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1. Full Text Plasmodium falciparum Plasmodium helical interspersed subtelomeric proteins contribute to cytoadherence and anchor P. falciparum erythrocyte membrane protein 1 to the host cell cytoskeleton
by Oberli, Alexander and Zurbrügg, Laura and Rusch, Sebastian and Brand, Françoise and Butler, Madeleine E and Day, Jemma L and Cutts, Erin E and Lavstsen, Thomas and Vakonakis, Ioannis and Beck, Hans‐Peter
Cellular Microbiology, ISSN 1462-5814, 10/2016, Volume 18, Issue 10, pp. 1415 - 1428
Summary Adherence of Plasmodium falciparum‐infected erythrocytes to host endothelium is conferred through the parasite‐derived virulence factor P. falciparum... 
PFEMP1 | DOMAIN | RESA PROTEIN | HISTIDINE-RICH PROTEIN | VAR GENES | MICROBIOLOGY | RED-BLOOD-CELLS | INFECTED ERYTHROCYTES | MALARIA PARASITES | BINDING | SURFACE-ANTIGENS | CELL BIOLOGY | Malaria, Falciparum | Humans | Cells, Cultured | Cell Adhesion | Protozoan Proteins - physiology | Protein Interaction Maps | Protein Transport | Erythrocytes - metabolism | Cytoskeleton - metabolism | Protein Binding | Host-Parasite Interactions | Plasmodium falciparum - physiology | Erythrocytes - parasitology | Proteins | Plasmodium falciparum | Virulence (Microbiology) | Malaria | Endothelium | Cytoskeleton | Erythrocytes | Original
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2. Full Text A conserved domain targets exported PHISTb family proteins to the periphery of Plasmodium infected erythrocytes
by Tarr, Sarah J and Moon, Robert W and Hardege, Iris and Osborne, Andrew R
Molecular & Biochemical Parasitology, ISSN 0166-6851, 08/2014, Volume 196, Issue 1, pp. 29 - 40
The extended PRESAN domain is a targeting domain used by multiple species to target PHISTb proteins to the cytoskeleton/plasma membrane of infected cells.... 
Plasmodium | Cytoskeleton | PRESAN | PHIST | Malaria | Protein export | KNOWLESI | FALCIPARUM | BIOCHEMISTRY & MOLECULAR BIOLOGY | MEMBRANE SKELETAL PROTEIN | TRAFFICKING | VIRULENCE | SPECTRIN | MALARIA PARASITE | RED-BLOOD-CELLS | SURFACE-ANTIGEN RESA | PARASITOLOGY | Protein Structure, Tertiary | Plasmodium vivax - metabolism | Plasmodium knowlesi - metabolism | Solubility | Plasmodium vivax - genetics | Plasmodium knowlesi - genetics | Protozoan Proteins - genetics | Protein Transport | Protozoan Proteins - metabolism | Plasmodium falciparum - genetics | Erythrocytes - metabolism | Cytoskeleton - metabolism | Protein Binding | Plasmodium falciparum - metabolism | Protozoan Proteins - chemistry | Erythrocytes - parasitology | Proteins
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3. Full Text Deletion of Plasmodium falciparum Protein RON3 Affects the Functional Translocation of Exported Proteins and Glucose Uptake
by Low, LM and Azasi, Y and Sherling, ES and Garten, M and Zimmerberg, J and Tsuboi, T and Brzostowski, J and Mu, JB and Blackman, MJ and Miller, LH
MBIO, ISSN 2150-7511, 07/2019, Volume 10, Issue 4
The survival of Plasmodium spp. within the host red blood cell (RBC) depends on the function of a membrane protein complex, termed the Plasmodium translocon of... 
ANTIBODIES | LOCALIZATION | SIZE | RESA | parasitophorous vacuolar space | MICROBIOLOGY | malaria | MALARIA PARASITES | PTEX | INVASION | GENE | parasite proteins | ERYTHROCYTE
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4. Full Text Impact of selected amino acids of HP0377 (Helicobacter pylori thiol oxidoreductase) on its functioning as a CcmG (cytochrome c maturation) protein and Dsb (disulfide bond) isomerase
by Grzeszczuk, Magdalena Joanna and Bąk, Aleksandra and Banaś, Anna Marta and Urbanowicz, Paweł and Dunin-Horkawicz, Stanislaw and Gieldon, Artur and Czaplewski, Cezary and Liwo, Adam and Jagusztyn-Krynicka, Elżbieta K
PLoS ONE, ISSN 1932-6203, 04/2018, Volume 13, Issue 4, p. e0195358
Helicobacter pylori HP0377 is a thiol oxidoreductase, a member of the CcmG family involved in cytochrome biogenesis, as previously shown by in vitro... 
SUBSTRATE-SPECIFICITY | BACILLUS-SUBTILIS RESA | BIOGENESIS | STRUCTURAL BASIS | BRADYRHIZOBIUM-JAPONICUM | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | SECRETION SYSTEM | EXTRACYTOPLASMIC THIOREDOXIN RESA | REDOX | CYSTEINE RESIDUES | Cytochrome c | Physiological aspects | Genetic aspects | Oxidoreductases | Research | Helicobacter pylori | Cytochrome | Enzymes | Plant mitochondria | Oxidoreductase | Isomerization | Amino acid composition | Proline | Amino acids | Biosynthesis | Biology | Phylogeny | Thioredoxin | Streptococcus infections | Proteins | Reduction | Thiol oxidoreductase | Chemical bonds | Reductase
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5. Full Text Pf155/RESA protein influences the dynamic microcirculatory behavior of ring-stage Plasmodium falciparum infected red blood cells
by Diez-Silva, Monica and Park, Yongkeun and Huang, Sha and Bow, Hansen and Mercereau-Puijalon, Odile and Deplaine, Guillaume and Lavazec, Catherine and Perrot, Sylvie and Bonnefoy, Serge and Feld, Michael S and Han, Jongyoon and Dao, Ming and Suresh, Subra
Scientific Reports, ISSN 2045-2322, 2012, Volume 2, Issue 1, p. 614
Proteins exported by Plasmodium falciparum to the red blood cell (RBC) membrane modify the structural properties of the parasitized RBC (Pf-RBC). Although... 
AMA1 | DIFFRACTION PHASE | DENSE GRANULES | SPECTRIN | RESA PROTEIN | MULTIDISCIPLINARY SCIENCES | RON2 | MALARIA | ERYTHROCYTE SURFACE-ANTIGEN | Temperature | Protozoan Proteins - metabolism | Humans | Erythrocytes - metabolism | Plasmodium falciparum - metabolism | Cell Membrane - metabolism | Plasmodium falciparum - growth & development | Erythrocytes - parasitology | Microspheres | Diffraction | Deformability | Temperature effects | Blood cells | Erythrocytes | Parasites | Velocity | Fever | Life Sciences | Cell Membrane | Plasmodium falciparum | Microbiology and Parasitology | Protozoan Proteins
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6. Full Text Structural and functional characterization of HP0377, a thioredoxin‐fold protein from Helicobacter pylori
by Yoon, Ji Young and Kim, Jieun and An, Doo Ri and Lee, Sang Jae and Kim, Hyoun Sook and Im, Ha Na and Yoon, Hye‐Jin and Kim, Jin Young and Kim, Soon‐Jong and Han, Byung Woo and Suh, Se Won
Acta Crystallographica Section D, ISSN 1399-0047, 05/2013, Volume 69, Issue 5, pp. 735 - 746
Maturation of cytochrome c is carried out in the bacterial periplasm, where specialized thiol‐disulfide oxidoreductases provide the correct reduction of... 
DsbC | HP0377 | cytochrome c biogenesis | Helicobacter pylori | HP1227 | HP0518 | DISULFIDE BOND FORMATION | CYTOCHROME-C BIOGENESIS | OXIDOREDUCTASE DSBA | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | BIOCHEMICAL RESEARCH METHODS | PERIPLASMIC THIOREDOXIN | CRYSTALLOGRAPHY | SUBSTRATE-SPECIFICITY | BIOPHYSICS | BACILLUS-SUBTILIS RESA | BRADYRHIZOBIUM-JAPONICUM | CYSTEINE RESIDUES | Protein Disulfide Reductase (Glutathione) - metabolism | Amino Acid Sequence | Catalytic Domain | Periplasmic Proteins - chemistry | Helicobacter pylori - chemistry | Cytochromes c - metabolism | Bacterial Proteins - chemistry | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | Cysteine - chemistry | Protein Disulfide Reductase (Glutathione) - chemistry | Helicobacter pylori - metabolism | Bacterial Proteins - metabolism | Protein Conformation | Periplasmic Proteins - metabolism | Oxidases | Cysteine | Thiols | Crystals | Drugstores | Biosynthesis | Thioredoxin | Cystine | Cytochrome c | Chemical properties | Structure | Mass spectrometry | Proteins | Enzymes
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7. Full Text Crystal structure and biophysical properties of Bacillus subtilis BdbD. An oxidizing thiol:disulfide oxidoreductase containing a novel metal site
by Crow, Allister and Lewin, Allison and Hecht, Oliver and Möller, Mirja Carlsson and Moore, Geoffrey R and Hederstedt, Lars and Le Brun, Nick E and Molekylär cellbiologi and Lund University and Molecular Cell Biology and Lunds universitet
Journal of Biological Chemistry, ISSN 0021-9258, 08/2009, Volume 284, Issue 35, pp. 23719 - 23733
BdbD is a thiol: disulfide oxidoreductase (TDOR) from Bacillus subtilis that functions to introduce disulfide bonds in substrate proteins/peptides on the... 
BOND FORMATION INVIVO | FORMATION IN-VIVO | ACTIVE-SITE | PSEUDOMONAS-AERUGINOSA | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | EXTRACYTOPLASMIC THIOREDOXIN RESA | ELECTRON-DENSITY MAPS | REDOX PROPERTIES | FUNCTIONAL-CHARACTERIZATION | DESTABILIZING DISULFIDE | Protein Disulfide Reductase (Glutathione) - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Oxidation-Reduction | Calcium - metabolism | Molecular Conformation | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Crystallization | Molecular Sequence Data | Calcium - chemistry | Protein Disulfide Reductase (Glutathione) - chemistry | Sequence Homology, Amino Acid | Protein Disulfide Reductase (Glutathione) - genetics | Protein Binding | Bacterial Proteins - metabolism | Binding Sites | Protein Structure and Folding | Biological Sciences | Naturvetenskap | Microbiology | Biokemi och molekylärbiologi | Mikrobiologi | Biochemistry and Molecular Biology | Biologi | Natural Sciences
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8. Full Text Haem‐delivery proteins in cytochrome c maturation System II
by Ahuja, Umesh and Kjelgaard, Peter and Schulz, Benjamin L and Thöny‐Meyer, Linda and Hederstedt, Lars and Molekylär cellbiologi and Lund University and Molecular Cell Biology and Department of Biology and Lunds universitet and Biologiska institutionen
Molecular Microbiology, ISSN 0950-382X, 09/2009, Volume 73, Issue 6, pp. 1058 - 1071
Summary Cytochromes of the c‐type function on the outer side of the cytoplasmic membrane in bacteria where they also are assembled from apo‐cytochrome... 
CHAPERONE CCME | BACTERIA | COMPLEX | BIOGENESIS | BACILLUS-SUBTILIS | ACTIVE-SITE | BIOSYNTHESIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | GENES | RESA | MICROBIOLOGY | Recombinant Proteins - metabolism | Amino Acid Sequence | Helicobacter - enzymology | Heme - metabolism | Hemeproteins - metabolism | Cytochromes c - metabolism | Molecular Sequence Data | Bacillus subtilis - enzymology | Recombinant Proteins - genetics | Bacillus subtilis - genetics | Carrier Proteins - metabolism | Escherichia coli - genetics | Helicobacter - metabolism | Escherichia coli - metabolism | Bacterial Proteins - metabolism | Cytochrome c | Biological products | Escherichia coli | Heme | Water quality | Soil inoculation | Membrane proteins | Biological Sciences | Biologi | Naturvetenskap | Natural Sciences
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9. Full Text CCS5, a thioredoxin-like protein involved in the assembly of plastid c-type cytochromes
by Gabilly, Stéphane T and Dreyfuss, Beth Welty and Karamoko, Mohamed and Corvest, Vincent and Kropat, Janette and Page, M. Dudley and Merchant, Sabeeha S and Hamel, Patrice P
Journal of Biological Chemistry, ISSN 0021-9258, 09/2010, Volume 285, Issue 39, pp. 29738 - 29749
The c-type cytochromes are metalloproteins with a heme molecule covalently linked to the sulfhydryls of a CXXCH hemebinding site. In plastids, at least six... 
HEME ATTACHMENT | BACILLUS-SUBTILIS RESA | CHLAMYDOMONAS-REINHARDTII | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | SYSTEM-II | XANTHOPHYLL CYCLE | THIOL-DISULFIDE OXIDOREDUCTASES | THYLAKOID LUMEN | BORDETELLA-PERTUSSIS | NUCLEAR TRANSFORMATION | Arabidopsis Proteins - genetics | Cytochromes f - genetics | Cytochromes c6 - genetics | Heme - metabolism | Oxidation-Reduction | Cytochromes c - metabolism | Cytochromes c6 - metabolism | Cytochromes c - genetics | Protozoan Proteins - genetics | Thylakoids - metabolism | Arabidopsis - metabolism | Arabidopsis - genetics | Arabidopsis Proteins - metabolism | Animals | Protozoan Proteins - metabolism | Thioredoxins - genetics | Chlamydomonas reinhardtii - genetics | Heme - genetics | Thylakoids - genetics | Thioredoxins - metabolism | Chlamydomonas reinhardtii - metabolism | Mutation | Binding Sites | Cytochromes f - metabolism | Index Medicus | Thiol | Bioenergetics | Membrane Biology | Disulfide | Heme | Cytochromes | Photosynthesis | Chloroplast | Reductase
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10. Full Text The heat shock protein 40 family of the malaria parasite Plasmodium falciparum
by Rug, Melanie and Maier, Alexander G
IUBMB Life, ISSN 1521-6543, 12/2011, Volume 63, Issue 12, pp. 1081 - 1086
Few diseases have had such a profound influence on human evolution and history as malaria. Despite intense efforts malaria infection continues to be a major... 
protein transport | Plasmodium | DnaJ | chaperone | heat shock protein 40 | malaria | host cell subversion | TRANSLOCATION | RESA PROTEIN | STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | INFECTED ERYTHROCYTE | VIRULENCE | CELL BIOLOGY | HOST ERYTHROCYTE | ERYTHROCYTE SURFACE-ANTIGEN | HSP40 PROTEINS | Malaria, Falciparum - parasitology | HSP40 Heat-Shock Proteins - metabolism | Animals | HSP40 Heat-Shock Proteins - genetics | Humans | Plasmodium falciparum - genetics | Plasmodium falciparum - metabolism | HSP40 Heat-Shock Proteins - classification | Protein Transport - genetics
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11. Full Text A strategic protein in cytochrome c maturation: Three-dimensional structure of CcmH and binding to apocytochrome c
by Di Matteo, Adele and Gianni, Stefano and Schininà, M. Eugenia and Giorgi, Alessandra and Altieri, Fabio and Calosci, Nicoletta and Brunori, Maurizio and Travaglini-Allocatelli, Carlo
Journal of Biological Chemistry, ISSN 0021-9258, 09/2007, Volume 282, Issue 37, pp. 27012 - 27019
CcmH ((c) under bar ytochromes (c) under bar (m) under bar aturation protein H) is an essential component of the assembly line necessary for the maturation of... 
IN-VITRO | HEME | BIOGENESIS | ACTIVE-SITE | PATHWAY | DISULFIDE-BOND FORMATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | RESA | REACTIVITY | ESCHERICHIA-COLI THIOREDOXIN | REDOX PROPERTIES | Cytochromes c - chemistry | Amino Acid Sequence | Pseudomonas aeruginosa - chemistry | Crystallization | Bacterial Outer Membrane Proteins - chemistry | Models, Molecular | Molecular Sequence Data | Cytochromes c - physiology | Binding Sites
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12. Full Text Immunoglobulin response to Plasmodium falciparum RESA proteins in uncomplicated and severe malaria
by Badaut, Cyril and Guyonnet, Léa and Milet, Jacqueline and Renard, Emmanuelle and Durand, Rémy and Viwami, Firmine and Sagbo, Gratien and Layla, Francis and Deloron, Philippe and Bonnefoy, Serge and Migot-Nabias, Florence
Malaria Journal, ISSN 1475-2875, 07/2015, Volume 14, Issue 1, p. 278
Background: The three members of the ring-infected erythrocyte surface antigen (RESA) proteins family share high sequence homologies, which impair the... 
B cell epitope | Severe malaria | Benin | Plasmodium falciparum | Ring-infected erythrocyte surface antigen | INFECTIOUS DISEASES | severe malaria | SICKLE-CELL TRAIT | TROPICAL MEDICINE | MEROZOITE INVASION | IN-VITRO | GENE | IMMUNE-RESPONSES | INFECTION | ERYTHROCYTE SURFACE-ANTIGEN | ANTIBODY-RESPONSE | BLOOD-STAGE ANTIGENS | PARASITOLOGY | PF155/RESA PROTECT | Cross-Sectional Studies | Immunoglobulin G - blood | Antibodies, Protozoan - immunology | Humans | Child, Preschool | Infant | Male | Plasmodium falciparum - immunology | Benin - epidemiology | Antibodies, Protozoan - blood | Recombinant Proteins - immunology | Immunoglobulin G - immunology | Malaria, Falciparum - epidemiology | Malaria, Falciparum - immunology | Female | Child | Protozoan Proteins - immunology | Cytokines - blood | Cytokines - immunology | Genetic polymorphisms | Malaria | Immunoglobulin G/blood | Malaria, Falciparum/immunology | Recombinant Proteins/immunology | Cytokines/immunology | Benin/epidemiology | Plasmodium falciparum/immunology | Cytokines/blood | Life Sciences | Microbiology and Parasitology | Antibodies, Protozoan/blood | Immunoglobulin G/immunology | Antibodies, Protozoan/immunology | Protozoan Proteins/immunology | Malaria, Falciparum/epidemiology
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13. Full Text A role for the Plasmodium falciparum RESA protein in resistance against heat shock demonstrated using gene disruption
by Silva, Monica Diez and Cooke, Brian M and Guillotte, Micheline and Buckingham, Donna W and Sauzet, Jean‐Pierre and Scanf, Cecile Le and Contamin, Hugues and David, Peter and Mercereau‐Puijalon, Odile and Bonnefoy, Serge
Molecular Microbiology, ISSN 0950-382X, 05/2005, Volume 56, Issue 4, pp. 990 - 1003
Summary During erythrocyte invasion, the Plasmodium falciparum Ring‐infected erythrocyte surface antigen (RESA) establishes specific interactions with... 
MEROZOITE INVASION | AOTUS MONKEYS | HUMAN-ANTIBODIES | MEMBRANE | BIOCHEMISTRY & MOLECULAR BIOLOGY | GROWTH IN-VITRO | MICROBIOLOGY | RED-BLOOD-CELLS | ERYTHROCYTE SURFACE-ANTIGEN | MALARIA PARASITES | MONKEY SAIMIRI-SCIUREUS | PF155/RESA | Malaria, Falciparum | Saimiri - parasitology | Animals, Genetically Modified | Humans | Hot Temperature | Protozoan Proteins - genetics | Antigens, Protozoan - metabolism | Animals | Protozoan Proteins - metabolism | CD36 Antigens - metabolism | Cell Shape | Plasmodium falciparum - genetics | Cytoskeleton - metabolism | Erythrocytes - cytology | Plasmodium falciparum - metabolism | Antigens, Protozoan - genetics | Mutation | Erythrocytes - parasitology
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14. Full Text Membrane-Spanning and Periplasmic Segments of CcmI Have Distinct Functions during Cytochrome c Biogenesis in Rhodobacter capsulatus
by Carsten Sanders and Clémence Boulay and Fevzi Daldal
Journal of Bacteriology, ISSN 0021-9193, 02/2007, Volume 189, Issue 3, pp. 789 - 800
Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
DISULFIDE BOND FORMATION | RHODOPSEUDOMONAS-CAPSULATA | SUBSTRATE-SPECIFICITY | LEUCINE-ZIPPER | ELECTRON-TRANSFER | PROTEIN | BACILLUS-SUBTILIS RESA | PHOTOSYNTHETIC GROWTH | ESCHERICHIA-COLI | HEME CHAPERONE CCME | MICROBIOLOGY | Protein Structure, Tertiary | Protein Structure, Secondary | Rhodobacter capsulatus - metabolism | Bacterial Outer Membrane Proteins - chemistry | Models, Molecular | Immunoblotting | Rhodobacter capsulatus - genetics | Porphyrins - metabolism | Cytochromes c - biosynthesis | Bacterial Outer Membrane Proteins - metabolism | Models, Biological | Periplasm - metabolism | Polymerase Chain Reaction | Gene Expression Regulation, Bacterial | Bacterial Outer Membrane Proteins - genetics | Cytochrome c | Genetic aspects | Research | Gram-negative bacteria | Apoprotein | Membrane proteins | Enzymes and Proteins
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15. Full Text Modifying RESA protein peptide 6671 to fit into HLA-DRβ 1 pockets induces protection against malaria
by Alba, Martha Patricia and Salazar, Luz Mary and Vargas, Luis Eduardo and Trujillo, Mary and Lopez, Yolanda and Patarroyo, Manuel Elkin
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 2004, Volume 315, Issue 4, pp. 1154 - 1164
6671 is a non-immunogenic, conserved high activity red blood cell binding peptide located between residues 141 and 160 of the Plasmodium falciparum RESA... 
Plasmodium falciparum | MHC | NMR | Malaria | HLA-DRβ 1 molecule | RESA | Molecule | HLA-DRβ
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