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1.

001-es BibID:BIBFORM075319
035-os BibID:(WoS)000473691900004 (Scopus)85067353429
Első szerző:Budis, Jaroslav
Cím:Combining count- and length-based z-scores leads to improved predictions in non-invasive prenatal testing / Budis Jaroslav, Gazdarica Juraj, Radvanszky Jan, Szucs Gabor, Kucharik Marcel, Strieskova Lucia, Gazdaricova Iveta, Harsanyova Maria, Duris Frantisek, Minarik Gabriel, Sekelska Martina, Nagy Balint, Turna Jan, Szemes Tomas
Dátum:2019
ISSN:1367-4803
Megjegyzések:Motivation: Non-invasive prenatal testing or NIPT is currently among the top researched topic in obstetric care. While the performance of the current state-of-the-art NIPT solutions achieve high sensitivity and specificity, they still struggle with a considerable number of samples that cannot be concluded with certainty. Such uninformative results are often subject to repeated blood sampling and re-analysis, usually after two weeks, and this period may cause a stress to the future mothers as well as increase the overall cost of the test. Results: We propose a supplementary method to traditional z-scores to reduce the number of such uninformative calls. The method is based on a novel analysis of the length profile of circulating cell free DNA which compares the change in such profiles when random-based and length-based elimination of some fragments is performed. The proposed method is not as accurate as the standard z-score; however, our results suggest that combination of these two independent methods correctly resolves a substantial portion of healthy samples with an uninformative result. Additionally, we discuss how the proposed method can be used to identify maternal aberrations, thus reducing the risk of false positive and false negative calls. Availability: The open-source code of the proposed methods, together with test data, is freely available for non-commercial users at github web page https://github.com/jbudis/lambda.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
non-invasive
prenatal
testing
improved
Megjelenés:Bioinformatics. - 35 : 8 (2019), p. 1284-1291. -
További szerzők:Gazdarica, Juraj Radvanszky, Jan Szűcs Gábor Kucharik, Marcel Strieskova, Lucia Gazdaricova, Iveta Harsanyova, Maria Duris, Frantisek Minarik, Gabriel Sekelska, Martina Nagy Bálint (1956-) (molekuláris genetikus) Turna, Jan Szemes, Tomas (1980-) (biológus)
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2.

001-es BibID:BIBFORM079797
035-os BibID:(WoS)000475910500002 (Scopus)85069472612
Első szerző:Csősz Éva (biokémikus, molekuláris biológus)
Cím:Analysis of networks of host proteins in the early time points following HIV transduction / Éva Csősz, Ferenc Tóth, Mohamed Mahdi, George Tsaprailis, Miklós Emri, József Tőzsér
Dátum:2019
ISSN:1471-2105
Megjegyzések:Background: Utilization of quantitative proteomics data on the network level is still a challenge in proteomics data analysis. Currently existing models use sophisticated, sometimes hard to implement analysis techniques. Our aim was to generate a relatively simple strategy for quantitative proteomics data analysis in order to utilize as much of the data generated in a proteomics experiment as possible. Results: In this study, we applied label-free proteomics, and generated a network model utilizing both qualitative, and quantitative data, in order to examine the early host response to Human Immunodeficiency Virus type 1 (HIV-1). A weighted network model was generated based on the amount of proteins measured by mass spectrometry, and analysis of weighted networks and functional sub-networks revealed upregulation of proteins involved in translation, transcription, and DNA condensation in the early phase of the viral life-cycle. Conclusion: A relatively simple strategy for network analysis was created and applied to examine the effect of HIV-1 on host cellular proteome. We believe that our model may prove beneficial in creating algorithms, allowing for both quantitative and qualitative studies of proteome change in various biological and pathological processes by quantitative mass spectrometry.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
weighted network
quantitative proteomics
host response
HIV-1
Megjelenés:Bmc Bioinformatics. - 20 (2019), p. 1-18. -
További szerzők:Tóth Ferenc (1980-) (molekuláris biológus) Mahdi, Mohamed (1979-) (orvos, tudományos segédmunkatárs) Tsaprailis, George Emri Miklós (1962-) (fizikus) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Pályázati támogatás:GINOP-2.3.3-15-2016-00020
GINOP
Bolyai János Kutatói Ösztöndíj
MTA
Felsőoktatási Intézményi Kiválósági Program
Egyéb
NKFI-6, 125238
Egyéb
NIEHS - ES06694
Egyéb
NIH/NCI - CA023074
Egyéb
NIH/NCRR - 1S10 RR028868-01
Egyéb
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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3.

001-es BibID:BIBFORM120789
035-os BibID:(Scopus)85191248548 (WoS)001208395200001
Első szerző:Golda Mária (molekuláris biológus)
Cím:P1' specificity of the S219V/R203G mutant tobacco etch virus protease / Mária Golda, Gyula Hoffka, Scott Cherry, Joseph E. Tropea, George T. Lountos, David S. Waugh, Alexander Wlodawer, József Tőzsér, János András Mótyán
Dátum:2024
ISSN:0887-3585
Megjegyzések:Proteases that recognize linear amino acid sequences with high specificity became indispensable tools of recombinant protein technology for the removal of various fusion tags. Due to its stringent sequence specificity, the catalytic domain of the nuclear inclusion cysteine protease of tobacco etch virus (TEV PR) is also a widely applied reagent for enzymatic removal of fusion tags. For this reason, efforts have been made to improve its stability and modify its specificity. For example, P1' autoproteolytic cleavage-resistant mutant (S219V) TEV PR was found not only to be nearly impervious to self-inactivation, but also exhibited greater stability and catalytic efficiency than the wild-type enzyme. An R203G substitution has been reported to further relax the P1' specificity of the enzyme, however, these results were obtained from crude intracellular assays. Until now, there has been no rigorous comparison of the P1' specificity of the S219V and S219V/R203G mutants in vitro, under carefully controlled conditions. Here, we compare the P1' amino acid preferences of these single and double TEV PR mutants. The in vitro analysis was performed by using recombinant protein substrates representing 20 P1' variants of the consensus TENLYFQ*SGT cleavage site, and synthetic oligopeptide substrates were also applied to study a limited set of the most preferred variants. In addition, the enzyme-substrate interactions were analyzed in silico. The results indicate highly similar P1' preferences for both enzymes, many side-chains can be accommodated by the S1' binding sites, but the kinetic assays revealed lower catalytic efficiency for the S219V/R203G than for the S219V mutant.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
tobacco etch virus
protein structure
molecular dynamics
fusion tag removal
enzymology
TEV protease
protease
Proteolysis
Megjelenés:Proteins-Structure Function And Bioinformatics. - 92 : 9 (2024), p. 1085-1096. -
További szerzők:Hoffka Gyula (1992-) (vegyész) Cherry, Scott Tropea, Joseph E. Lountos, George T. Waugh, David S. Wlodawer, Alexander Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész) Mótyán János András (1981-) (biokémikus, molekuláris biológus)
Pályázati támogatás:TKP2021-EGA-20
Egyéb
ÚNKP-23-5-DE-486
Egyéb
BO/00110/23/5
MTA
75N91019D00024
Egyéb
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Intézményi repozitóriumban (DEA) tárolt változat
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4.

001-es BibID:BIBFORM040670
Első szerző:Mahalingam, Bhuvaneshwari
Cím:Combining mutations in HIV-1 protease to understand mechanisms of resistance / Mahalingam Bhuvaneshwari, Boross Peter, Wang Yuan-Fang, Louis John M., Fischer Christopher C., Tozser Jozsef, Harrison Robert W., Weber Irene T.
Dátum:2002
ISSN:0887-3585
Megjegyzések:HIV-1 develops resistance to protease inhibitors predominantly by selecting mutations in the protease gene. Studies of resistant mutants of HIV-1 protease with single amino acid substitutions have shown a range of independent effects on specificity, inhibition, and stability. Four double mutants, K45I/L90M, K45I/V82S, D30N/V82S, and N88D/L90M were selected for analysis on the basis of observations of increased or decreased stability or enzymatic activity for the respective single mutants. The double mutants were assayed for catalysis, inhibition, and stability. Crystal structures were analyzed for the double mutants at resolutions of 2.2-1.2 A to determine the associated molecular changes. Sequence-dependent changes in protease-inhibitor interactions were observed in the crystal structures. Mutations D30N, K45I, and V82S showed altered interactions with inhibitor residues at P2/P2', P3/P3'/P4/P4', and P1/P1', respectively. One of the conformations of Met90 in K45I/L90M has an unfavorably close contact with the carbonyl oxygen of Asp25, as observed previously in the L90M single mutant. The observed catalytic efficiency and inhibition for the double mutants depended on the specific substrate or inhibitor. In particular, large variation in cleavage of p6(pol)-PR substrate was observed, which is likely to result in defects in the maturation of the protease from the Gag-Pol precursor and hence viral replication. Three of the double mutants showed values for stability that were intermediate between the values observed for the respective single mutants. D30N/V82S mutant showed lower stability than either of the two individual mutations, which is possibly due to concerted changes in the central P2-P2' and S2-S2' sites. The complex effects of combining mutations are discussed.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Proteins-Structure Function And Bioinformatics. - 48 : 1 (2002), p. 107-116. -
További szerzők:Boross Péter (1972-) (biokémikus, vegyész) Wang, Yuan-Fang Louis, John M. Fischer, Christopher C. Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész) Harrison, Robert W. Weber, Irene T.
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Intézményi repozitóriumban (DEA) tárolt változat
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5.

001-es BibID:BIBFORM126434
Első szerző:Mótyán János András (biokémikus, molekuláris biológus)
Cím:Characterization of the E26H Mutant Schistosoma japonicum Glutathione S-Transferase / Mótyán János András, Nagyné Veres Ágota, Tőzsér József
Dátum:2025
ISSN:0887-3585
Megjegyzések:Glutathione-S-transferase, such as that of Schistosoma japonicum (sjGST) belongs to the most widely utilized fusion tags in the recombinant protein technology. The E26H mutation of sjGST has already been found to remarkably improve its ability for binding divalent ions, enabling its purification with immobilized metal affinity chromatography (IMAC). Nevertheless, most characteristics of this mutant remained unexplored to date. In this study, we performed a comparative analysis of the wild-type and the E26H mutant sjGST by using in vitro as well as in silico approaches. We confirmed that the sjGST(E26H) protein exhibits significantly increased affinity for binding nickel ions as compared to the wild-type. In addition, we proved that the sjGST(E26H) can be purified efficiently either with glutathione- or immobilized metal ion-affinity chromatography, even in consecutive purification steps. The human retroviral-like aspartic protease 1 (ASPRV1) conjugated with the sjGST(E26H) fusion tag was also successfully purified by using both of these affinity chromatographic approaches. Our studies revealed that the E26H mutant sjGST can be used as a versatile affinity tag because the modified protein retains the kinetic features of the wild-type and its affinity towards glutathione, while can be purified efficiently by IMAC, as well.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Schistosoma japonicum
recombinant protein
protein purification
GST
mutagenesis
glutathione S-transferase
fusion tag
affinity chromatography
Megjelenés:Proteins-Structure Function And Bioinformatics. - 93 : 5 (2025), p. 1054-1066. -
További szerzők:Veres Ágota (laboráns) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Pályázati támogatás:TKP2021-EGA-20
Egyéb
ÚNKP-22-2-I-DE-391
Egyéb
ÚNKP-23-5-DE-486
Egyéb
BO/00110/23/5
MTA
University of Debrecen (UD) Program for Scientific Publication
Egyéb
UD Faculty of Medicine Research Fund (Bridging fund)
Egyéb
UD Scientific Research Bridging Fund (DETKA)
Egyéb
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6.

001-es BibID:BIBFORM050899
035-os BibID:PMID:24044430 Article ID: 275
Első szerző:Mótyán János András (biokémikus, molekuláris biológus)
Cím:A molecular model of the full-length human NOD-like receptor family CARD domain containing 5 (NLRC5) protein / János András Mótyán, Péter Bagossi, Szilvia Benkő, József Tőzsér
Dátum:2013
ISSN:1471-2105
Megjegyzések:Pattern recognition receptors of the immune system have key roles in the regulation of pathways after the recognition of microbial- and danger-associated molecular patterns in vertebrates. Members of NOD-like receptor (NLR) family typically function intracellularly. The NOD-like receptor family CARD domain containing 5 (NLRC5) is the largest member of this family that also contains the largest number of leucine-rich repeats (LRRs).Due to the lack of crystal structures of full-length NLRs, projects have been initiated with the aim to model certain or all members of the family, but systematic studies did not model the full-length NLRC5 due to its unique domain architecture.Our aim was to analyze the LRR sequences of NLRC5 and some NLRC5-related proteins and to build a model for the full-length human NLRC5 by homology modeling. RESULTS: LRR sequences of NLRC5 were aligned and were compared with the consensus pattern of ribonuclease inhibitor protein (RI)-like LRR subfamily. Two types of alternating consensus patterns previously identified for RI repeats were also found in NLRC5. A homology model for full-length human NLRC5 was prepared and, besides the closed conformation of monomeric NLRC5, a heptameric platform was also modeled for the opened conformational NLRC5 monomers. CONCLUSIONS: Identification of consensus patterns of leucine-rich repeat sequences helped to identify LRRs in NLRC5 and to predict their number and position within the protein. In spite of the lack of fully adequate template structures, the presence of an untypical CARD domain and unusually high number of LRRs in NLRC5, we were able to construct a homology model for both the monomeric and homo-heptameric full-length human NLRC5 protein.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
NLRC5
Molecular modeling
LRR protein
NOD-like receptor
Megjelenés:BMC Bioinformatics 14 : 1 (2013), p. 1-11. -
További szerzők:Bagossi Péter (1966-2011) (biokémikus, vegyész) Benkő Szilvia (1973-) (molekuláris biológus) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
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7.

001-es BibID:BIBFORM003489
035-os BibID:(scopus)54549105754 (wos)000260487500001
Első szerző:Roszik János (biofizikus)
Cím:AccPbFRET : an ImageJ plugin for semi-automatic, fully corrected analysis of acceptor photobleaching FRET images / Roszik János, Szöllősi János, Vereb György
Dátum:2008
Megjegyzések:The acceptor photobleaching fluorescence resonance energy transfer (FRET) method is widely used for monitoring molecular interactions in cells. This method of FRET, while among those with the simplest mathematics, is robust, self-controlled and independent of fluorophore amounts and ratios. RESULTS: AccPbFRET is a user-friendly, efficient ImageJ plugin which allows fully corrected, pixel-wise calculation and detailed, ROI (region of interest)-based analysis of FRET efficiencies in microscopic images. Furthermore, automatic registration and semi-automatic analysis of large image sets is provided, which are not available in any existing FRET evaluation software. CONCLUSIONS: Despite of the widespread applicability of the acceptor photobleaching FRET technique, this is the first paper where all possible sources of major errors of the measurement and analysis are considered, and AccPbFRET is the only program which provides the complete suite of corrections - for registering image pairs, for unwanted photobleaching of the donor, for cross-talk of the acceptor and/or its photoproduct to the donor channel and for partial photobleaching of the acceptor. The program efficiently speeds up the analysis of large image sets even for novice users and is freely available.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
acceptor photobleaching
FRET
CLSM
software
Megjelenés:BMC Bioinformatics. - 9 : 1 (2008), p. 346. -
További szerzők:Szöllősi János (1953-) (biofizikus) Vereb György (1965-) (biofizikus, orvos)
Internet cím:elektronikus változat
DOI
elektronikus változat
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8.

001-es BibID:BIBFORM116513
035-os BibID:(Scopus)85173464630 (WOS)001077676500001
Első szerző:Sanches, Karoline
Cím:Structure-function relationships in domain peptides : from the sea anemone / Sanches Karoline, Ashwood Lauren M., Olushola-Siedoks Abisola Ave-Maria, Wai Dorothy C. C., Rahman Arfatur, Shakeel Kashmala, Naseem Muhammad Umair, Panyi Gyorgy, Prentis Peter J., Norton Raymond S.
Dátum:2024
ISSN:0887-3585
Megjegyzések:Diverse structural scaffolds have been described in peptides from sea anemones, with the ShKT domain being a common scaffold first identified in ShK toxin from Stichodactyla helianthus. ShK is a potent blocker of voltage-gated potassium channels (KV1.x), and an analog, ShK-186 (dalazatide), has completed Phase 1 clinical trials in plaque psoriasis. The ShKT domain has been found in numerous other species, but only a tiny fraction of ShKT domains has been characterized functionally. Despite adopting the canonical ShK fold, some ShKT peptides from sea anemones inhibit KV1.x, while others do not. Mutagenesis studies have shown that a Lys-Tyr (KY) dyad plays a key role in KV1.x blockade, although a cationic residue followed by a hydrophobic residue may also suffice. Nevertheless, ShKT peptides displaying an ShK-like fold and containing a KY dyad do not necessarily block potassium channels, so additional criteria are needed to determine whether new ShKT peptides might show activity against potassium channels. In this study, we used a combination of NMR and molecular dynamics (MD) simulations to assess the potential activity of a new ShKT peptide. We determined the structure of ShKT-Ts1, from the sea anemone Telmatactis stephensoni, examined its tissue localization, and investigated its activity against a range of ion channels. As ShKT-Ts1 showed no activity against KV1.x channels, we used MD simulations to investigate whether solvent exposure of the dyad residues may be informative in rationalizing and potentially predicting the ability of ShKT peptides to block KV1.x channels. We show that either a buried dyad that does not become exposed during MD simulations, or a partially exposed dyad that becomes buried during MD simulations, correlates with weak or absent activity against KV1.x channels. Therefore, structure determination coupled with MD simulations, may be used to predict whether new sequences belonging to the ShKT family may act as potassium channel blockers.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
molecular dynamics
NMR
peptide
potassium channel
sea anemone
ShKT domain
structure determination
Megjelenés:Proteins-Structure Function And Bioinformatics. - 92 : 2 (2024), p. 192-205. -
További szerzők:Ashwood, Lauren M. Olushola-Siedoks, Abisola Ave-Maria Wai, Dorothy C. C. Rahman, Arfatur Shakeel, Kashmala (1997-) (Molekuláris biológus) Naseem, Muhammad Umair (1993-) (biofizikus, molekuláris biológus) Panyi György (1966-) (biofizikus) Prentis, Peter Norton, Raymond S.
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Intézményi repozitóriumban (DEA) tárolt változat
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9.

001-es BibID:BIBFORM018163
Első szerző:Sebestyén Endre
Cím:DoOPSearch : a web-based tool for finding and analysing common conserved motifs in the promoter regions of different chordate and plant genes / Sebestyén Endre, Nagy Tibor, Suhai Sándor, Barta Endre
Dátum:2009
ISSN:1471-2105
Megjegyzések:The comparative genomic analysis of a large number of orthologous promoter regions of the chordate and plant genes from the DoOP databases shows thousands of conserved motifs. Most of these motifs differ from any known transcription factor binding site (TFBS). To identify common conserved motifs, we need a specific tool to be able to search amongst them. Since conserved motifs from the DoOP databases are linked to genes, the result of such a search can give a list of genes that are potentially regulated by the same transcription factor(s). Results We have developed a new tool called DoOPSearch http://doopsearch.abc.hu webcite for the analysis of the conserved motifs in the promoter regions of chordate or plant genes. We used the orthologous promoters of the DoOP database to extract thousands of conserved motifs from different taxonomic groups. The advantage of this approach is that different sets of conserved motifs might be found depending on how broad the taxonomic coverage of the underlying orthologous promoter sequence collection is (consider e.g. primates vs. mammals or Brassicaceae vs. Viridiplantae). The DoOPSearch tool allows the users to search these motif collections or the promoter regions of DoOP with user supplied query sequences or any of the conserved motifs from the DoOP database. To find overrepresented gene ontologies, the gene lists obtained can be analysed further using a modified version of the GeneMerge program. Conclusion We present here a comparative genomics based promoter analysis tool. Our system is based on a unique collection of conserved promoter motifs characteristic of different taxonomic groups. We offer both a command line and a web-based tool for searching in these motif collections using user specified queries. These can be either short promoter sequences or consensus sequences of known transcription factor binding sites. The GeneMerge analysis of the search results allows the user to identify statistically overrepresented Gene Ontology terms that might provide a clue on the function of the motifs and genes.
Tárgyszavak:Orvostudományok Elméleti orvostudományok konferenciacikk
Megjelenés:Bmc Bioinformatics [electronic resource]. - 10 : Suppl.6. (2009), p. S6. -
További szerzők:Nagy Tibor (Gödöllő) Suhai Sándor Barta Endre (1963-) (molekuláris biológus)
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Intézményi repozitóriumban (DEA) tárolt változat
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10.

001-es BibID:BIBFORM118278
035-os BibID:(Scopus)85183055620 (WoS)001148366700001
Első szerző:Simanjuntak, Masriana Vivi
Cím:Revealing Propolis Potential Activity on Inhibiting Estrogen Receptor and Heat Shock Protein 90 Overexpressed in Breast Cancer by Bioinformatics Approaches / Masriana Vivi Simanjuntak, Muhammad Miftah Jauhar, Putri Hawa Syaifie, Adzani Gaisani Arda, Etik Mardliyati, Wervyan Shalannanda, Beni Rio Hermanto, Isa Anshori
Dátum:2024
ISSN:1177-9322
Megjegyzések:Breast cancer is the most commonly diagnosed cancer globally, with the highest incidence of breast cancer occurring in Asian countries including Indonesia. Among the types of breast cancer, the estrogen receptor (ER)-positive subtype which is prominent with estrogen receptor alpha (ER?) and heat shock protein 90 (HSP90) overexpression genes becomes the most prevalent than the others, approximately 75% of all breast cancer cases. ER? and HSP90 play a role in breast cancer activities including breast tumor growth, invasion, and metastasis mechanism. Propolis, a natural bee product, has been explored for its anticancer activity. However, there is lack of studies that evaluated the potential inhibitor from propolis compounds to the ER? and HSP90 proteins. Therefore, this article focuses on examining the correlation between ER? and HSP90's role in breast cancer and investigating the potential of 93 unique propolis compositions in inhibiting these genes in breast cancer using in silico approaches. This study revealed the positive correlation between ER? and HSP90 genes in breast cancer disease development. Furthermore, we also found novel potential bioactive compounds of propolis against breast cancer through binding with ER? and HSP90; they were 3',4',7-trihydroxyisoflavone and baicalein-7-O-?-D glucopyranoside, respectively. Further research on these compounds is needed to elucidate deeper mechanisms and activity in the real biological system to develop new breast cancer drug treatments.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Breast cancer
estrogen receptor alpha
heat shock protein 90
in silico
propolis
Megjelenés:Bioinformatics and Biology Insights. - 18 (2024), p. 1-19. -
További szerzők:Jauhar, Muhammad Miftah Syaifie, Putri Hawa Arda, Adzani Gaisani Mardliyati, Etik Shalannanda, Wervyan Hermanto, Beni Rio Anshori, Isa
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Intézményi repozitóriumban (DEA) tárolt változat
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11.

001-es BibID:BIBFORM002428
Első szerző:Thallinger, Gerhard G.
Cím:TAMEE : data management and analysis for tissue microarrays / Thallinger G. G., Baumgartner K., Pirklbauer M., Uray M., Pauritsch E., Méhes G., Buck C. R., Zatloukal K., Trajanoski Z.
Dátum:2007
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
külföldön készült közlemény
Megjelenés:BMC Bioinformatics 8 (2007), p. 81-92. -
További szerzők:Baumgartner, Kerstin Pirklbauer, Martin Uray, Martina Pauritsch, Elke Méhes Gábor (1966-) (patológus) Buck, Charles R. Zatloukal, Kurt Trajanoski, Zlatko
Internet cím:elektronikus változat
DOI
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