY,
VOLUME:
188,
ISSUE:
9
INDEXED IN:
Scopus
WOS
CrossRef
Handle
IN MY:
ORCID
46
TITLE:
Spectroelectrochemistry of type II cytochrome c3 on a glycosylated self-assembled monolayer
Full Text
AUTHORS:
Ines Gomes
;
Roberto E Di Paolo
;
Patricia M Pereira
;
Ines A C Pereira
;
Ligia M Saraiva
; Soledad Penades;
Ricardo Franco
;
PUBLISHED:
2006
,
SOURCE:
LANGMUIR,
VOLUME:
22,
ISSUE:
24
INDEXED IN:
Scopus
WOS
CrossRef
:
5
IN MY:
ORCID
|
ResearcherID
47
TITLE:
The Tmc complex from Desulfovibrio vulgaris hildenborough is involved in transmembrane electron transfer from periplasmic hydrogen oxidation
Full Text
AUTHORS:
Patricia M Pereira
;
Miguel Teixeira
;
Antonio V Xavier
;
Ricardo O Louro
;
Ines A C Pereira
;
PUBLISHED:
2006
,
SOURCE:
BIOCHEMISTRY,
VOLUME:
45,
ISSUE:
34
INDEXED IN:
Scopus
WOS
CrossRef
IN MY:
ORCID
|
ResearcherID
48
TITLE:
X-ray structure of the membrane-bound cytochrome c quinol dehydrogenase NrfH reveals novel haem coordination
AUTHORS:
Maria Luisa Rodrigues
;
Tania F Oliveira
;
Ines A C Pereira
;
Margarida Archer
;
PUBLISHED:
2006
,
SOURCE:
EMBO JOURNAL,
VOLUME:
25,
ISSUE:
24
INDEXED IN:
Scopus
WOS
CrossRef
IN MY:
ORCID
|
ResearcherID
49
TITLE:
Hydrogenases in Desulfovibrio vulgaris Hildenborough: structural and physiologic characterisation of the membrane-bound [NiFeSe] hydrogenase
Full Text
AUTHORS:
Valente, FMA
;
Oliveira, ASF
;
Gnadt, N
; Pacheco, I;
Coelho, AV
;
Xavier, AV
;
Teixeira, M
;
Soares, CM
;
Pereira, IAC
;
PUBLISHED:
2005
,
SOURCE:
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY,
VOLUME:
10,
ISSUE:
6
INDEXED IN:
Scopus
WOS
CrossRef
IN MY:
ORCID
|
ResearcherID
50
TITLE:
Sulphate respiration from hydrogen in Desulfovibrio bacteria: a structural biology overview
Full Text
AUTHORS:
Matias, PM
;
Pereira, IAC
;
Soares, CM
;
Carrondo, MA
;
PUBLISHED:
2005
,
SOURCE:
PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY,
VOLUME:
89,
ISSUE:
3
INDEXED IN:
Scopus
WOS
IN MY:
ORCID
|
ResearcherID
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