KOL | Vilmos FülöpClinical Medicine Doctoral School, University of Szeged, Szeged, Hungary | 6 Magyar Honvédség Egészségügyi Központ, Szülészet-Nőgyógyászati Osztály Budapest Magyarország. | 7 ... |
KOL Resume for Vilmos Fülöp
| Year | |
|---|---|
| 2022 | Clinical Medicine Doctoral School, University of Szeged, Szeged, Hungary 6 Magyar Honvédség Egészségügyi Központ, Szülészet-Nőgyógyászati Osztály Budapest Magyarország. |
| 2021 | School of Life Science, University of Warwick, Coventry, West Midlands CV4 7AL, UK |
| 2020 | School of Life Sciences, University of Warwick, Coventry CV4 7AL, UK |
| 2019 | School of Life Sciences, University of Warwick, Coventry, CV4 7AL, U.K. Magyar Honvédség Egészségügyi Központ, Szülészeti-nőgyógyászati Osztály, Semmelweis Egyetem Gyakorló Kórház Budapest, Podmaniczky u. 111., 1062. Egészségügyi Kar, Miskolci Egyetem Miskolc. |
| 2017 | School of Life Sciences, University of Warwick, Gibbet Hill Road, Coventry, CV4 7AL, UK |
| 2016 | School of Life Sciences, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL, UK |
| 2015 | Department of Obstetrics and Gynecology, Military Hospital, Budapest, Hungary. |
| 2013 | School of Life Sciences, The University of Warwick, Coventry, CV4 7AL, United Kingdom |
| 2012 | Department of Biological Sciences, University of Warwick, Gibbet Hill Road Coventry CV4 7AL, UK School of life science, University of Warwick, Coventry, United Kingdom |
| 2011 | Department of Obstetrics and Gynecology, National Health Center, Budapest, Hungary |
| 2010 | Department of Biological Sciences, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL, United Kingdom |
| 2009 | National Institute of Health, Budapest, Hungary Department of Biological Sciences, University of Warwick, Coventry, UK |
| 2008 | Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, United Kingdom, School of Biological Sciences, University of Auckland, Auckland, New Zealand, and Centre for Metalloprotein Spectroscopy and Biology, School of Biological Sciences, University of East Anglia, Norfolk, NR4 7TJ, United Kingdom |
| 2007 | Department of Biological Sciences, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL, UK |
| 2006 | University of Warwick Department of Biological Sciences UK Department of Obstetrics and Gynaecology, National Health Center, Budapest, Hungary |
| 2005 | Department of Biological Sciences, University of Warwick, Gibbit Hill Road, Coventry CV4 7AL, United Kingdom |
| 2004 | Division of Gynecologic Oncology, Department of Obstetrics and Gynecology, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA. Department of Obstetrics and Gynecology, National Health Center, 35 Szabolcs Street, Budapest 1135, Hungary |
| 2003 | New England Trophoblastic Disease Center, Donald P. Goldstein, MD Trophoblastic Tumor Registry, Division of Gynecologic Oncology, Department of Obstetrics and Gynecology, Brigham and Women's Hospital, Gillette Center for Women's Cancer, Dana-Farber Cancer Institute, Dana-Farber Harvard Cancer Center, Harvard Medical School, Boston, Massachusetts; and Department of Obstetrics and Gynecology, National Health Center, Budapest, Hungary. |
| 2002 | Laboratory of Gynecologic Oncology, Division of Gynecologic Oncology, Department of Obstetrics and Gynecology, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, USA. Department of Obstetrics and Gynecology, Haynal Imre University of Health Sciences (HIETE), Budapest, Hungary |
| 2001 | Egészségtudományi Kar, Szülészeti- és Nógyógyászati Klinika, Semmelweis Egyetem, Budapest. ‡Department of Biological Sciences, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL, United Kingdom and the |
| 2000 | Department of Biological Sciences, University of Warwick Coventry UK |
| 1999 | Department of Organic Chemistry, University of Veszprém, 8201 Veszprém, Hungary, Research Group for Petrochemistry of the Hungarian Academy of Sciences 8201 Veszprém, Hungary, and Central Research Institute of Chemistry of the Hungarian Academy of Sciences, 1525 Budapest, Hungary |
| 1998 | Department of Obstetrics and Gynecology, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, USA. |
| 1997 | Laboratory of Molecular Biophysics, University of Oxford, South Parks Road Oxford, OX1 3QU, UK |
| 1996 | Central Research Institute for Chemistry, Hungarian Academy of Sciences, H-1525 Budapest 114, PO Box 17, Hungary Laboratory of Molecular Biophysics and Oxford Center for Molecular Sciences University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom |
| 1995 | Laboratory of Molecular Biophysics and the Oxford Centre for Molecular Sciences, University of Oxford, South Parks Road, 0X1 3QU, Oxford, UK Obstetrical and Gynaecological Clinic ofHaynal Imre Medical University, Budapest |
| 1994 | Oxford Centre for Molecular Sciences and Laboratory of Molecular Biophysics, Oxford University, South Parks Road, Oxford, OX1 3QU, UK |
| 1993 | Laboratory of Molecular Biophysics and Oxford Centre for Molecular Sciences University of Oxford, South Parks Road Oxford OX1 3QU, U.K. and Department of Biochemistry, University of Oxford South Parks Road, Oxford OX1 3QU, U.K. Central Research Institute of Chemistry, Hungarian Academy of Sciences, H-1525 Budapest, PO Box 17, Hungary |
| 1992 | Boston, Massachusetts |
| 1991 | Central Research Institute for Chemistry, Hungarian Academy of Sciences, P.O. Box 17, H-1525 Budapest Hungary Laboratory of Molecular Biophysics, University of Oxford, The Rex Richards Building, South Parks Road, Oxford OX1 3QU, UK |
| 1990 | Central Research Institute of Chemistry for Hungarian Academy of Sciences , 1525, Budapest, NERC Institute of Virology and Environmental Microbiology, Mansfield Road, Oxford OX1 3SR, United Kingdom |
| 1989 | Central Research Institute for Chemistrya, POB 17, H‐1525 Budapest (Hungary) Veszprém University of Chemical Engineering, 8201 Veszprém Hungary |
| 1988 | Central Research Institute for Chemistry, Hungarian Academy of Sciences, P.O. Box 17, H-1525 Budapest, Hungary |
| 1987 | Central Research Institute of Chemistry, Hungarian Academy of Sciences, Budapest-114, POB 17, H-1525 Hungary |
Vilmos Fülöp: Influence Statistics
| Concept | World rank |
|---|---|
| his507 | #1 |
| acetolactate renantiomer | #1 |
| report betaalpha8isomerase | #1 |
| cytotoxic abortion | #1 |
| engineering disulfide movements | #1 |
| uncomplicated molar cases | #1 |
| axial interatomic distances | #1 |
| mechanism acetolactate | #1 |
| membered spirorings | #1 |
| immunohistochemically cell | #1 |
| 120 patients evidence | #1 |
| serine peptidases enzyme | #1 |
| 24dihydroxyhepta2ene17 hpch | #1 |
| function trpf gene | #1 |
| axial nso | #1 |
| esrf c222 | #1 |
| prias substrate specificity | #1 |
| alloimmune background efficacy | #1 |
| specificity subhisa | #1 |
| indication rsa patients | #1 |
| blades propeller | #1 |
| molecular processes mechanism | #1 |
| heme substrate access | #1 |
| crystals maximum length | #1 |
| uncomplicated hydatidiform mole | #1 |
| sulfilimines 1 | #1 |
| domains prolyl | #1 |
| 27 angstroms | #1 |
| chloride cuclphco | #1 |
| hydrogenbonded dimers lattice | #1 |
| dioate aldolase | #1 |
| dibenzoyl peroxide copper | #1 |
| unnatural dipeptide | #1 |
| adipinato copper | #1 |
| oligopeptidase substrate | #1 |
| hydrolase unusual member | #1 |
| mechanism prior rearrangement | #1 |
| adipinate | #1 |
| peptidase stabilizes | #1 |
| catalytically competent form | #1 |
| psaccp | #1 |
| ph3sigeme3 | #1 |
| structures inhibition studies | #1 |
| cupph32o | #1 |
| pyridine dibenzoyl peroxide | #1 |
| structures phosphoribosyl isomerase | #1 |
| acylamino acid peptide | #1 |
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Prominent publications by Vilmos Fülöp
Matrix Metalloproteinases and Their Inhibitors in Gestational Trophoblastic Diseases and Normal Placenta
[ PUBLICATION ]
OBJECTIVE: Our purpose was to investigate the expression of matrix metalloproteinases (MMPs) in gestational trophoblastic diseases and normal first-trimester placenta.
METHODS: Paraffin sections of 16 partial moles, 25 complete moles, 10 gestational choriocarcinomas, and 11 normal first-trimester placentas were studied immunohistochemically for expression of MMP-1, MMP-2, MMP-3, MMP-9, MMP-13, and tissue inhibitor of metalloproteinase-1 (TIMP-1).
RESULTS: Nine (90.0%) of the ...
| Known for Normal Placenta | Matrix Metalloproteinases | Extravillous Trophoblast | Choriocarcinoma Expression | Tissue Inhibitor |
N-terminal arm exchange is observed in the 2.15 Å crystal structure of oxidized nitrite reductase from Pseudomonas aeruginosa
[ PUBLICATION ]
BACKGROUND: Nitrite reductase from Pseudomonas aeruginosa (NiR-Pa) is a dimer consisting of two identical 60 kDa subunits, each of which contains one c and one d1 heme group. This enzyme, a soluble component of the electron-transfer chain that uses nitrate as a source of energy, can be induced by the addition of nitrate to the bacterial growth medium. NiR-Pa catalyzes the reduction of nitrite (NO2-) to nitric oxide (NO); in vitro, both cytochrome c551 and azurin are efficient electron ...
| Known for Pseudomonas Aeruginosa | Nitrite Reductase | Nir Pa | D1 Heme | Nitric Oxide |
Non-invasive diagnosis of endometriosis based on a combined analysis of six plasma biomarkers
[ PUBLICATION ]
BACKGROUND: Lack of a non-invasive diagnostic test contributes to the long delay between onset of symptoms and diagnosis of endometriosis. The aim of this study was to evaluate the combined performance of six potential plasma biomarkers in the diagnosis of endometriosis.
METHODS: This case-control study was conducted in 294 infertile women, consisting of 93 women with a normal pelvis and 201 women with endometriosis. We measured plasma concentrations of interleukin (IL)-6, IL-8, tumour ...
| Known for Diagnosis Endometriosis | Plasma Biomarkers | Secretory Phase | Controls Women | Stepwise Logistic Regression |
OBJECTIVE: The goal of this work was to study the expression of epidermal growth factor receptor (EGFR) and c-erbB-3 and c-erbB-4 oncogenes in gestational trophoblastic diseases and normal first-trimester placenta.
STUDY DESIGN: Paraffin sections of 16 cases of partial mole, 25 cases of complete mole, 10 cases of gestational choriocarcinoma, and 11 cases of therapeutic abortion were studied immunohistochemically for EGFR, c-erbB-3, and c-erbB-4 proteins. The presence of EGFR mRNA was ...
| Known for Gestational Trophoblastic | Normal Placenta | Complete Mole | Growth Factor | Situ Hybridization |
The principal physiological role of mitochondrial cytochrome c is electron transfer during oxidative phosphorylation. c-Type cytochromes are almost always characterized by covalent attachment of heme to protein through two thioether bonds between the heme vinyl groups and the thiols of cysteine residues in a Cys-Xxx-Xxx-Cys-His motif. Uniquely, however, members of the evolutionarily divergent protist phylum Euglenozoa, which includes Trypanosoma and Leishmania species, have mitochondrial ...
| Known for Mitochondrial Cytochrome | Thioether Bond | Heme Lyase | Substrate Recognition | Covalent Attachment |
BACKGROUND: Cytochrome c peroxidase from Pseudomonas aeruginosa (PsCCP) represents a new class of peroxidases which work without the need to create a semi-stable free radical for catalysis. The enzyme is located in the bacterial periplasm where its likely function is to provide protection against toxic peroxides. The soluble 323-residue single polypeptide chain contains two covalent c-type haems with very different properties: one of them is a low-potential (-330 mV) centre where ...
| Known for Crystal Structure | Haem Cytochrome | Pseudomonas Aeruginosa | New Class | Hydrogen Peroxide |
OBJECTIVE: Our purpose was to identify potential differences in gene expression between normal trophoblast and choriocarcinoma cells.
METHODS: The Atlas human cDNA expression array hybridization technique was used to study the gene expression pattern in normal trophoblast and choriocarcinoma cell lines. Furthermore, to confirm heat shock protein-27 (Hsp-27) expression data, reverse transcriptase-PCR (RT-PCR), Western blot, and immunohistochemical analyses were used in vitro with cell ...
| Known for Cell Lines | Gene Expression | Heat Shock | Human Trophoblast | Western Blot |
The identification of enzymes responsible for oxidation of lignin in lignin-degrading bacteria is of interest for biotechnological valorization of lignin to renewable chemical products. The genome sequences of two lignin-degrading bacteria, Ochrobactrum sp., and Paenibacillus sp., contain no B-type DyP peroxidases implicated in lignin degradation in other bacteria, but contain putative multicopper oxidase genes. Multi-copper oxidase CueO from Ochrobactrum sp. was expressed and ...
| Known for Bacterial Lignin | Copper Oxidase | Crystal Structure | Genome Sequences | Catalytic Activity |
Breech presentation: its predictors and consequences. An analysis of the Hungarian Tauffer Obstetric Database (1996–2011)
[ PUBLICATION ]
INTRODUCTION: Breech presentation is linked to abnormal pregnancy outcomes. However, the causality of this association is unknown. We aimed to investigate predictors of term breech presentation and pregnancy outcomes of breech presentation.
MATERIAL AND METHODS: Using a Hungarian registry, all term (≥ 37 weeks), singleton pregnancies with cephalic, and breech presentation in 1996-2011 were analyzed (n = 41 796). Covariates were maternal medical history and data on the present pregnancy. ...
| Known for Breech Presentation | Newborn Infant | 95 Confidence Interval | Maternal Age | Pregnancy Outcome |
The central tunnel of the eight-bladed beta-propeller domain of cytochrome cd1 (nitrite reductase) is seen, from a 1.28 A resolution structure, to contain hydrogen donors and acceptors that are satisfied by interaction either with water or the d1 haem. The d1 haem, although bound by an extensive network of hydrogen bonds, is not distorted in its binding pocket and is confirmed to have exactly the dioxoisobacteriochlorin structure proposed from chemical studies. A biological rationale is ...
| Known for Cytochrome Cd1 | Nitrite Reductase | D1 Haem | Methanol Dehydrogenase | Amino Acid |
The anatomy of a bifunctional enzyme: Structural basis for reduction of oxygen to water and synthesis of nitric oxide by cytochrome cd1
[ PUBLICATION ]
Cytochrome cd1-nitrite reductase is a bifunctional enzyme that catalyzes the one-electron reduction of nitrite to nitric oxide and the four-electron reduction of oxygen to water. The 1.55 A crystal structure of the dimeric enzyme from Thiosphaera pantotropha is reported here. The protein was sequenced from the X-ray structure. Each subunit contains a covalent c heme with two axial His ligands (His-17, His-69) and a unique noncovalent d1 heme ligated by Tyr-25 and His-200. The d1 heme is ...
| Known for Nitric Oxide | Cytochrome Cd1 | Structural Basis | Bifunctional Enzyme | Chemical Models |
Evolution of Substrate Specificity in a Recipient’s Enzyme Following Horizontal Gene Transfer
[ PUBLICATION ]
Despite the prominent role of horizontal gene transfer (HGT) in shaping bacterial metabolism, little is known about the impact of HGT on the evolution of enzyme function. Specifically, what is the influence of a recently acquired gene on the function of an existing gene? For example, certain members of the genus Corynebacterium have horizontally acquired a whole l-tryptophan biosynthetic operon, whereas in certain closely related actinobacteria, for example, Mycobacterium, the trpF gene ...
| Known for Substrate Specificity | Horizontal Gene Transfer | Hgt Evolution | Enzyme Function | Trpf Gene |
BACKGROUND: Cytochrome c peroxidase from yeast is a soluble haem-containing protein found in the mitochondrial electron transport chain where it probably protects against toxic peroxides. The aim of this study was to obtain a reliable structure for the doubly oxidized transient intermediate (termed compound I) in the reaction of cytochrome c peroxidase with hydrogen peroxide. This intermediate contains a semistable free radical on Trp191, and an oxyferryl haem group.
RESULTS: Compound I ...
| Known for Laue Diffraction | Peroxidase Compound | Hydrogen Peroxide | Yeast Cytochrome | Radical Site |
Key People For Normal Placenta
Vilmos Fülöp:Expert Impact
Concepts for whichVilmos Fülöphas direct influence:Normal placenta, Complete mole, Prolyl oligopeptidase, Breech presentation, Active site, Crystal structure, Molar pregnancy, Nitrite reductase.
Vilmos Fülöp:KOL impact
Concepts related to the work of other authors for whichfor which Vilmos Fülöp has influence:Crystal structure, Prolyl oligopeptidase, Active site, Nitrite reductase, Electron transfer, Nitric oxide, Amino acid.
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