First name,Last name,Preferred title,Overview,Position,Department,Individual
Vishal,Gohil,Associate Professor,"Despite the fundamental role of the mitochondrion in cellular energy production and its involvement in numerous human diseases, we still do not know the function of nearly 20% of the known mitochondrial proteins. My laboratory applies genomic, genetic, and biochemical tools to uncover the role of these uncharacterized proteins in the mitochondrial respiratory chain (MRC) biogenesis. MRC is the main site of cellular respiration and energy production and since the core components of the MRC are evolutionarily conserved, we reason that the assembly factors required to build the MRC should also be conserved. Therefore, we utilize multiple models systems, including yeast, zebrafish, and human cell lines, to determine the role of these conserved, uncharacterized mitochondrial proteins in bioenergetics, organismal development, and human disease pathogenesis.
Another poorly understood aspect of the mitochondrial energy metabolism is the role of phospholipids in maintaining the structural and functional integrity of the MRC. Although it is well known that the MRC is localized in the inner mitochondrial membrane, how the unique lipid milieu of the mitochondrial membrane influences the assembly and activity of the MRC is not fully understood. We have constructed yeast mutants with defined mitochondrial phospholipid compositions to systematically determine each lipid's role in MRC assembly and activity. Ultimately, defining the roles of mitochondrial proteins and phospholipids will allow us to develop better diagnostic and therapeutic options for human disorders resulting from mitochondrial dysfunction.",Faculty Affiliate||Assistant Professor,Energy Institute||Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n03100e49
Timothy,Devarenne,Associate Professor,"We study the biochemical and molecular mechanisms underlying the control of programmed cell death (PCD) in plants and how PCD is manipulated during plant-pathogen interactions. Specifically we study the interaction between tomato and Pseudomonas syringae pv. tomato (Pst) the causative agent of bacterial spot disease. Resistance to this disease is conferred by the host Pto serine/threonine protein kinase which recognizes Pst strains expressing the type III effector protein AvrPto.
PCD is induced during both resistant and susceptible plant-pathogen interactions. In the case of a resistant interaction, PCD induced by the plant, known as the hypersensitive response (HR), and acts to limit the spread of the pathogen. In susceptible plant-pathogen interactions plant PCD is induced by the pathogen after infection leading to death of the host. Studies have indicated that the genes controlling host PCD during the HR are the same genes that are manipulated by the pathogen during susceptible interactions. The difference lies in the timing of controlling the activity of these genes; HR PCD occurs within 12 hours of pathogen recognition while pathogen-induced PCD occurs several days after infection.
Many of these genes that control plant PCD are serine/threonine (S/T) protein kinase. We are interested in studying a specific class of S/T protein kinases that control PCD in plants called AGC kinases and how they are regulated in both resistant and susceptible plant-pathogen interactions. Additionally, when plants are not attacked by pathogens, PCD is a process that requires constant control so that cell death does not occur. We are looking at the signaling mechanisms and pathways employed to keep PCD under check in non-pathogen challenged plants.",Faculty Affiliate||Associate Professor,Energy Institute||Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n11411275
Jorge,Cruz-Reyes,Professor,"We combine approaches in molecular genetics, structural biology, biochemistry, proteomics, and bioinformatics to study the amazing RNA biology of trypanosome parasites. One research line is on an RNA editing process by uridine insertion and deletion that creates amino acid coding triplets in most mRNAs. Yet a single error in the U-changes yields a frame-shift. Trypanosomes split from other eukaryotic lineages over a hundred million years ago, yet this editing has analogies with RNAi, CRISPR/Cas9, mRNA splicing and other systems directed by small non-coding RNAs (ncRNAs).",Professor||Professor,Texas A&M AgriLife Research||Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n147e77ee
Inna,Krieger,Research Assistant Professor,,Research Assistant Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n1b08b016
Tatyana,Igumenova,,"My laboratory is broadly interested in understanding the structural basis of signal transduction events that occur at the membrane surface. These events are mediated by signaling proteins that reversibly associate with membranes in response to binding second messengers, such as Ca2+ ions, diacylglycerol, and phosphoinositides. One of the key kinases regulating these signal transduction pathways is the Protein Kinase C (PKC) family. Aberrant levels of PKC expression or activity have been implicated in a large number of human diseases, such as cancer, cardiac failure, Alzheimer's disease, and diabetes. Despite the significance of PKC in signal transduction and human health, the structural and dynamical basis of its activation upon binding to lipid membranes remains elusive.",Associate Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n1c6e6632
Xiuren,Zhang,Professor,"Our laboratory focuses on systemic analysis of biochemical, molecular and biological functions of AGO family proteins (AGOs-mics) in genetically tractable Arabidopsis and economically important crops (i.e. rice). We'd like to identify the small RNAs, mRNA targets and protein components which associate with these AGOs. We will study protein/RNA and protein/protein interactions in these RISC assembly events. Our goal is to understand how these AGOs are functionally specialized or redundant corresponding to endogenous development cues and external environmental stimuli. Particularly, we'd like to learn how plants reprogram their gene expression through the small RNAs and AGOs to construct a new cellular niche in responses to environmental challenges and biotic stresses.
Another aspect of our research involves host/virus interaction. Plants take advantage of RNA silencing pathways to defend themselves from exogenous nucleic acid invaders (i.e. viruses). As an anti-host defense mechanism, viruses encode suppressors that can block RNA silencing responses. We have recently demonstrated that CMV 2b disables AGO1 cleavage activity to inhibit RNA silencing and to counter host defense. We are now extending our study to suppressors of several other viruses and the molecular mechanisms of their suppression.",Associate Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n220933ad
Pingwei,Li,Professor,"The research in my lab focuses on elucidating the structural basis of innate immune responses towards microbial nucleic acids. The cGAS/STING pathway plays a central role in innate immunity toward bacterial and viral DNA. cGAS is activated by dsDNA and catalyzes the synthesis of a cyclic dinucleotide cGAMP, which binds to the adaptor STING that mediates the recruitment and activation of protein kinase TBK1 and transcription factor IRF-3. Activated IRF-3 translocates to the nucleus and induces the expression of type I interferons (IFN), an important family of antiviral cytokine. To elucidate the mechanism of cGAS activation, we determined the structures of cGAS in isolation and in complex with DNA. The cGAS/DNA complex structure reveals that cGAS interacts with DNA through two binding sites. Enzyme assays and IFN-? reporter assays of cGAS mutants demonstrate that interactions at both DNA binding sites are essential for cGAS activation. To investigate how cGAMP activates STING, we determined the structures of STING in isolation and in complex with cGAMP. These structures reveal that STING forms a V-shaped dimer and binds cGAMP at the dimer interface. We have also determined the structures of TBK1 in complex with two inhibitors, which show that TBK1 exhibits an I?B kinase fold with distinct domain arrangement. To elucidate the mechanism of IRF-3 recruitment by STING, we determined the structure of a phosphorylated STING peptide bound to IRF-3. To understand how phosphorylation activates IRF-3, we solved the structure of an IRF-3 phosphomimetic mutant bound to CBP, which reveals how phosphorylation induces the dimerization and activation of IRF-3.",Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n31ebad17
Robert,Chapkin,Distinguished Professor,"Research in the Chapkin lab focuses on dietary/microbial modulators related to the prevention of cancer and chronic inflammatory diseases.
Our central goal is to (1) understand cancer chemoprevention at a fundamental level, and (2) to test pharmaceutical agents in combination with dietary/microbial (countermeasures to the Western diet) to more effectively improve gut health and reduce systemic chronic inflammation. Since diet influences gut microbiota composition and metabolite production, to unravel the interrelationships among gut health and the structure of the gut microbial ecosystem, we are in the process of evaluating (using transgenic mouse, Drosophila models and humans) how the gut microbiome modulates intestinal cells, innate immune cells and tumors. As part of this endeavor, we are modeling at the molecular level the dynamic relationship between diet and gut microbe-derived metabolites which modulate chronic inflammation and the hierarchical cellular organization of the intestine, e.g., stem cell niche.",Distinguished Professor||Professor,Biochemistry and Biophysics||Nutrition,https://scholars.library.tamu.edu/vivo/display/n3fbb59f8
Thomas,Meek,Professor,"Marketed drugs have been developed for representatives of all six classes of enzymes, and comprise essential therapies for the treatment of cancers, HIV/AIDS, hypercholesterolemia, and bacterial infections. The availability of known point mutations that are causative of human cancers , as well as the full genomic descriptions of many pathogens, such as parasitic protozoa and infectious bacteria, provides an emerging means to identify new or known enzymes that would constitute potential drug targets. Likewise, the availability of crystal structures of many of these enzymes or their analogues, provides a means to rationally design new inhibitors of enzyme drug targets via the use of molecular modelling and a full understanding of the chemical mechanism of the target enzymes, as an important adjuvant to inhibitor discovery via high-throughput screening.
Our laboratory will initially focus on the detailed study of the mechanisms of cysteine proteases such as cathepsin C, the isocitrate lyase of Mycobacterium tuberculosis, and human ATP-citrate lyase, by the use of pre-steady-state and steady-state kinetics, as well as by use of existing crystal structures of these enzymes, to inform the design of both covalent and other mechanism-based modes for the inactivation of these enzymes. We will design and synthesize candidate inhibitors, and test them against these and other enzyme targets, and determine their suitability as potential drug candidates.",Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n41081941
Dzmitry,Kurouski,Assistant Professor,"My laboratory is broadly interested in elucidation of structural organization of amyloid oligomers using Tip-Enhanced Raman Spectroscopy (TERS).
The ultimate objective of our studies is to unravel structural elements on surfaces of amyloid oligomers that are responsible for their toxicity and propensity to propagate into amyloid fibrils. These findings will help to guide pharmaceutical drug screening efforts towards finding selective blockaders of amyloid fibrillation at the stage where their aggregates are minimally toxic. Finally, resolving the structure of amyloid oligomers will give an inside how to cure Alzheimer's and Parkinson's diseases and dementia.",Assistant Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n43453d43
Paul,Straight,Associate Professor,"Our goal is to understand how microorganisms interact in complex communities. Specifically, we study how small molecules produced in a microbial community affect the growth, development and metabolic output of the organisms. We use a combination of microbiology, genetic, genomic, and biochemical approaches to dissect complex interspecies interactions. Currently, our research focuses on the interactions of the soil bacteria Bacillus subtilis and members of the genus Streptomyces, known for their prolific production of bioactive small molecules and development of aerial structures and spores.",Associate Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n5540637b
Jean-Philippe,Pellois,Professor,"Our goal is to determine how proteins function in space and time in the context of complex cellular networks. We focus on chemistry-driven approaches to manipulate protein structure beyond what is feasible with standard genetics. In particular, we use semi-synthetic light-activatable proteins as biophysical probes to investigate protein mechanisms inside living cells. Areas of interest include the important but poorly understood process of protein S-acylation, signal transduction, and protein trafficking.",Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n5815f42d
Joshua,Wand,Professor and Department Head,"We are broadly interested in how the biophysical properties of proteins are manifested in their biological function. We are particularly engaged in trying to reveal the nature of internal protein motion and how this influences functions ranging from molecular recognition to allostery and catalysis. These basic ideas are being employed in a range of studies including protein engineering to optimize protein drugs, reverse micelle encapsulation to aid fragment-based drug discovery, understanding the regulation of Parkin, which is involved in mitophagy and early onset Parkinson's Disease, and the enzyme AKR1C3, which is central to resistant forms of prostate cancer.",Professor and Department Head,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n6caf5ddd
William,Park,Professor,"Most of our work in the last few years has focused on manipulating starch biosynthesis in plants. This has led to the identification of a number of specific DNA polymorphisms that have a profound impact on the structure and functional properties of starch granules. Interestingly, the effect of some of these polymorphisms is temperature sensitive. For example, a key G/T polymorphism at the 5' leader intron splice site of rice granule bound starch synthase has little phenotypic effect at 18 ?C, but at 25 ?C it activates an alternate splice site that results in a premature open reading frame. At 32 ?C, a third nonconsensus TT/GT splice site is activated. This type of temperature sensitivity is one of the key factors responsible for the complex genotype x environment relationships seen in starch structure and represents a good target for manipulation via biotechnology. We have also worked with an industrial partner and a breeder to develop the first commercial rice varieties specifically tailored to work with a new type of processing technology and to identify the genes responsible for optimal raw material/process interactions. Other work in the laboratory is focused on the identification and manipulation of DNA polymorphisms associated with disease resistance and with herbicide resistance in the wild relatives of crop plants.",Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n7012b9fe
Junjie,Zhang,Associate Professor,"The living cell contains a collection of molecular machines to grow and function. These machines include the ribosomes, the chaperons, the proteasomes and other enzymes. Malfunction of these machines, if occurred in human, are related to many diseases. Understanding their three-dimensional (3D) structures is essential to understand how these machines work in the cell and eventually to treat those related diseases.
Here we use an experimental technique called cryo-electron microscopy (cryo-EM) to image these cellular machines in their native environment at liquid nitrogen temperatures. We then use image processing and graphics techniques to visualize their 3D structures, answering the questions such as how they assemble and how they interact with each other.
In addition, we develop computational modeling tools to interpret and animate these obtained 3D structures to further describe their movements and dynamics.",Associate Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n701e163f
Margaret,Glasner,Associate Professor,"Evolution is the organizing principle of biology and provides the cornerstone of our approach to understand the relationships between protein structure and function. We combine bioinformatics, biochemistry, and genetics to address fundamental questions about protein evolution, such as: What structural and mechanistic features of enzymes increase their capacity to evolve new functions? How do new metabolic pathways evolve? Are there multiple evolutionary pathways to evolve new enzyme activities?
Our primary focus is on how catalytic promiscuity serves as the raw material for evolving new enzyme activities. Catalytic promiscuity is the ability to catalyze different chemical reactions using the same active site. Many enzymes in one branch of the protein family we are studying are catalytically promiscuous, and this activity has been incorporated into new metabolic pathways more than once. Comparing the sequences and structures of these proteins will identify characteristics that permitted them to evolve the second activity.
Our goal is to use results from our research to identify fundamental evolutionary principles that can can help decipher protein structure-function relationships, predict protein functions, and improve protein engineering methods.",Associate Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n721200c3
Elizabeth,Pishko,Lecturer,,Lecturer,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n75e85328
David,Peterson,Professor and Associate Department Head,"We are interested in the molecular mechanisms of transcriptional regulation in mammalian cells. Many of our experiments have focused on the transcription of the proviral genome of the retrovirus mouse mammary tumor virus, which is subject to both positive and negative control. A number of cellular proteins that are important for viral transcription have been identified, and we would like to define the precise roles of these proteins in establishing correct levels of viral gene expression. We are also exploring some specific questions related to the general mechanism of transcription initiation by RNA polymerase II and the biochemical details of transcriptional regulation. In particular, we are developing assays to directly assess effects of transcriptional regulatory proteins on discrete steps in the initiation process, including transcription complex assembly, separation of the two strands of template DNA at the initiation site, and promoter clearance by the polymerase as it begins RNA synthesis.",Professor and Associate Department Head,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n8186cf95
Sumana,Datta,Assistant Provost,"We are currently investigating how organismal level cues regulate the onset of stem cell division during development. Our primary system is the neuroblasts in the brain of the fruit fly, Drosophila melanogaster. The trol gene of Drosophila encodes the fly homolog of the mammalian heparan sulfate glycoprotein, Perlecan. Perlecan is found in mice, humans, and C. elegans, and is widely known as a co-receptor for the growth factor FGF. We have shown that Trol, the Drosophila Perlecan homolog, is required for signaling by FGF. Furthermore, we have demonstrated that Trol is also a likely candidate for the Hedgehog co-receptor. Hedgehogs are peptide growth factors which are conserved in mammals and require heparan sulfate glycoproteins for their movement and long-range signaling; however, until now the identity of the protein core was unknown. Our studies demonstrate genetic interactions between trol and hedgehog or patched mutations (patched is the Hedgehog receptor). Further studies reveal that both FGF and Hedgehog signaling activate stem cell division. Current projects involve determining how Trol stimulates FGF and Hedgehog signaling through genetic, molecular, and biochemical analyses.",Assistant Provost,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n8ce436a7
David,Threadgill,Professor,"Our laboratory uses the mouse as an experimental genetic model to investigate factors that contribute to inter-individual differences in health and disease. Ourcurrent research activities include the identification and functional characterization of alleles contributing to cancer susceptibility, the function of theErbbgenefamily in development and disease, and the role of genetic variation in response to environmental stimuli. To support these investigations, we also aredeveloping new genetic tools to support mammalian systems genetic approaches to phenotypes with complex genetic and environmental etiologies.",Director||Professor||Professor||Professor,Cell Biology and Genetics||Institute of Genome Sciences and Society||Biochemistry and Biophysics||Nutrition,https://scholars.library.tamu.edu/vivo/display/n8ee0b54f
James,Sacchettini,Professor,"My lab uses X-ray crystallography to better understand the relationship between proteins and ligands. Tiny differences in the structure of a molecule can radically change the interaction between a protein and ligand and we are only begining to understand how many factors play a role in this interaction. By manipulating the individual components of a compound it is possible to create a chemical that binds to the protein better than the natural substrate, and prevent the natural reaction from occurring. This is the basis for rational drug design. Our efforts have lead us to collaborations with other labs and scientists in many disciplines as our approach to directed compound design has applications not only in basic research but also in pesticide development, health research and clinical research.",Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n90385563
Chavela,Carr,Lecturer,,Lecturer,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/na40e43dd
Gregory,Reinhart,Professor and Head,"Our laboratory is interested in the mechanisms by which enzymes are regulated in the cell. In particular, we are interested in allosteric regulation of enzyme activity. Consequently, we are interested in understanding the nature of the conformational change in proteins that can be effected by the binding of ligands, and specifically how these changes alter the catalytic behavior of enzymes subject to allosteric regulation. We endeavor to investigate properties that are complementary to those determined by x-ray crystallography in order to develop a comprehensive picture of the structure-function relationships involved in the regulatory phenomenon. For example, we are interested in how the dynamics of protein structure might dictate the nature of an allosteric effect. Techniques and approaches that we use in the laboratory include analysis of enzyme kinetics; analysis of the thermodynamics of enzyme-ligand interactions; time-resolved and steady-state fluorescence spectroscopy; analysis of the effects of temperature and hydrostatic pressure (up to 4 kbar) on enzyme properties, site-specific mutagenesis, isothermal titration calorimetry, and molecular graphics.",Professor and Head,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/na6e2a0db
Stephen,Safe,Distinguished Professor,The aryl hydrocarbon receptor (AhR) is a nuclear helix-loop-helix transcription factor which forms a ligand-induced nuclear heterodimer with the AhR nuclear translocator (Arnt) protein. Research in this laboratory is focused on the molecular mechanism of crosstalk between the AhR and estrogen receptor (ER) signaling pathways in which the AhR inhibits estrogen-induced gene expression. The antiestrogenic activities of some AhR agonists are also being developed as drugs for clinical treatment of breast and endometrial cancers in women. Research on estrogen-dependent gene expression in various cancer cell lines is focused on analysis of several gene promoters to determine the mechanisms of ERa and ERb action. This includes several genes that are activated through interactions of the ER with Sp1 protein and other DNA-bound transcription factors.,Distinguished Professor||Distinguished Professor||Syd Kyle Chair,School of Veterinary Medicine and Biomedical Sciences||Biochemistry and Biophysics||Veterinary Physiology and Pharmacology,https://scholars.library.tamu.edu/vivo/display/nb20fdbd9
Jae,Cho,Assistant Professor,"Our research interests lie in the interface between biology and other areas of science (chemistry and physics). NMR is our primary tool for structural and biophysical analysis. We also extensively use other techniques including Circular Dichroism and Fluorescence spectroscopy, and Isothermal calorimetry. These biophysical analyses are corroborated by sophisticated engineering and tuning of target proteins using semi-synthetic chemical biology techniques, in addition to traditional molecular biology methods.",Assistant Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/ncfe16216
Michael,Manson,Professor,"Bacteria have a limited behavioral repertoire. Their most conspicuous behavior is chemotaxis - the pursuit of molecules that are favorable to acquire and the avoidance of chemicals that are best to avoid. The simplicity of bacterial motility and chemotaxis and the amenability of the model species Escherichia coli to genetic, biochemical and physiological manipulation have facilitated rapid advances in understanding the molecular mechanisms of biological energy conversion and signal transduction.
Our laboratory studies the inputs and outputs of chemotaxis. Ligands interact with the periplasmic receptor domain of a chemotactic signal transducer that spans the cell membrane. This interaction is converted into an intracellular signal that is communicated to the flagella. Molecules can be sensed either by binding directly to a receptor or by first interacting with a periplasmic binding protein, which then interacts with a receptor.",Professor||Professor,Biology||Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/ne190242a
Hays,Rye,Associate Professor,"A fundamental principle of biology is the use of chemical energy in the form of ATP to assemble, disassemble and alter macromolecular structure. Specialized control proteins known as molecular chaperones are often responsible for this activity and have been recognized in recent years to be essential for regulating many aspects of cellular biology. Using a variety of biophysical and biochemical techniques, the Rye lab focuses on three fundamental cellular processes that require molecular chaperones: (1) protein folding (2) protein disaggregation and (3) vesicle trafficking. In each of these cases, large quantities ATP are burned, resulting in molecular organization in the case of protein folding, and molecular disassembly and remodeling in the case of protein disaggregation and vesicle trafficking. We are interested in understanding the detailed biophysical mechanisms that underpin these events. Why are these processes so energetically expensive? Are there any similarities in how the energy is used between these very different molecular processes? Are there general principles of energy transduction in biology that can be gleaned by comparing these examples with other molecular machines, such as cytoskeletal motors? Understanding how molecular chaperones control protein and membrane organization will provide key insights into not only basic cell biology, but will also illuminate aspects of many diseases that spring from aberrant protein and membrane dynamics.",Associate Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/ne7fb85e1
Ryland,Young,Professor,"Most bacterial viruses (phages) cause lysis of their host cell to release the progeny virions. Large phages elaborate an enzyme (""endolysin"") to degrade the cell wall and also a small membrane protein (""holin""). The holin accumulates in the membrane and then, at a precisely scheduled time, suddenly forms a hole to allow release of endolysin through the cytoplasmic membrane to gain access to the wall. We use molecular genetics and biochemistry to study how this small protein is able to act as a molecular ""clock"" and punch holes in membranes. Small phages make single proteins which cause host lysis in a different way. This strategy is to target the host cell wall synthesis machinery; that is, the virus makes a ""protein antibiotic"" that causes lysis in the same way as antibiotics like penicillin by inhibiting an enzyme in the multi-step pathway of murein biosynthesis. Thus, when the infected cell tries to divide, it blows up, or lyses, because it can't make the new cell wall between the daughter cells. Remarkably, each of three different, small phages blocks a different step in the pathway. These small lysis proteins are models for a completely new class of antibacterial antibiotics. Also, the E. coli SlyD protein is required for this mode of lysis in one case. SlyD is a member of an ubiquitous family of proteins related to human ""immunophilins,"" the targets of immune-suppression drugs. We study SlyD to learn about the role of this class of proteins in biology.",Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/nea775348
John,Mullet,Professor,"Functional genomics, bioinformatics, and DNA chip technology are fundamentally changing research on biological systems. Knowledge of complete genome sequences and high resolution genome technology provide an extraordinary opportunity to understand complex biological processes and to relate detailed understanding of protein structure and biochemical mechanism to the function of whole organisms and biological systems in nature.
Our research team is helping to build genome maps and DNA diagnostic microarrays/chips for analysis of global gene expression and biodiversity. This new technology is being used to explore the molecular basis of several fundamental plant responses: (1) light responsive genetic systems that help protect plants from damage by high intensity UV/blue light; (2) genetic systems that allow plants to adapt to the environment; (3) genes and signal transduction pathways that help protect plants from insects and disease; and (4) genes that regulate plant development (flowering time, fertility restoration, chloroplast development/number).",Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/nf1c81fcb