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Title: Characterization of SNAG-zinc finger protein (ZFP) transcription factors.
Creator: Chiang, Cindy Chung-Yue., Charles E. Schmidt College of Science, Department of Biological Sciences
Abstract/Description: Transcriptional regulation is an important area of research due to the fact that it leads to gene expression. Transcription factors associated with the regulation can either be activators or repressors of target genes, acting directly or with the aid of other factors. A majority of transcriptional repressors are zinc finger proteins (ZFPs) which bind to specific DNA sequences. The Snail/Gfi (SNAG) domain family, with members such as Slug, Smuc, Snail, and Scratch, are transcriptional...
Show moreTranscriptional regulation is an important area of research due to the fact that it leads to gene expression. Transcription factors associated with the regulation can either be activators or repressors of target genes, acting directly or with the aid of other factors. A majority of transcriptional repressors are zinc finger proteins (ZFPs) which bind to specific DNA sequences. The Snail/Gfi (SNAG) domain family, with members such as Slug, Smuc, Snail, and Scratch, are transcriptional repressors shown to play a role in various diseases such as cancer. The SNAG transcription factors contain a conserved SNAG repression domain and DNA binding domain zinc fingers. The specific DNA sequences to which each SNAG-ZFP binds, as well as a general consensus -TGCACCTGTCCGA, have been determined. Also, putative protein-protein interactions in which the Slug domain participates has been identified via binding assays. All these results contribute to better understanding of SNAG-ZFP functions.
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Date Issued: 2009
PURL: http://purl.flvc.org/FAU/186676
Subject Headings: Zinc-finger proteins, Synthesis, Metalloproteins, Synthesis, Genetic transcription, Regulation, Cellular signal transduction, Gene expression
Format: Document (PDF)

Title: A comprehensive study of mammalian SNAG transcription family members.
Creator: Chiang, Cindy Chung-Yue., Charles E. Schmidt College of Science, Department of Biological Sciences
Abstract/Description: Transcriptional regulation by the family of SNAG (Snail/Gfi-1) zinc fingers has been shown to play a role in various developmental states and diseases. These transcriptional repressors have function in both DNA- and protein-binding, allowing for multiple interactions by a single family member. This work aims to characterize the SNAG members Slug, Smuc, Snail, Scratch, Gfi-1, Gfi-1B, and IA-1 in terms of both DNA-protein and protein-protein interactions. The specific DNA sequences to which the...
Show moreTranscriptional regulation by the family of SNAG (Snail/Gfi-1) zinc fingers has been shown to play a role in various developmental states and diseases. These transcriptional repressors have function in both DNA- and protein-binding, allowing for multiple interactions by a single family member. This work aims to characterize the SNAG members Slug, Smuc, Snail, Scratch, Gfi-1, Gfi-1B, and IA-1 in terms of both DNA-protein and protein-protein interactions. The specific DNA sequences to which the zinc finger regions bind were determined for each member, and a general consensus of TGCACCTGTCCGA, was developed for four of the members. Via these studies, we also reveal thebinding affinities of E-box (CANNTG) sequences to the members, since this core is found for multiple members' binding sites. Additionally, protein-protein interactions of SNAG members to other biological molecules were investigated. The Slug domain and Scratch domain have unknown function, yet through yeast two-hybrid screening, we were able to determine protein interaction partners for them as well as for other full length SNAG members. These protein-interacting partners have suggested function as corepressors during transcriptional repression. The comprehensive information determined from these studies allow for a better understanding of the functional relationship between SNAG-ZFPs and other genes. The collected data not only creates a new profile for each member investigated, but it also allows for further studies to be initiated from the results.
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Date Issued: 2012
PURL: http://purl.flvc.org/fcla/dt/3342041
Subject Headings: Cellular signal transduction, Zinc-finger proteins, Synthesis, Metalloproteins, Synthesis, Genetic transcription, Regulation
Format: Document (PDF)

Title: Molecular characterization of a subset of KRAB-ZFPs.
Creator: Chamoun, Alain., Charles E. Schmidt College of Science, Department of Biological Sciences
Abstract/Description: There are approximately 20,000 genes in the human genome. Around 2% of these genes code for transcriptional repressors known as KRAB-ZFPs. It is already known that Zinc-Finger Proteins contain two main functional domains at either end of the polypeptide. In today's database, you will find a KRAB (Kruppell-associated Box) domain at one end and a tandem array of Zinc-finger repeats at the other end. The carboxyl terminal tandem Zinc-finger repeats function as sequence-specific DNA-binding...
Show moreThere are approximately 20,000 genes in the human genome. Around 2% of these genes code for transcriptional repressors known as KRAB-ZFPs. It is already known that Zinc-Finger Proteins contain two main functional domains at either end of the polypeptide. In today's database, you will find a KRAB (Kruppell-associated Box) domain at one end and a tandem array of Zinc-finger repeats at the other end. The carboxyl terminal tandem Zinc-finger repeats function as sequence-specific DNA-binding domains. The amino terminal KRAB domain serves as a repressor domain, which will recruit a co-repressor termed KAP-1 (KRAB Associated Protein-1). Located in between these two domains is a region of uncharacterized DNA referred to as the "Linker Region". This thesis will explore the DNA-binding domains of 6 known KRAB-ZFPs, as well as utilize the linker regions to derive an evolutionary history for this superfamily.
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Date Issued: 2010
PURL: http://purl.flvc.org/FAU/2684313
Subject Headings: Zinc-finger proteins, Synthesis, Metalloproteins, Synthesis, Genetic transcription, Regulation, Gene expression
Format: Document (PDF)

Title: A role for polynucleotide phosphorylase in protecting cells and controlling RNA quality under oxidative stress.
Creator: Wu, Jinhua., Charles E. Schmidt College of Science, Department of Biological Sciences
Abstract/Description: RNA damage occurring under oxidative stress has been shown to cause RNA dysfunction and must be detrimental to cells and organisms. We propose that damaged RNA can be removed by specific RNA surveillance activities. In this work, we investigated the role of polynucleotide phosphorylase (PNPase), a 3'->5' exoribonuclease, in protecting the cells against oxidative stress and eliminating oxidatively-damaged RNA. Previously, it was reported that E. coli PNPase has a higher affinity to poly(8-oxoG...
Show moreRNA damage occurring under oxidative stress has been shown to cause RNA dysfunction and must be detrimental to cells and organisms. We propose that damaged RNA can be removed by specific RNA surveillance activities. In this work, we investigated the role of polynucleotide phosphorylase (PNPase), a 3'->5' exoribonuclease, in protecting the cells against oxidative stress and eliminating oxidatively-damaged RNA. Previously, it was reported that E. coli PNPase has a higher affinity to poly(8-oxoG:A). We further confirmed that E. coli PNPase can specifically bind to an oxidized RNA with a high affinity. An E. coli strain deficient in PNPase (pnp) is hypersensitive to hydrogen peroxide (H2O2). Importantly, the level of H2O2-induced RNA damage, measured by the content of 8-hydroxyguanosine, increases significantly in the pnp mutant cells. Consistent with the notion that PNPase plays a direct role in these processes, introduction of the pnp gene encoding E. coli PNPase can restore the viability and RNA oxidation level of the pnp mutant cells in response to H2O2 treatment. Interestingly, degradosome-association is not required for PNPase to protect cell against oxidative stress. PNPase is evolutionary conserved in most of organisms of all domains of life. The human polynucleotide phosphorylase (hPNPase) localizes mainly in mitochondria and plays pleiotropic roles in cell differentiation and has been previously shown to bind 8- oxoG-RNA with a high affinity. Here we show that similar to E. coli PNPase, hPNPase plays an indispensable role in protecting HeLa cells against oxidative stress. The viability in HeLa cell and 8-oxoG levels in RNA are inversely correlated in response to H2O2- treatment. After removal of oxidative challenge, the elevated level of 8-oxoG in RNA decreases, suggesting the existence of surveillance mechanism(s) for cleaning up oxidized RNA., We have shown that hPNPase may be responsible for the surveillance of oxidized RNA in mammalian cells.Overexpresion of hPNPase reduces RNA oxidation and increases HeLa cell viability against H2O2 insult. Conversely, hPNPase knockdown decreases the viability and increases 8-oxoG level in HeLa cells exposed to H2O2. Taken together, our results suggest that RNA oxidation is a challenging problem for living organisms, and PNPase may play an important role in protecting both prokaryotic and eukaryotic cells by limiting damage to RNA under oxidative stress.
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Date Issued: 2008
PURL: http://purl.flvc.org/FAU/186302
Subject Headings: RNA, Metabolism, Biopolymers, Physiological transport, Bacterial genetics, Proteins, Synthesis, Cellular signal transduction
Format: Document (PDF)

Title: Structure-function relationships in eukaryotic and prokaryotic family 6 glycosyltransferases.
Creator: Tumbale, Percy., Charles E. Schmidt College of Medicine, Department of Biomedical Science
Abstract/Description: Carbohydrate Active Enzyme family 6 (CA6) glycosyltransferases (GTs) are type II transmembrane proteins localized in the Golgi apparatus. CA6 GTs have a GT-A fold, a type of structure that resembles the Rossman fold and catalyze the transfer either galactose (Gal) or N-acetylgalactosamine (GalNAc) from the UDP nucleotide sugar to an non-reducing terminal Gal or GalNAc on an acceptor via an a-1,3 linkage. In this reaction, the anomeric configuration of the sugar moiety of the donor is retained...
Show moreCarbohydrate Active Enzyme family 6 (CA6) glycosyltransferases (GTs) are type II transmembrane proteins localized in the Golgi apparatus. CA6 GTs have a GT-A fold, a type of structure that resembles the Rossman fold and catalyze the transfer either galactose (Gal) or N-acetylgalactosamine (GalNAc) from the UDP nucleotide sugar to an non-reducing terminal Gal or GalNAc on an acceptor via an a-1,3 linkage. In this reaction, the anomeric configuration of the sugar moiety of the donor is retained in the product. CA6 GTs includes the histo-blood group A and B GTs, a-galactosyltransferase (a3GT), Forssman glycolipid synthase (FS), isogloboside 3 synthase (iGb3) in mammals. a3GT and its products (a-Gal epitode) are present in most mammals but are absent in humans and old world primates because of inactivating mutations. The absence of a3GT and its products results in the production of anti-a-Gal epitope natural antibodies in these species., Up to date, the catalytic mechanisms of the CA6 GTs are not well understood. Based on previous structural and mutagenesis studies of bovine aB3GT, we investigated active site residues (His315, Asp316, Ser318, His319, and Lys359) that are highly conserved among CA6 GTs. We have also investigated the role of the C-terminal region by progressive C-terminal truncations. Findings from these studies clarify the functional roles of these residues in structure, catalysis, and specificity in these enzymes and have implications for their catalytic mechanisms. GTs are useful tools in synthesis of glycans for various applications in science and medicine. Methods for the large scale production of pure glycans are continuously being developed. We created a limited randomized combinatorial library based on knowledge of structural information and sequence analysis of the enzyme and its mammalian homologues., Two GalNAc-specific variants were identified from the library and one Glc-specific variant was identified by site-direct mutagenesis. The glycosyltransferase activities of these variants are expected to be improved by further screens of libraries which are designed using the variants as templates. The mammalian CA6 GTs that have been characterized to date are metal-independent and require the divalent cation, Mn2+ for activity. In some recently-discovered bacterial CA6 GTs, the DXD sequence that is present in eukaryotic GTs is replaced by NXN. We cloned and expressed one of these proteins from Bacteroides ovatus, a bacterium that has been linked with inflammatory bowel disease. Functional characterization shows it is a metal-independent monomeric GT that efficiently catalyzes the synthesis of oligosaccharides similar to human blood group A glycan., Mutational studies indicated that despite the lack of a metal cofactor there are similarities in structure-function relationships between the bacterial and vertebrate family 6 GTs.
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Date Issued: 2009
PURL: http://purl.flvc.org/FAU/186686
Subject Headings: Molecular biology, Mathematical models, Glycotransferase genes, Biological transport, Proteins, Synthesis, Evolutionary genetics
Format: Document (PDF)

Title: Molecular characterization of ARID and DDT domain.
Creator: MacDonald, Emmanuel., Charles E. Schmidt College of Science, Department of Biological Sciences
Abstract/Description: Transcriptional regulation of genes is vital to cell success making it an important aspect of research. Transcriptional regulation can occur in many ways; transcription factors bind to the promoter region and block transcription, disrupt an activator protein, or interact with histones to lead to higher order chromatin. Plant HomeoDomain can recognize and bind to different methylation states of histone tails. PHD proteins use other functional regions to carry out functions. Two associated...
Show moreTranscriptional regulation of genes is vital to cell success making it an important aspect of research. Transcriptional regulation can occur in many ways; transcription factors bind to the promoter region and block transcription, disrupt an activator protein, or interact with histones to lead to higher order chromatin. Plant HomeoDomain can recognize and bind to different methylation states of histone tails. PHD proteins use other functional regions to carry out functions. Two associated domains having DNA-binding capacity were characterized in this study; the ARID domains of JARID1A and JARID1C and the DDT domains of BAZ1A, BAZ1B and BAZ2A. These genes are important because of their roles in various diseases such as cancer. The consensus sequences for BAZ1A-DDT is GGACGGRnnGG, GnGAGRGCRnnGGnG, RAGGGGGRnG and CRYCGGT. Consensus sequences for BAZ1B-DDT were CGnCCAnCTTnTGGG and YGCCCCTCCCCnR. Consensus sequences for BAZ2A-DDT were TACnnAGCnY and CnnCCRGCnRTGnYY. Consensus sequence for JARID1A-ARID was GnYnGCGYRCYnCnG. Consensus sequences for JARID1C-ARID was RGGRGCCRGGY.
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Date Issued: 2010
PURL: http://purl.flvc.org/FAU/2705077
Subject Headings: Genetic transcription, Regulation, Transcription factors, Zinc-finger proteins, Synthesis, Cellular signal transduction, Gene expression
Format: Document (PDF)

Title: Metalloprotease Profiling in Melanoma.
Creator: Giricz, Orsolya, Florida Atlantic University, Fields, Gregg B., Charles E. Schmidt College of Science, Department of Chemistry and Biochemistry
Abstract/Description: The proteolytic activities of the ADAM (a disintegrin and metalloproteinase), ADAMTS (a disintegrin and metalloproteinases with thrombospondin motifs) and MMP (matrix metalloproteinase) protein families play important roles in normal and multiple pathological conditions. These metalloproteases have potential implications in the degradation of the extracellular matrix and in the processing of bioactive molecules. Under pathological conditions these proteases are involved in many diverse...
Show moreThe proteolytic activities of the ADAM (a disintegrin and metalloproteinase), ADAMTS (a disintegrin and metalloproteinases with thrombospondin motifs) and MMP (matrix metalloproteinase) protein families play important roles in normal and multiple pathological conditions. These metalloproteases have potential implications in the degradation of the extracellular matrix and in the processing of bioactive molecules. Under pathological conditions these proteases are involved in many diverse processes from tumor cell migration to cartilage destruction in rheumatoid arthritis. In the present study, the gene expression levels of six ADAMs, eight MMPs, and four ADAMTSs were analyzed by Real Time PCR. RNA was isolated from multiple normal fibroblast and metastatic melanoma cell lines, as well as the isogenic normal tissue and tumor samples. This method allowed for detected changes in mRNA expressiOn of the individual metalloproteainase genes to be compared between normal and metastatic states, and also between tissue and cultured cells. Substantial differences have been observed in the level of ADAM and MMP mRNA expression between tissue and cell lines. In general, the level of expression is several folds higher in cultured cells compared to the isogenic tissue they are derived from. Protein microarrays were utilized in order to evaluate the correlations between MMP and TIMP mRNA copy numbers and protein abundance in cell culture. In several cases, distinct differences were observed regarding the localization of the proteins examined. In order to determine if the metalloprotease genes that were elevated at the level of RNA expression produce functional proteins, the foundations of an in situ FRET assay have been established. This will greatly aid in a better understanding of the behavior of metallopeptidases in a cellular context.
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Date Issued: 2008
PURL: http://purl.flvc.org/fau/fd/FA00000859
Subject Headings: Tumor markers--Research, Metalloproteinases--Inhibitors, Melanoma--Research, Proteins--Synthesis, Genetic translation
Format: Document (PDF)

Title: Study of the Coupling Between Transcription and mRNA Processing Utilizing a Novel Bcl-x Mini-gene.
Creator: Devanney, Sean C., Caputi, Massimo, Florida Atlantic University
Abstract/Description: The Bel family of genes are fundamental to the apoptotic mechanism. Bcl-x a member of this family, is alternatively spliced to create two main isoforms a long (Bcl-xL) and a short (Bcl-xS) variant. The long form exhibits anti-apoptotic activity, while the short form favors apoptosis. The proper balance of expression of these two isoforms is crucial for several developmental processes such as thymic selection and neural reshaping. A number of cancer types have been shown to over-express the...
Show moreThe Bel family of genes are fundamental to the apoptotic mechanism. Bcl-x a member of this family, is alternatively spliced to create two main isoforms a long (Bcl-xL) and a short (Bcl-xS) variant. The long form exhibits anti-apoptotic activity, while the short form favors apoptosis. The proper balance of expression of these two isoforms is crucial for several developmental processes such as thymic selection and neural reshaping. A number of cancer types have been shown to over-express the long form, thereby granting them some protection from apoptosis. To study the transcriptional and post-transcriptional mechanisms regulating gene expression, the Bcl-x gene has been utilized. A complex mini-gene construct has been create in order to monitor the effects that promoter sequences, 5'UTR and 3'UTR's have on mRNA splicing, RNA export, stability and translation. Abundant evidence exists indicating that RNA processing events such as transcription, splicing and export are coupled, yet the mechanisms and factors involved in regulating these processes are poorly understood. The mini-gene is identical to the endogenous gene with the exception of a deletion to the 50Kb intron and the addition of a tag to differentiate the mini-gene product from the endogenous mRNA and protein. This novel system allows for the study of transcriptional and post-transcriptional mechanisms regulating gene expression from RNA biogenesis on to the protein level.
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Date Issued: 2007
PURL: http://purl.flvc.org/fau/fd/FA00000741
Subject Headings: Genetic transcription, Proteins--Synthesis, Messenger RNA, Gene expression, Oncogenes--Research
Format: Document (PDF)

Title: Study on the Role oftmRNA in Protecting Escherichia coli Cell Under Oxidative stress.
Creator: Kollipara, Gayatri, Li, Zhongwei, Florida Atlantic University, Charles E. Schmidt College of Medicine, Department of Biomedical Science
Abstract/Description: tmRNA is a small stable RNA present in Eubacteria. Through a mechanism called trans-translation, tmRNA mediates ribosome rescue and quality control of proteins and mRNA. In this study, the Escherichia coli (E. coli) mutant lacking tmRNA was demonstrated hypersensitive to oxidative stress. The role of tmRNA-mediated surveillance mechanism in protecting E. coli cell under oxidative stress condition was examined. The tmRNA-mediated tagged protein levels were elevated in cells under oxidative...
Show moretmRNA is a small stable RNA present in Eubacteria. Through a mechanism called trans-translation, tmRNA mediates ribosome rescue and quality control of proteins and mRNA. In this study, the Escherichia coli (E. coli) mutant lacking tmRNA was demonstrated hypersensitive to oxidative stress. The role of tmRNA-mediated surveillance mechanism in protecting E. coli cell under oxidative stress condition was examined. The tmRNA-mediated tagged protein levels were elevated in cells under oxidative stress condition, demonstrating the enhanced need for tmRNA under such condition. Our results suggest that mRNA damage by oxidative stress may cause reduced cell viability, and that tmRNA is required to rescue cells under such condition. Furthermore, our observations showed that tmRNA is required for the optimal growth of E. coli under normal aeration but not under anaerobic condition, suggesting that oxidation ofmRNA is the major reason for requirement oftmRNA during normal aeration.
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Date Issued: 2007
PURL: http://purl.flvc.org/fau/fd/FA00000782
Subject Headings: Proteins--Synthesis, Bacterial genetics, Escherichia coli infections, Cells--Evolution
Format: Document (PDF)

Title: Comprehensive study of the ZAD family of zinc finger transcription factors in Drosophila melanogaster.
Creator: Krystel, Joseph., Charles E. Schmidt College of Science, Department of Biological Sciences
Abstract/Description: The zinc finger associated domain (ZAD) family of transcription factors from Drosophila melanogaster is not well described in the literature, in part because it is very difficult to study by traditional mutagenesis screens. Bioinformatic studies indicate this is due to overlapping functions remaining after a recent evolutionary divergence. I set out to use in vitro-binding techniques to identify the characteristics of the ZAD family and test this theory. I have constructed glutathione S...
Show moreThe zinc finger associated domain (ZAD) family of transcription factors from Drosophila melanogaster is not well described in the literature, in part because it is very difficult to study by traditional mutagenesis screens. Bioinformatic studies indicate this is due to overlapping functions remaining after a recent evolutionary divergence. I set out to use in vitro-binding techniques to identify the characteristics of the ZAD family and test this theory. I have constructed glutathione S-transferase (GST)-ZAD domain chimeric proteins for use in pull down protein binding assays,and GST-Zinc finger (ZnF) array domain chimera for electrophoretic mobility shift assays (EMSA). Protein binding assays indicated two putative conserved interactors, similar to the analogous KRAB system in mammals. ... Competitive bindings were carried out to show a specificity of binding conferred by the identified conserved positions. While the consensus binding sites show relatively few similarities, the predicted target genes identified by the consensus binding sites show significant overlap. The nature of this overlap conforms to the known characteristics of the ZAD family but points to a more positive selection to maintain conservation of function.
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Date Issued: 2012
PURL: http://purl.flvc.org/FAU/3355627
Subject Headings: Cellular signal transduction, Drosophila melanogaster, Cytogenetics, Transcription factors, Zinc-finger proteins, Synthesis, Genetic transcription, Regulation, Gene expression
Format: Document (PDF)

Title: Elucidation of the features of the zinc finger associated domain (ZAD) family of transportation factors in Drosophila melanogaster.
Creator: Krystel, Joseph., Charles E. Schmidt College of Science, Department of Biological Sciences
Abstract/Description: The zinc finger associated domain (ZAD) containing family of transcription factors is not well described in the literature, in part because it is very difficult to study by mutagenesis. We used in vitro-binding techniques to identify characteristics of the ZAD family, by constructing glutathione Stransferase (GST)-ZAD domain chimeric proteins for use in protein binding assays, and GST-Zinc finger array domain chimera for binding site selections. Protein binding assays indicated a possible...
Show moreThe zinc finger associated domain (ZAD) containing family of transcription factors is not well described in the literature, in part because it is very difficult to study by mutagenesis. We used in vitro-binding techniques to identify characteristics of the ZAD family, by constructing glutathione Stransferase (GST)-ZAD domain chimeric proteins for use in protein binding assays, and GST-Zinc finger array domain chimera for binding site selections. Protein binding assays indicated a possible shared cofactor, as seen in the analogous KRAB system in mammals. DNA binding assays have provided a consensus binding sequence for five of the ZAD proteins, consistent with previously reported work on ZAD and unpublished work on mammalian transcription factors. Research is ongoing with an additional ~50 ZAD proteins to more fully map the binding characters of ZAD proteins.
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Date Issued: 2009
PURL: http://purl.flvc.org/FAU/186768
Subject Headings: Cellular signal transduction, Drosophila melanogaster, Cytogenetics, Transcription factors, Zinc-finger proteins, Synthesis, Genetic transcription, Regulation, Gene expression
Format: Document (PDF)

Title: Identification of longitudinals lacking (LOLA) target genes in Drosophila melanogaster.
Creator: Qureshi, Bazila., Charles E. Schmidt College of Science, Department of Biological Sciences
Abstract/Description: Longitudinals lacking gene (LOLA) is a transcription factor that is involved in a variety of axon guidance decisions in Drosophila melanogaster nervous system. Besides having a role as an epigenetic silencer and in the programmed cell death in Drosophila's ovary, this gene is also an example of complex transcription unit. LOLA is a transcription repressor and can generate 17 DNA - binding isoforms, through alternative splicing, each containing distinct zinc-finger proteins. This unique...
Show moreLongitudinals lacking gene (LOLA) is a transcription factor that is involved in a variety of axon guidance decisions in Drosophila melanogaster nervous system. Besides having a role as an epigenetic silencer and in the programmed cell death in Drosophila's ovary, this gene is also an example of complex transcription unit. LOLA is a transcription repressor and can generate 17 DNA - binding isoforms, through alternative splicing, each containing distinct zinc-finger proteins. This unique DNAbinding binding sequence to which LOLA-ZFP binds has been determined for four of the lola isoforms F, J, P and K. Also, bioinformatics' tool approach has been taken to identify the target genes that are regulated by these four LOLA splice variants. Future work will be done for the five other LOLA isoforms to categorize their putative DNA-binding sequences and subsequently their protein interactions.
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Date Issued: 2010
PURL: http://purl.flvc.org/FAU/2684893
Subject Headings: Transcription factors, Cellular signal transduction, Zinc-finger proteins, Synthesis, Genetic transcription, Regulation, Drosophila melanogaster, Cytogenetics, Gene expression
Format: Document (PDF)

Synthesis (9)	+ -
Genetic transcription (8)	+ -
Cellular signal transduction (7)	+ -
Gene expression (7)	+ -
Regulation (7)	+ -

Zinc-finger proteins (7)	+ -
Transcription factors (4)	+ -
Cytogenetics (3)	+ -
Drosophila melanogaster (3)	+ -
Metalloproteins (3)	+ -
Proteins--Synthesis (3)	+ -
Bacterial genetics (2)	+ -
Proteins (2)	+ -
Biological transport (1)	+ -
Biopolymers (1)	+ -
Cells--Evolution (1)	+ -
Escherichia coli infections (1)	+ -
Evolutionary genetics (1)	+ -
Genetic translation (1)	+ -
Glycotransferase genes (1)	+ -
Mathematical models (1)	+ -
Melanoma--Research (1)	+ -
Messenger RNA (1)	+ -
Metabolism (1)	+ -
Metalloproteinases--Inhibitors (1)	+ -
Molecular biology (1)	+ -
Oncogenes--Research (1)	+ -
Physiological transport (1)	+ -
RNA (1)	+ -
Tumor markers--Research (1)	+ -

Charles E. Schmidt College of Science (9)	+ -
Department of Biological Sciences (8)	+ -
Florida Atlantic University (3)	+ -
Charles E. Schmidt College of Medicine (2)	+ -
Chiang, Cindy Chung-Yue. (2)	+ -

Department of Biomedical Science (2)	+ -
Krystel, Joseph. (2)	+ -
Caputi, Massimo (1)	+ -
Chamoun, Alain. (1)	+ -
Department of Chemistry and Biochemistry (1)	+ -
Devanney, Sean C. (1)	+ -
Fields, Gregg B. (1)	+ -
Giricz, Orsolya (1)	+ -
Kollipara, Gayatri (1)	+ -
Li, Zhongwei (1)	+ -
MacDonald, Emmanuel. (1)	+ -
Qureshi, Bazila. (1)	+ -
Tumbale, Percy. (1)	+ -
Wu, Jinhua. (1)	+ -

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