2021 

124. Hypercholesterolemia and 27-hydroxycholesterol increase S100A8 and RAGE expression in the brain: a link between cholesterol, alarmins and neurodegeneration
Loera-Valencia, R., Muhammad-Al-Mustafa, I., Goikolea, J., Lodeiro, M., Mateos, L., Björkhem, I. Puerta, E., Romão M.A., Gomes, C.M., Merino-Serrais, P., Maioli, S., Cedazo-Minguez, A. 
Molecular Neurobiology (2021) accepted/in press

123. Computational analysis of the interactions between the S100B extracellular chaperone and its amyloid β peptide client
Rodrigues, F.E.P., Figueira, A.J., Gomes, C.M., Machuqueiro, M. 
Int J Mol Sci (2021) 22(7), 3629
https://doi.org/10.3390/ijms22073629

122. Targeting S100B with Peptides Encoding Intrinsic Aggregation-Prone Sequence Segments
Cristóvão, J.S., Romão, M.A., Gallardo, R., Schymkowitz, J., Rousseau, F., Gomes, C.M.
Molecules (2021) 
https://doi.org/10.3390/molecules26020440

121. Electron transfer flavoprotein and its role in mitochondrial energy metabolism in health and disease 
Henriques, B.J.,  Olsen, R., Gomes, C.M:, Bross, P. 
Gene (2021) 
https://doi.org/10.1016/j.gene.2021.145407

2020

120. Cu(II)-binding to S100B triggers polymerization of disulfide cross-linked tetramers with enhanced chaperone activity against amyloid-β aggregation.
Cristóvão, J. S., Moreira, G. G., Rodrigues, F. E. P., Carapeto, A. P., Rodrigues, M. S., Cardoso, I., Ferreira, A. E., Machuqueiro, M., Fritz, G. & Gomes, C. M.
Chemical Communications (2020).
 https://doi.org/10.1039/D0CC06842J

119. MIRRAGGE – Minimum Information Required for Reproducible AGGregation Experiments.
Martins, P. M. et al.
Frontiers in Molecular Neuroscience (2020). 13. 
 https://doi.org/10.3389/fnmol.2020.582488 

118. The S100B alarmin is a dual-function chaperone suppressing Aβ oligomerization through combined zinc chelation and inhibition of protein aggregation
Cristóvão, J. S., Figueira, A. J., Carapeto, A., Rodrigues, M. S., Cardoso, I., and Gomes, C. M. 
ACS chemical neuroscience (2020)
 https://doi.org/10.1021/acschemneuro.0c00392

117. Glucosylpolyphenols as Inhibitors of Aβ-Induced Fyn Kinase Activation and Tau Phosphorylation: Synthesis, Membrane Permeability, and Exploratory Target Assessment within the Scope of Type 2 Diabetes and Alzheimer’s Disease.
de Matos, A. M. et al.
Journal of Medicinal Chemistry (2020). 63, 11663Z-11690.
 https://doi.org/10.1021/acs.jmedchem.0c00841 

116. Functional Recovery of a GCDH Variant Associated to Severe Deflavinylation-Molecular Insights into Potential Beneficial Effects of Riboflavin Supplementation in Glutaric Aciduria-Type I Patients.
Ribeiro, J. V., Gomes, C. M. & Henriques, B. J.
Int J Mol Sci (2020). 21.
https://doi.org/10.3390/ijms21197063

115. Potential complementation effects of two disease-associated mutations in tetrameric glutaryl-CoA dehydrogenase is due to inter subunit stability-activity counterbalance.
Ribeiro, J. V., Lucas, T. G., Bross, P., Gomes, C. M. & Henriques, B. J.
Biochimica et biophysica acta. Proteins and proteomics (2020). 1868, 140269. https://doi.org/10.1016/j.bbapap.2019.140269

114. Conformational analysis of the riboflavin-responsive ETF:QO-p.Pro456Leu variant associated with mild multiple acyl-CoA dehydrogenase deficiency.
Lucas, T. G., Henriques, B. J. & Gomes, C. M.
Biochimica et biophysica acta. Proteins and proteomics (2020). 1868, 140393. https://doi.org/10.1016/j.bbapap.2020.140393

2019

113. Identification of temperature-sensitive mutations and characterization of thermolabile RNase II variants.
Reis, F. P., Barria, C., Gomez-Puertas, P., Gomes, C. M. & Arraiano, C. M.
FEBS Lett (2019). 593, 352-360. https://doi.org/10.1002/1873-3468.13313

112. Zinc Binding to Tau Influences Aggregation Kinetics and Oligomer Distribution.
Moreira, G. G., Cristovao, J. S., Torres, V. M., Carapeto, A. P., Rodrigues, M. S., Landrieu, I., Cordeiro, C. & Gomes, C. M.
Int J Mol Sci (2019). 20. https://doi.org/10.3390/ijms20235979

111. Molecular and Clinical Investigations on Portuguese Patients with Multiple acyl-CoA Dehydrogenase Deficiency.
Henriques, B. J., Lucas, T. G., Martins, E., Gaspar, A., Bandeira, A., Nogueira, C., Brandao, O., Rocha, H., Vilarinho, L. & Gomes, C. M.
Current molecular medicine (2019). 19, 487-493. https://doi.org/10.2174/1566524019666190507114748

110. Distribution and Relative Abundance of S100 Proteins in the Brain of the APP23 Alzheimer’s Disease Model Mice.
Hagmeyer, S., Romão, M. A., Cristóvão, J. S., Vilella, A., Zoli, M., Gomes, C. M. & Grabrucker, A. M.
Frontiers in Neuroscience (2019). 13. https://doi.org/10.3389/fnins.2019.00640

109. S100 Proteins in Alzheimer’s Disease.
Cristóvão, J. S. & Gomes, C. M.
Frontiers in Neuroscience (2019). 13. https://doi.org/10.3389/fnins.2019.00463

2018

108. Impaired oligodendrogenesis and myelination by elevated S100B levels during neurodevelopment.
Santos, G., Barateiro, A., Gomes, C.M., Brites, D., Fernandes, A.
Neuropharmacology (2018). 129, 69-83. https://doi.org/https://doi.org/10.1016/j.neuropharm.2017.11.002

107. Zinc binding to S100B affords regulation of trace metal homeostasis and excitotoxicity in the brain.
Hagmeyer, S., Cristóvão, J.S., Mulvihill, J.J., Boeckers, T.M., Gomes, C.M., Grabrucker, A.M. .
Frontiers in Molecular Neuroscience (2018). 10. https://doi.org/https://doi.org/0.3389/fnmol.2017.00456

106. The neuronal S100B protein is a calcium-tuned suppressor of amyloid-β aggregation.
Cristóvão, J. S., Morris, V.K., Cardoso, I., Leal, S.S., Martínez, J., Botelho, H.M., Göbl, C., David, R., Kierdorf, K., Alemi, M., Madl. T., Fritz, G., Reif, B., Gomes, C.M.
Science Advances (2018). 4, eaaq1702. https://doi.org/https://doi.org/10.1126/sciadv.aaq1702

2017 

105. Synthesis and effects of flavonoid structure variation on amyloid-β aggregation.
Matos, A. M., Cristóvão, J.S., Yashunsky, D.V., Nifantiev, N.E., Viana, A.S., Gomes, C.M., Rauter, A.P.
Pure and Applied Chemistry (2017). 89. https://doi.org/https://doi.org/10.1515/pac-2017-0201

104. Characterization of plasma labile heme in hemolytic conditions.
Gouveia, Z., Carlos, A.R., Yuan, X., Aires-da-Silva, F., Stocker, R., Maghzal, G.J., Leal, S.S., Gomes, C.M., Todorovic, S., Iranzo, O., Ramos, S., Santos, A.C., Hamza, I., Gonçalves, J., Soares, M.P.
FEBS Journal (2017). 284, 3278-3301. https://doi.org/https://doi.org/10.1111/febs.14192

2016

103. Evidence for synergistic action of transthyretin and IGF-I over the IGF-I receptor.
Vieira, M., Leal, S. S., Gomes, C. M. & Saraiva, M. J.
Biochim Biophys Acta (2016). 1862, 797-804. https://doi.org/10.1016/j.bbadis.2016.01.008

102. Free Superoxide is an Intermediate in the Production of H2O2 by Copper(I)-Abeta Peptide and O2.
Reybier, K., Ayala, S., Alies, B., Rodrigues, J. V., Bustos Rodriguez, S., La Penna, G., Collin, F., Gomes, C. M., Hureau, C. & Faller, P.
Angewandte Chemie (International ed. in English) (2016). 55, 1085-1089. https://doi.org/10.1002/anie.201508597

101. Therapeutic Approaches Using Riboflavin in Mitochondrial Energy Metabolism Disorders.
Henriques, B. J., Lucas, T. G. & Gomes, C. M.
Current drug targets (2016). 17, 1527-1534

100. Metals and Neuronal Metal Binding Proteins Implicated in Alzheimer's Disease.
Cristovao, J. S., Santos, R. & Gomes, C. M.
Oxid Med Cell Longev (2016). 2016, 9812178. https://doi.org/10.1155/2016/9812178

98. Metallothioneins in Prion- and Amyloid-Related Diseases.
Adam, P., Krizkova, S., Heger, Z., Babula, P., Pekarik, V., Vaculovicoa, M., Gomes, C. M., Kizek, R. & Adam, V.
Journal of Alzheimer's disease : JAD (2016). 51, 637-656. https://doi.org/10.3233/JAD-150984
2015

2015

97. Calcium dysregulation links ALS defective proteins and motor neuron selective vulnerability.
Leal, S. S. & Gomes, C. M.
Frontiers in cellular neuroscience (2015). 9, 225. https://doi.org/10.3389/fncel.2015.00225

96. Aberrant zinc binding to immature conformers of metal-free copper-zinc superoxide dismutase triggers amorphous aggregation.
Leal, S. S., Cristovao, J. S., Biesemeier, A., Cardoso, I. & Gomes, C. M.
Metallomics (2015). 7, 333-346. https://doi.org/10.1039/c4mt00278d

95. Calcium binding to gatekeeper residues flanking aggregation-prone segments underlies non-fibrillar amyloid traits in superoxide dismutase 1 (SOD1).
Estacio, S. G., Leal, S. S., Cristovao, J. S., Faisca, P. F. & Gomes, C. M.
Biochim Biophys Acta (2015). 1854, 118-126. https://doi.org/10.1016/j.bbapap.2014.11.005

94. On the hunt for truly biocompatible ionic liquids for lipase-catalyzed reactions.
Deive, F. J., Ruivo, D., Rodrigues, J. V., Gomes, C. M., Sanroman, M. A., Rebelo, L. P. N., Esperanca, J. M. S. S. & Rodriguez, A.
RSC Advances (2015). 5, 3386-3389. https://doi.org/10.1039/c4ra15021j

2014

93. Structural-functional evaluation of ionic liquid libraries for the design of co-solvents in lipase-catalysed reactions.
Rodrigues, J. V., Ruivo, D., Rodriguez, A., Deive, F. J., Esperanca, J. M., Marrucho, I. M., Gomes, C. M. & Rebelo, L. P. N.
Green Chemistry (2014). https://doi.org/10.1039/c4gc01329h

92. Ethylmalonic Encephalopathy ETHE1 R163W/R163Q Mutations Alter Protein Stability and Redox Properties of the Iron Centre.
Henriques, B. J., Lucas, T. G., Rodrigues, J. V., Frederiksen, J. H., Teixeira, M. S., Tiranti, V., Bross, P. & Gomes, C. M.
PloS one (2014). 9, e107157. https://doi.org/10.1371/journal.pone.0107157

91. A Conserved Cysteine Residue of Bacillus subtilis SpoIIIJ Is Important for Endospore Development.
Corte, L., Valente, F., Serrano, M., Gomes, C. M., Moran, C. P., Jr. & Henriques, A. O.
PloS one (2014). 9, e99811. https://doi.org/10.1371/journal.pone.0099811

90. Probing the kinetic stabilities of Friedreich's ataxia clinical variants using a solid phase GroEL chaperonin capture platform.
Correia, A. R., Naik, S., Fisher, M. T. & Gomes, C. M.
Biomolecules (2014). 4, 956-979. https://doi.org/10.3390/biom4040956

2013

89. Calcium Ions Promote Superoxide Dismutase 1 (SOD1) Aggregation into Non-fibrillar Amyloid: A link to toxic effects of Calcium overload in ALS?
Leal, S. S., Cardoso, I., Valentine, J. S. & Gomes, C. M.
J Biol Chem (2013). 288, 25219-25228. https://doi.org/10.1074/jbc.M113.470740

88. Neurodegeneration in Friedreich's Ataxia: From Defective Frataxin to Oxidative Stress.
Gomes, C. M. & Santos, R.
Oxid Med Cell Longev (2013). 2013, 487534. https://doi.org/10.1155/2013/487534

87. Revertants, Low Temperature, and Correctors Reveal the Mechanism of F508del-CFTR Rescue by VX-809 and Suggest Multiple Agents for Full Correction.
Farinha, C. M., King-Underwood, J., Sousa, M., Correia, A. R., Henriques, B. J., Roxo-Rosa, M., Da Paula, A. C., Williams, J., Hirst, S., Gomes, C. M. & Amaral, M. D.
Chemistry & biology (2013). 20, 943-955. https://doi.org/10.1016/j.chembiol.2013.06.004

86. Small molecules present in the cerebrospinal fluid metabolome influence superoxide dismutase 1 aggregation.
Cristovao, J. S., Leal, S. S., Cardoso, I. & Gomes, C. M.
Int J Mol Sci (2013). 14, 19128-19145. https://doi.org/10.3390/ijms140919128

85. Intrinsically Disordered and Aggregation Prone Regions Underlie beta-Aggregation in S100 Proteins.
Carvalho, S. B., Botelho, H. M., Leal, S. S., Cardoso, I., Fritz, G. & Gomes, C. M.
PloS one (2013). 8, e76629. https://doi.org/10.1371/journal.pone.0076629

2012

84. The sulfur oxygenase reductase from the mesophilic bacterium Halothiobacillus neapolitanus is a highly active thermozyme.
Veith, A., Botelho, H. M., Kindinger, F., Gomes, C. M. & Kletzin, A.
Journal of bacteriology (2012). 194, 677-685. https://doi.org/10.1128/JB.06531-11

83. Protein folding modulates the swapped dimerization mechanism of methyl-accepting chemotaxis heme sensors.
Silva, M. A., Lucas, T. G., Salgueiro, C. A. & Gomes, C. M.
PloS one (2012). 7, e46328. https://doi.org/10.1371/journal.pone.0046328

82. Cofactors and metabolites as protein folding helpers in metabolic diseases.
Rodrigues, J. V., Henriques, B. J., Lucas, T. G. & Gomes, C. M.
Curr Top Med Chem (2012). 12, 2546-2559. https://doi.org/http://dx.doi.org/10.2174/1568026611212220009

81. Mechanism of superoxide and hydrogen peroxide generation by human electron-transfer flavoprotein and pathological variants.
Rodrigues, J. V. & Gomes, C. M.
Free radical biology & medicine (2012). 53, 12-19. https://doi.org/10.1016/j.freeradbiomed.2012.04.016

80. Metal ions as modulators of protein conformation and misfolding in neurodegeneration.
Leal, S. S., Botelho, H. M. & Gomes, C. M.
Coordination Chemistry Reviews (2012). 256, 2253-2270. https://doi.org/10.1016/j.ccr.2012.04.004

79. Protein misfolding in disease and small molecule therapies.
Gomes, C. M.
Curr Top Med Chem (2012). 12, 2460-2469. https://doi.org/http://dx.doi.org/10.2174/1568026611212220002

78. S100A6 Amyloid Fibril Formation Is Calcium-modulated and Enhances Superoxide Dismutase-1 (SOD1) Aggregation.
Botelho, H. M., Leal, S. S., Cardoso, I., Yanamandra, K., Morozova-Roche, L. A., Fritz, G. & Gomes, C. M.
J Biol Chem (2012). 287, 42233-42242. https://doi.org/10.1074/jbc.M112.396416

77. Mutations at the flavin binding site of ETF:QO yield a MADD-like severe phenotype in Drosophila.
Alves, E., Henriques, B. J., Rodrigues, J. V., Prudencio, P., Rocha, H., Vilarinho, L., Martinho, R. G. & Gomes, C. M.
Biochim Biophys Acta (2012). 1822, 1284-1292. https://doi.org/10.1016/j.bbadis.2012.05.003

2011

76. Protein stability in an ionic liquid milieu: on the use of differential scanning fluorimetry.
Rodrigues, J. V., Prosinecki, V., Marrucho, I., Rebelo, L. P. & Gomes, C. M.
Physical chemistry chemical physics : PCCP (2011). 13, 13614-13616. https://doi.org/10.1039/c1cp21187k

75. Cofactors and metabolites as potential stabilizers of mitochondrial acyl-CoA dehydrogenases.
Lucas, T. G., Henriques, B. J., Rodrigues, J. V., Bross, P., Gregersen, N. & Gomes, C. M.
Biochim Biophys Acta (2011). 1812, 1658-1663. https://doi.org/10.1016/j.bbadis.2011.09.009

74. A polymorphic position in electron transfer flavoprotein modulates kinetic stability as evidenced by thermal stress.
Henriques, B. J., Fisher, M. T., Bross, P. & Gomes, C. M.
FEBS Lett (2011). 585, 505-510. https://doi.org/10.1016/j.febslet.2011.01.002

73. Structural reorganization renders enhanced metalloprotein stability.
Botelho, H. M. & Gomes, C. M.
Chem Commun (Camb) (2011). 47, 11149-11151. https://doi.org/10.1039/c1cc13354c

2010

72. Enhanced superoxide and hydrogen peroxide detection in biological assays.
Rodrigues, J. V. & Gomes, C. M.
Free radical biology & medicine (2010). 49, 61-66

71. Structural requirements for VAP-B oligomerization and their implication in amyotrophic lateral sclerosis-associated VAP-B(P56S) neurotoxicity.
Kim, S., Leal, S. S., Ben Halevy, D., Gomes, C. M. & Lev, S.
J Biol Chem (2010). 285, 13839-13849

70. Emerging roles for riboflavin in functional rescue of mitochondrial beta-oxidation flavoenzymes.
Henriques, B. J., Olsen, R. K., Bross, P. & Gomes, C. M.
Current medicinal chemistry (2010). 17, 3842-3854

69. Mutational hotspots in electron transfer flavoprotein underlie defective folding and function in multiple acyl-CoA dehydrogenase deficiency.
Henriques, B. J., Bross, P. & Gomes, C. M.
Biochim Biophys Acta (2010). 1802, 1070-1077

68. Natural and amyloid self-assembly of S100 proteins: structural basis of functional diversity.
Fritz, G., Botelho, H. M., Morozova-Roche, L. A. & Gomes, C. M.
The FEBS journal (2010). 277, 4578-4590

67. Iron-binding activity in yeast frataxin entails a trade off with stability in the alpha1/beta1 acidic ridge region.
Correia, A. R., Wang, T., Craig, E. A. & Gomes, C. M.
Biochem J (2010). 426, 197-203

66. Role of a novel disulfide bridge within the all-beta fold of soluble Rieske proteins.
Botelho, H. M., Leal, S. S., Veith, A., Prosinecki, V., Bauer, C., Frohlich, R., Kletzin, A. & Gomes, C. M.
J Biol Inorg Chem (2010). 15, 271-281

65. No evidence of direct binding between ursodeoxycholic acid and the p53 DNA-binding domain.
Amaral, J. D., Correia, A. R., Steer, C. J., Gomes, C. M. & Rodrigues, C. M.
Bioscience reports (2010). 30, 359-364

64. Role of flavinylation in a mild variant of multiple acyl-CoA dehydrogenation deficiency: a molecular rationale for the effects of riboflavin supplementation.
Henriques, B. J., Rodrigues, J. V., Olsen, R. K., Bross, P. & Gomes, C. M.
J Biol Chem (2009). 284, 4222-4229

63. The conserved Trp155 in human frataxin as a hotspot for oxidative stress related chemical modifications.
Correia, A. R., Ow, S. Y., Wright, P. C. & Gomes, C. M.
Biochem Biophys Res Commun (2009). 390, 1007-1011

62. Metal ions modulate the folding and stability of the tumor suppressor protein S100A2.
Botelho, H. M., Koch, M., Fritz, G. & Gomes, C. M.
The FEBS journal (2009). 276, 1776-1786

61. The prominent conformational plasticity of lactoperoxidase: a chemical and pH stability analysis.
Boscolo, B., Leal, S. S., Salgueiro, C. A., Ghibaudi, E. M. & Gomes, C. M.
Biochim Biophys Acta (2009). 1794, 1041-1048

2008

60. A novel type of monoheme cytochrome c: biochemical and structural characterization at 1.23 A resolution of Rhodothermus marinus cytochrome c.
Stelter, M., Melo, A. M., Pereira, M. M., Gomes, C. M., Hreggvidsson, G. O., Hjorleifsdottir, S., Saraiva, L. M., Teixeira, M. & Archer, M.
Biochemistry (2008). 47, 11953-11963

59. Protein misfolding in conformational disorders: rescue of folding defects and chemical chaperoning.
Leandro, P. & Gomes, C. M.
Mini Rev Med Chem (2008). 8, 901-911

58. On the relative contribution of ionic interactions over iron-sulfur clusters to ferredoxin stability.
Leal, S. S. & Gomes, C. M.
Biochim Biophys Acta (2008). 1784, 1596-1600

57. Kinetic analysis of L1 homophilic interaction: role of the first four immunoglobulin domains and implications on binding mechanism.
Gouveia, R. M., Gomes, C. M., Sousa, M., Alves, P. M. & Costa, J.
J Biol Chem (2008). 283, 28038-28047

56. Crystallographic analysis of the intact metal centres [3Fe-4S](1+/0) and [4Fe-4S](2+/1+) in a Zn(2+)-containing ferredoxin.
Frazao, C., Aragao, D., Coelho, R., Leal, S. S., Gomes, C. M., Teixeira, M. & Carrondo, M. A.
FEBS Lett (2008). 582, 763-767

55. On the relation between native geometry and conformational plasticity.
Faisca, P. F. & Gomes, C. M.
Biophys Chem (2008). 138, 99-106

54. Dynamics, stability and iron-binding activity of frataxin clinical mutants.
Correia, A. R., Pastore, C., Adinolfi, S., Pastore, A. & Gomes, C. M.
The FEBS journal (2008). 275, 3680-3690

53. A Spectroscopic Study of the Temperature Induced Modifications on Ferredoxin Folding and Iron-Sulfur Moieties.
Todorovic, S., Leal, S. S., Salgueiro, C. A., Zebger, I., Hildebrandt, P., Murgida, D. H. & Gomes, C. M.
Biochemistry (2007). 46, 10733-10738

52. Conformational states and protein stability in a proteomic perspective.
Prosinecki, V., Faísca, P. F. N. & Gomes, C. M.
Current Proteomics (2007). 4, 44-52

51. ApoA-I cleaved by transthyretin has reduced ability to promote cholesterol efflux and increased amyloidogenicity.
Liz, M. A., Gomes, C. M., Saraiva, M. J. & Sousa, M. M.
J Lipid Res (2007). 48, 2385-2395

50. Studies of the molten globule state of ferredoxin: Structural characterization and implications on protein folding and iron-sulfur center assembly.
Leal, S. S. & Gomes, C. M.
Proteins (2007). 68, 606-616

49. Lactoperoxidase folding and catalysis relies on the stabilization of the alpha-helix rich core domain: A thermal unfolding study.
Boscolo, B., Leal, S. S., Ghibaudi, E. M. & Gomes, C. M.
Biochim Biophys Acta (2007). 1774, 1164-1172

2006

48. X-ray Structure of a self-compartmentalizing sulfur cycle metalloenzyme.
Urich, T., Gomes, C. M., Kletzin, A. & Frazao, C.
Science (2006). 311, 996-1000

47. Natural domain design: enhanced thermal stability of a zinc-lacking ferredoxin isoform shows that a hydrophobic core efficiently replaces the structural metal site.
Rocha, R., Leal, S. S., Teixeira, V. H., Regalla, M., Huber, H., Baptista, A. M., Soares, C. M. & Gomes, C. M.
Biochemistry (2006). 45, 10376-10384

46. A Proteomic Approach toward the Selection of Proteins with Enhanced Intrinsic Conformational Stability.
Prosinecki, V., Botelho, H. M., Francese, S., Mastrobuoni, G., Moneti, G., Urich, T., Kletzin, A. & Gomes, C. M.
J Proteome Res (2006). 5, 2720-2726

45. Combined spectroscopic and calorimetric characterisation of rubredoxin reversible thermal transition.
Henriques, B. J., Saraiva, L. M. & Gomes, C. M.
J Biol Inorg Chem (2006). 11, 73-81

44. Conformational stability of human frataxin and effect of Friedreich's ataxia-related mutations on protein folding.
Correia, A. R., Adinolfi, S., Pastore, A. & Gomes, C. M.
Biochem J (2006). 398, 605-611

2005

43. Linear three-iron centres are unlikely cluster degradation intermediates during unfolding of iron-sulfur proteins.
Leal, S. S. & Gomes, C. M.
Biol Chem (2005). 386, 1295-1300

42. A Rieske ferredoxin typifying a subtype within Rieske proteins: spectroscopic, biochemical and stability studies.
Kletzin, A., Ferreira, A. S., Hechler, T., Bandeiras, T. M., Teixeira, M. & Gomes, C. M.
FEBS Lett (2005). 579, 1020-1026

41. Probing the mechanism of rubredoxin thermal unfolding in the absence of salt bridges by temperature jump experiments.
Henriques, B. J., Saraiva, L. M. & Gomes, C. M.
Biochem Biophys Res Commun (2005). 333, 839-844

40. The sulphur oxygenase reductase from Acidianus ambivalens is a multimeric protein containing a low-potential mononuclear non-haem iron centre.
Urich, T., Bandeiras, T. M., Leal, S. S., Rachel, R., Albrecht, T., Zimmermann, P., Scholz, C., Teixeira, M., Gomes, C. M. & Kletzin, A.
Biochem J (2004). 381, 137-146

39. Coupling of the pathway of sulphur oxidation to dioxygen reduction: characterization of a novel membrane-bound thiosulphate:quinone oxidoreductase.
Muller, F. H., Bandeiras, T. M., Urich, T., Teixeira, M., Gomes, C. M. & Kletzin, A.
Mol Microbiol (2004). 53, 1147-1160

38. Studies on the degradation pathway of iron-sulfur centers during unfolding of a hyperstable ferredoxin: cluster dissociation, iron release and protein stability.
Leal, S. S., Teixeira, M. & Gomes, C. M.
J Biol Inorg Chem (2004). 9, 987-996

37. Dissimilatory oxidation and reduction of elemental sulfur in thermophilic archaea.
Kletzin, A., Urich, T., Muller, F., Bandeiras, T. M. & Gomes, C. M.
J Bioenerg Biomembr (2004). 36, 77-91

36. Active site structure of the aa3 quinol oxidase of Acidianus ambivalens.
Das, T. K., Gomes, C. M., Bandeiras, T. M., Pereira, M. M., Teixeira, M. & Rousseau, D. L.
Biochim Biophys Acta (2004). 1655, 306-320

2003

35. Docking and electron transfer studies between rubredoxin and rubredoxin:oxygen oxidoreductase.
Victor, B. L., Vicente, J. B., Rodrigues, R., Oliveira, S., Rodrigues-Pousada, C., Frazao, C., Gomes, C. M., Teixeira, M. & Soares, C. M.
J Biol Inorg Chem (2003). 8, 475-488

34. FTIR spectroscopic characterization of the cytochrome aa3 from Acidianus ambivalens: evidence for the involvement of acidic residues in redox coupled proton translocation.
Hellwig, P., Gomes, C. M. & Teixeira, M.
Biochemistry (2003). 42, 6179-6184

33. The respiratory chain of the thermophilic archaeon Sulfolobus metallicus: studies on the type-II NADH dehydrogenase.
Bandeiras, T. M., Salgueiro, C. A., Huber, H., Gomes, C. M. & Teixeira, M.
Biochim Biophys Acta (2003). 1557, 13-19

2002

32. Module fusion in an A-type flavoprotein from the cyanobacterium Synechocystis condenses a multiple-component pathway in a single polypeptide chain.
Vicente, J. B., Gomes, C. M., Wasserfallen, A. & Teixeira, M.
Biochem Biophys Res Commun (2002). 294, 82-87

31. Plasticity of proton pathways in haem-copper oxygen reductases.
Pereira, M. M., Gomes, C. M. & Teixeira, M.
FEBS Lett (2002). 522, 14-18

30. The quinol:fumarate oxidoreductase from the sulphate reducing bacterium Desulfovibrio gigas: spectroscopic and redox studies.
Lemos, R. S., Gomes, C. M., LeGall, J., Xavier, A. V. & Teixeira, M.
J Bioenerg Biomembr (2002). 34, 21-30

29. Quinol:fumarate oxidoreductases and succinate:quinone oxidoreductases: phylogenetic relationships, metal centres and membrane attachment.
Lemos, R. S., Fernandes, A. S., Pereira, M. M., Gomes, C. M. & Teixeira, M.
Biochim Biophys Acta (2002). 1553, 158-170

28. Formation of a linear [3Fe-4S] cluster in a seven-iron ferredoxin triggered by polypeptide unfolding.
Jones, K., Gomes, C. M., Huber, H., Teixeira, M. & Wittung-Stafshede, P.
J Biol Inorg Chem (2002). 7, 357-362

27. An archaeal b-type cytochrome containing a nonfunctional carbonic anhydrase-like domain.
Gomes, C. M., Kletzin, A. & Teixeira, M.
J Biol Inorg Chem (2002). 7, 483-489

26. A novel type of nitric-oxide reductase. Escherichia coli flavorubredoxin.
Gomes, C. M., Giuffre, A., Forte, E., Vicente, J. B., Saraiva, L. M., Brunori, M. & Teixeira, M.
J Biol Chem (2002). 277, 25273-25276. https://doi.org/doi: 10.1074/jbc.M203886200

25. Functional control of the binuclear metal site in the metallo-beta-lactamase-like fold by subtle amino acid replacements.
Gomes, C. M., Frazao, C., Xavier, A. V., Legall, J. & Teixeira, M.
Protein Sci (2002). 11, 707-712

24. Acidianus ambivalens type-II NADH dehydrogenase: genetic characterisation and identification of the flavin moiety as FMN.
Bandeiras, T. M., Salgueiro, C., Kletzin, A., Gomes, C. M. & Teixeira, M.
FEBS Lett (2002). 531, 273-277

2001

23. High stability of a ferredoxin from the hyperthermophilic archaeon A. ambivalens: involvement of electrostatic interactions and cofactors.
Moczygemba, C., Guidry, J., Jones, K. L., Gomes, C. M., Teixeira, M. & Wittung-Stafshede, P.
Protein Sci (2001). 10, 1539-1548

22. Acidianus ambivalens Complex II typifies a novel family of succinate dehydrogenases.
Lemos, R. S., Gomes, C. M. & Teixeira, M.
Biochem Biophys Res Commun (2001). 281, 141-150

21. The 'strict' anaerobe Desulfovibrio gigas contains a membrane-bound oxygen-reducing respiratory chain.
Lemos, R. S., Gomes, C. M., Santana, M., LeGall, J., Xavier, A. V. & Teixeira, M.
FEBS Lett (2001). 496, 40-43

20. Could a diiron-containing four-helix-bundle protein have been a primitive oxygen reductase?
Gomes, C. M., Le Gall, J., Xavier, A. V. & Teixeira, M.
Chembiochem (2001). 2, 583-587

19. A new type-II NADH dehydrogenase from the archaeon Acidianus ambivalens: characterization and in vitro reconstitution of the respiratory chain.
Gomes, C. M., Bandeiras, T. M. & Teixeira, M.
J Bioenerg Biomembr (2001). 33, 1-8

18. Heme-copper oxidases with modified D- and K-pathways are yet efficient proton pumps.
Gomes, C. M., Backgren, C., Teixeira, M., Puustinen, A., Verkhovskaya, M. L., Wikstrom, M. & Verkhovsky, M. I.
FEBS Lett (2001). 497, 159-164

17. Kinetics of electron and proton transfer during O(2) reduction in cytochrome aa(3) from A. ambivalens: an enzyme lacking Glu(I-286).
Gilderson, G., Aagaard, A., Gomes, C. M., Adelroth, P., Teixeira, M. & Brzezinski, P.
Biochim Biophys Acta (2001). 1503, 261-270

 

This section contains most, but not all, of Cláudio's PhD work publications

2000

16. Stability and folding of the ferredoxin from the hyperthermophilic archaeon Acidianus ambivalens.
Wittung-Stafshede, P., Gomes, C. M. & Teixeira, M.
J Inorg Biochem (2000). 78, 35-41

15. Spectroscopic studies and characterization of a novel electron-transfer chain from Escherichia coli involving a flavorubredoxin and its flavoprotein reductase partner.
Gomes, C. M., Vicente, J. B., Wasserfallen, A. & Teixeira, M.
Biochemistry (2000). 39, 16230-16237

14. Structure of a dioxygen reduction enzyme from Desulfovibrio gigas.
Frazao, C., Silva, G., Gomes, C. M., Matias, P., Coelho, R., Sieker, L., Macedo, S., Liu, M. Y., Oliveira, S., Teixeira, M., Xavier, A. V., Rodrigues-Pousada, C., Carrondo, M. A. & Le Gall, J.
Nat Struct Biol (2000). 7, 1041-1045. https://doi.org/doi:10.1038/80961
1999

2000 

13. Desulfovibrio gigas neelaredoxin. A novel superoxide dismutase integrated in a putative oxygen sensory operon of an anaerobe.
Silva, G., Oliveira, S., Gomes, C. M., Pacheco, I., Liu, M. Y., Xavier, A. V., Teixeira, M., Legall, J. & Rodrigues-pousada, C.
Eur J Biochem (1999). 259, 235-243

12. The superoxide dismutase activity of desulfoferrodoxin from Desulfovibrio desulfuricans ATCC 27774.
Romao, C. V., Liu, M. Y., Le Gall, J., Gomes, C. M., Braga, V., Pacheco, I., Xavier, A. V. & Teixeira, M.
Eur J Biochem (1999). 261, 438-443

11. The unusual iron sulfur composition of the Acidianus ambivalens succinate dehydrogenase complex.
Gomes, C. M., Lemos, R. S., Teixeira, M., Kletzin, A., Huber, H., Stetter, K. O., Schafer, G. & Anemuller, S.
Biochim Biophys Acta (1999). 1411, 134-141

10. Redox-linked transient deprotonation at the binuclear site in the aa(3)-type quinol oxidase from Acidianus ambivalens: implications for proton translocation.
Das, T. K., Gomes, C. M., Teixeira, M. & Rousseau, D. L.
Proc Natl Acad Sci U S A (1999). 96, 9591-9596

9. Dynamics of the binuclear center of the quinol oxidase from Acidianus ambivalens.
Aagaard, A., Gilderson, G., Gomes, C. M., Teixeira, M. & Brzezinski, P.
Biochemistry (1999). 38, 10032-10041

1998

8. Characterisation of a new rubredoxin isolated from Desulfovibrio desulfuricans 27774: definition of a new family of rubredoxins.
LeGall, J., Liu, M. Y., Gomes, C. M., Braga, V., Pacheco, I., Regalla, M., Xavier, A. V. & Teixeira, M.
FEBS Lett (1998). 429, 295-298

7. Ambineela, an unusual blue protein isolated from the archaeon Acidianus ambivalens.
Gomes, C. M. & Teixeira, M.
Biochem Biophys Res Commun (1998). 249, 23-25

6. The NADH oxidase from the thermoacidophilic archaea Acidianus ambivalens: isolation and physicochemical characterisation.
Gomes, C. M. & Teixeira, M.
Biochem Biophys Res Commun (1998). 243, 412-415

5. Evidence for a novel type of iron cluster in the respiratory chain of the archaeon Sulfolobus metallicus.
Gomes, C. M., Huber, H., Stetter, K. O. & Teixeira, M.
FEBS Lett (1998). 432, 99-102

4. Di-cluster, seven-iron ferredoxins from hyperthermophilic Sulfolobales.
Gomes, C. M., Faria, A., Carita, J. C., Mendes, J., Regalla, M., Chicau, P., Huber, H., Stetter, K. O. & Teixeira, M.
J Biol Inorg Chem (1998). 3, 499-507

1997

3. Studies on the redox centers of the terminal oxidase from Desulfovibrio gigas and evidence for its interaction with rubredoxin.
Gomes, C. M., Silva, G., Oliveira, S., LeGall, J., Liu, M. Y., Xavier, A. V., Rodrigues-Pousada, C. & Teixeira, M.
J Biol Chem (1997). 272, 22502-22508

2. Functional properties of the quinol oxidase from Acidianus ambivalens and the possible catalytic role of its electron donor--studies on the membrane-integrated and purified enzyme.
Giuffre, A., Gomes, C. M., Antonini, G., D'Itri, E., Teixeira, M. & Brunori, M.
Eur J Biochem (1997). 250, 383-388

1995 

1. A seven-iron ferredoxin from the thermoacidophilic archaeon Desulfurolobus ambivalens.
Teixeira, M., Batista, R., Campos, A. P., Gomes, C., Mendes, J., Pacheco, I., Anemuller, S. & Hagen, W. R.
Eur J Biochem (1995). 227, 322-327  

Invited chapters contributed to edited books

10. Metals and amyloid gain-of-toxic mechanisms in neurodegenerative diseases
Cristóvão, J. S., Moreira, G. G., Grabrucker, A. M. & Gomes, C. M. in Protein Homeostasis Diseases (ed Angel L. Pey), 181-195 (Academic Press, 2020).

9. Riboflavin (vitamin B2) and mitochondrial energy
Henriques, B. J. & Gomes, C. M. in Molecular Nutrition (ed Vinood B. Patel), 225-244 (Academic Press, 2020).

8. Thermal Shift and Stability Assays of Disease-Related Misfolded Proteins Using Differential Scanning Fluorimetry.
Lucas, T. G., Gomes, C. M. & Henriques, B. J.
Methods Mol Biol (2019). 1873, 255-264. https://doi.org/10.1007/978-1-4939-8820-4_16

7. Biophysical and Spectroscopic Methods for Monitoring Protein Misfolding and Amyloid Aggregation.
Cristóvão, J. S., Henriques, B. J. & Gomes, C. M.
Methods Mol Biol (2019). 1873, 3-18. https://doi.org/10.1007/978-1-4939-8820-4_1

6. Preparation of Amyloidogenic Aggregates from EF-Hand beta-Parvalbumin and S100 Proteins.
Martinez, J., Cristovao, J. S., Sanchez, R., Gasset, M. & Gomes, C. M.
Methods Mol Biol (2018). 1779, 167-179. https://doi.org/10.1007/978-1-4939-7816-8_11

5. Chapter 18 - Structural Heterogeneity and Bioimaging of S100 Amyloid Assemblies
Carvalho, S. B., Cardoso, I., Botelho, H. M., Yanamandra, K., Fritz, G., Gomes, C. M. & Morozova-Roche, L. A. in Bio-nanoimaging (eds Vladimir N. Uversky & Yuri L. Lyubchenko), 197-212 (Academic Press, 2014).

4. Riboflavin and beta-oxidation Flavoenzymes
Henriques, B. J., Rodrigues, J. V. & Gomes, C. M. in B Vitamins and Folate: Chemistry, Analysis, Function and Effects (ed Victor R Preedy), 611-632 (The Royal Society of Chemistry, 2012).

3. Analysis of S100 Oligomers and Amyloids
Botelho, H. M., Fritz, G. & Gomes, C. M. in Amyloid Proteins: Methods and Protocols Methods in Molecular Biology (eds E.M. Sigurdsson, M. Calero & M. Gasset), ( Springer Science+Business Media, 2012).

2.Iron-Sulfur Clusters, Protein Folds, and Ferredoxin Stability
Leal, S. S. & Gomes, C. M. in Protein Folding and Metal Ions (eds C.M. Gomes & P Wittung-Stafshede), 81-96 (CRC Press, 2010).

1. Metal Ions, Protein Folding, and Conformational States
Gomes, C. M. & Wittung-Stafshede, P. in Protein Folding and Metal Ions (eds C.M. Gomes & P Wittung-Stafshede), 3-11 (CRC Press, 2010). 

Cláudio Gomes: "A promoção e reconhecimento da qualidade da investigação científica tem um impacto muito positivo dentro e fora da própria Universidade"
Notícias FCUL, 15-01-2021

 
Equipa liderada por português descobre proteína do cérebro que protege de Alzheimer
Observador, 29/06/2018

 
Equipa liderada por português descobre como atrasar uma das causas de Alzheimer
TSF, 30/06/2018

  
Entrevista a Cláudio M. Gomes. 'Ainda há muito por saber em relação à doença de Alzheimer
Semanário Sol, 24/07/2018

 

New Role for Cytokine S100B: Inhibiting amyloid Aggregation
Alzforum, 03/07/2018

Entrevista a Cláudio M. Gomes. 'A ciência é global e colaborativa'
Notícias FCUL, 09-07-2018


Reportagem: Novo modelo para uma doença rara
Programa ‘Com Ciência’ RTP2, 20/06/2012

Reportagem: a Noite Europeia dos Investigadores
Telejornal, RTP1. 25 Setembro 2008

 
Usam extremófilos para estudar a vida
Jornal de Notícias, 30/11/2000


"Nature" revela importante descoberta de um grupo de cientistas portugueses
Diário de Notícias, 28/11/2000