Other search tools

About this data

The publication data currently available has been vetted by Vanderbilt faculty, staff, administrators and trainees. The data itself is retrieved directly from NCBI's PubMed and is automatically updated on a weekly basis to ensure accuracy and completeness.

If you have any questions or comments, please contact us.

Results: 1 to 10 of 19

Publication Record

Connections

Metals in Biology 2016: Molecular Basis of Selection of Metals by Enzymes.
Guengerich FP
(2016) J Biol Chem 291: 20838-20839
MeSH Terms: Enzymes, Metalloproteins, Metals
Show Abstract · Added March 14, 2018
This ninth Metals in Biology Thematic Series deals with the fundamental issue of why certain enzymes prefer individual metals. Why do some prefer sodium and some prefer potassium? Is it just the size? Why does calcium have so many regulatory functions? Why do some proteins have an affinity for zinc? How is the homeostasis of calcium and zinc achieved? How do enzymes discriminate between the similar metals magnesium and manganese? Four Minireviews address these and related questions about metal ion preferences in biological systems.
© 2016 by The American Society for Biochemistry and Molecular Biology, Inc.
0 Communities
1 Members
0 Resources
3 MeSH Terms
Introduction: Metals in Biology: METALS AT THE HOST-PATHOGEN INTERFACE.
Guengerich FP
(2015) J Biol Chem 290: 18943-4
MeSH Terms: Animals, Homeostasis, Host-Pathogen Interactions, Humans, Metalloproteins
Show Abstract · Added March 14, 2018
This seventh Metals in Biology Thematic Series deals with the metal-based interactions of mammalian hosts with pathogens. Both pathogens and hosts have complex regulatory systems for metal homeostasis. Understanding these provides strategies for fighting pathogens, either by excluding essential metals from the microbes, by delivery of excess metals to cause toxicity, or by complexing metals in microorganisms. Intervention is possible by delivery of complexing reagents or by targeting the microbial regulatory apparatus.
© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.
0 Communities
1 Members
0 Resources
5 MeSH Terms
Thematic minireview series: metals in biology 2013.
Guengerich FP
(2013) J Biol Chem 288: 13164
MeSH Terms: Animals, Biology, Humans, Metalloproteins, Review Literature as Topic, Trace Elements
Show Abstract · Added March 7, 2014
One-half of the available protein structures contain metals, explaining their roles as essential trace elements. Metals are also critical in many aspects of nucleic acid biochemistry. This prologue briefly introduces the fifth of the Thematic Series on Metals in Biology, which began in the Journal of Biological Chemistry in 2009. The five minireviews in this 2013 series deal with the molybdenum prosthetic group (a pterin known as Moco); the biosynthesis of the "M-cluster" molybdenum prosthetic group of nitrogenase; the biosynthesis of the nickel-based metallocenter of the enzyme urease; several of the processing, transport, and medical aspects of cobalamins; and the growing roles of heme sensor proteins.
0 Communities
1 Members
0 Resources
6 MeSH Terms
Functional interactions between Lmo2, the Arf tumor suppressor, and Notch1 in murine T-cell malignancies.
Treanor LM, Volanakis EJ, Zhou S, Lu T, Sherr CJ, Sorrentino BP
(2011) Blood 117: 5453-62
MeSH Terms: Adaptor Proteins, Signal Transducing, Animals, Cell Transformation, Neoplastic, Cocarcinogenesis, Cyclin-Dependent Kinase Inhibitor p16, DNA-Binding Proteins, Disease Progression, Female, Gene Expression, LIM Domain Proteins, Loss of Heterozygosity, Male, Metalloproteins, Mice, Mice, Inbred C57BL, Mice, Knockout, Mice, Transgenic, Mutation, Neoplastic Stem Cells, Precursor Cells, T-Lymphoid, Precursor T-Cell Lymphoblastic Leukemia-Lymphoma, Promoter Regions, Genetic, Receptor, Notch1, Signal Transduction
Show Abstract · Added May 27, 2014
LMO2 is a target of chromosomal translocations in T-cell tumors and was activated by retroviral vector insertions in T-cell tumors from X-SCID patients in gene therapy trials. To better understand the cooperating genetic events in LMO2-associated T-cell acute lymphoblastic leukemia (T-ALL), we investigated the roles of Arf tumor suppressor loss and Notch activation in murine models of transplantation. Lmo2 overexpression enhanced the expansion of primitive DN2 thymocytes, eventually facilitating the stochastic induction of clonal CD4(+)/CD8(+) malignancies. Inactivation of the Arf tumor suppressor further increased the self-renewal capacity of the primitive, preleukemic thymocyte pool and accelerated the development of aggressive, Lmo2-induced T-cell lympholeukemias. Notch mutations were frequently detected in these Lmo2-induced tumors. The Arf promoter was not directly engaged by Lmo2 or mutant Notch, and use of a mouse model in which activation of a mutant Notch allele depends on previous engagement of the Arf promoter revealed that Notch activation could occur as a subsequent event in T-cell tumorigenesis. Therefore, Lmo2 cooperates with Arf loss to enhance self-renewal in primitive thymocytes. Notch mutation and Arf inactivation appear to independently cooperate in no requisite order with Lmo2 overexpression in inducing T-ALL, and all 3 events remained insufficient to guarantee immediate tumor development.
0 Communities
1 Members
0 Resources
24 MeSH Terms
Murine leukemias with retroviral insertions at Lmo2 are predictive of the leukemias induced in SCID-X1 patients following retroviral gene therapy.
Davé UP, Akagi K, Tripathi R, Cleveland SM, Thompson MA, Yi M, Stephens R, Downing JR, Jenkins NA, Copeland NG
(2009) PLoS Genet 5: e1000491
MeSH Terms: Adaptor Proteins, Signal Transducing, Animals, Base Sequence, DNA, Neoplasm, DNA-Binding Proteins, Genetic Therapy, Hematopoietic Stem Cell Transplantation, Humans, Interleukin Receptor Common gamma Subunit, LIM Domain Proteins, Leukemia, Experimental, Leukemia-Lymphoma, Adult T-Cell, Metalloproteins, Mice, Mice, SCID, Models, Genetic, Molecular Sequence Data, Mutagenesis, Insertional, Proto-Oncogene Proteins, Retroviridae, Transplantation, Autologous, Virus Integration, X-Linked Combined Immunodeficiency Diseases
Show Abstract · Added March 5, 2014
Five X-linked severe combined immunodeficiency patients (SCID-X1) successfully treated with autologous bone marrow stem cells infected ex vivo with an IL2RG-containing retrovirus subsequently developed T-cell leukemia and four contained insertional mutations at LMO2. Genetic evidence also suggests a role for IL2RG in tumor formation, although this remains controversial. Here, we show that the genes and signaling pathways deregulated in murine leukemias with retroviral insertions at Lmo2 are similar to those deregulated in human leukemias with high LMO2 expression and are highly predictive of the leukemias induced in SCID-X1 patients. We also provide additional evidence supporting the notion that IL2RG and LMO2 cooperate in leukemia induction but are not sufficient and require additional cooperating mutations. The highly concordant nature of the genetic events giving rise to mouse and human leukemias with mutations at Lmo2 are an encouraging sign to those wanting to use mice to model human cancer and may help in designing safer methods for retroviral gene therapy.
0 Communities
2 Members
0 Resources
23 MeSH Terms
Regulation of LMO2 mRNA and protein expression in erythroid differentiation.
Brandt SJ, Koury MJ
(2009) Haematologica 94: 447-8
MeSH Terms: Adaptor Proteins, Signal Transducing, Cell Differentiation, DNA-Binding Proteins, Erythrocytes, Erythropoiesis, Gene Expression Regulation, Humans, LIM Domain Proteins, Metalloproteins, Proto-Oncogene Proteins, RNA, Messenger
Added March 19, 2014
0 Communities
1 Members
0 Resources
11 MeSH Terms
Mammary tumors initiated by constitutive Cdk2 activation contain an invasive basal-like component.
Corsino PE, Davis BJ, Nørgaard PH, Parker NN, Law M, Dunn W, Law BK
(2008) Neoplasia 10: 1240-52
MeSH Terms: Animals, Breast Neoplasms, Cadherins, Catenins, Cell Adhesion Molecules, Cell Line, Tumor, Cyclin D1, Cyclin-Dependent Kinase 2, Female, Humans, Immunoblotting, Immunohistochemistry, Intermediate Filament Proteins, Mammary Neoplasms, Experimental, Mammary Tumor Virus, Mouse, Metalloproteins, Mice, Mice, Transgenic, Microscopy, Fluorescence, Neoplasm Invasiveness, Nerve Tissue Proteins, Nestin, Phosphoproteins, Protein Transport, Stress Fibers, Zyxin, beta Catenin
Show Abstract · Added April 24, 2015
The basal-like subtype of breast cancer is associated with invasiveness, high rates of postsurgical recurrence, and poor prognosis. Aside from inactivation of the BRCA1 tumor-suppressor gene, little is known concerning the mechanisms that cause basal breast cancer or the mechanisms responsible for its invasiveness. Here, we show that the heterogeneous mouse mammary tumor virus-cyclin D1-Cdk2 (MMTV-D1K2) transgenic mouse mammary tumors contain regions of spindle-shaped cells expressing both luminal and myoepithelial markers. Cell lines cultured from these tumors exhibit the same luminal/myoepithelial mixed-lineage phenotype that is associated with human basal-like breast cancer and express a number of myoepithelial markers including cytokeratin 14, P-cadherin, alpha smooth muscle actin, and nestin. The MMTV-D1K2 tumor-derived cell lines form highly invasive tumors when injected into mouse mammary glands. Invasion is associated with E-cadherin localization to the cytoplasm or loss of E-cadherin expression. Cytoplasmic E-cadherin correlates with lack of colony formation in vitro and beta-catenin and p120(ctn) localization to the cytoplasm. The data suggest that the invasiveness of these cell lines results from a combination of factors including mislocalization of E-cadherin, beta-catenin, and p120(ctn) to the cytoplasm. Nestin expression and E-cadherin mislocalization were also observed in human basal-like breast cancer cell lines, suggesting that these results are relevant to human tumors. Together, these results suggest that abnormal Cdk2 activation may contribute to the formation of basal-like breast cancers.
1 Communities
0 Members
0 Resources
27 MeSH Terms
Molecular profiling indicates avian branchiomotor nuclei invade the hindbrain alar plate.
Ju MJ, Aroca P, Luo J, Puelles L, Redies C
(2004) Neuroscience 128: 785-96
MeSH Terms: Animals, Body Patterning, Cadherins, Chick Embryo, Eye Proteins, Gene Expression Regulation, Developmental, Hedgehog Proteins, Homeodomain Proteins, Immunohistochemistry, In Situ Hybridization, Interferon Type I, Metalloproteins, Neurons, PAX6 Transcription Factor, PAX7 Transcription Factor, Paired Box Transcription Factors, Pregnancy Proteins, RNA, Messenger, Repressor Proteins, Reverse Transcriptase Polymerase Chain Reaction, Rhombencephalon, Spinal Cord, Trans-Activators, Transcription Factors
Show Abstract · Added November 5, 2010
It is generally believed that the spinal cord and hindbrain consist of a motor basal plate and a sensory alar plate. We now have molecular markers for these territories. The relationship of migrating branchiomotor neurons to molecularly defined alar and basal domains was examined in the chicken embryo by mapping the expression of cadherin-7 and cadherin-6B, in comparison to genetic markers for ventrodorsal patterning (Otp, Pax6, Pax7, Nkx2.2, and Shh) and motoneuron subpopulations (Phox2b and Isl1). We show cadherin-7 is expressed in a complete radial domain occupying a lateral region of the hindbrain basal plate. The cadherin-7 domain abuts the medial border of Pax7 expression; this common limit defines, or at least approximates, the basal/alar boundary. The hindbrain branchiomotor neurons originate in the medial part of the basal plate, close to the floor plate. Their cadherin-7-positive axons grow into the alar plate and exit the hindbrain close to the corresponding afferent nerve root. The cadherin-7-positive neuronal cell bodies later translocate laterally, following this axonal trajectory, thereby passing through the cadherin-7-positive basal plate domain. Finally, the cell bodies traverse the molecularly defined basal/alar boundary and move into positions within the alar plate. After the migration has ended, the branchiomotor neurons switch expression from cadherin-7 to cadherin-6B. These findings demonstrate that a specific subset of primary motor neurons, the branchiomotor neurons, migrate into the alar plate of the chicken embryo. Consequently, the century-old concept that all primary motor neurons come to reside in the basal plate should be revised.
0 Communities
0 Members
1 Resources
24 MeSH Terms
Gene therapy insertional mutagenesis insights.
Davé UP, Jenkins NA, Copeland NG
(2004) Science 303: 333
MeSH Terms: Adaptor Proteins, Signal Transducing, Animals, DNA-Binding Proteins, Gene Expression, Genetic Therapy, Genetic Vectors, Humans, LIM Domain Proteins, Leukemia, T-Cell, Metalloproteins, Mice, Mutagenesis, Insertional, Proto-Oncogene Proteins, Receptors, Interleukin-2, Retroviridae, Severe Combined Immunodeficiency, Virus Integration
Added March 5, 2014
0 Communities
1 Members
0 Resources
17 MeSH Terms
Rap1 couples cAMP signaling to a distinct pool of p42/44MAPK regulating excitability, synaptic plasticity, learning, and memory.
Morozov A, Muzzio IA, Bourtchouladze R, Van-Strien N, Lapidus K, Yin D, Winder DG, Adams JP, Sweatt JD, Kandel ER
(2003) Neuron 39: 309-25
MeSH Terms: Animals, Antirheumatic Agents, Bacterial Proteins, Behavior, Animal, Blotting, Western, Colforsin, Conditioning (Psychology), Cues, Cyclic AMP, Electric Stimulation, Electrophysiology, Excitatory Postsynaptic Potentials, Gene Expression Regulation, Enzymologic, Hippocampus, Immunoenzyme Techniques, In Situ Hybridization, Interleukin 1 Receptor Antagonist Protein, Long-Term Potentiation, Memory, Metalloproteins, Mice, Mice, Transgenic, Mitogen-Activated Protein Kinase 1, Mitogen-Activated Protein Kinase 3, Mitogen-Activated Protein Kinases, Mutation, Neuronal Plasticity, Prosencephalon, Proto-Oncogene Proteins B-raf, Proto-Oncogene Proteins c-raf, RNA, Messenger, Reaction Time, Sialoglycoproteins, Signal Transduction, Subcellular Fractions, Synapses, Synaptic Transmission, Tetanus, Theta Rhythm, Valine, rap1 GTP-Binding Proteins
Show Abstract · Added May 19, 2014
Learning-induced synaptic plasticity commonly involves the interaction between cAMP and p42/44MAPK. To investigate the role of Rap1 as a potential signaling molecule coupling cAMP and p42/44MAPK, we expressed an interfering Rap1 mutant (iRap1) in the mouse forebrain. This expression selectively decreased basal phosphorylation of a membrane-associated pool of p42/44MAPK, impaired cAMP-dependent LTP in the hippocampal Schaffer collateral pathway induced by either forskolin or theta frequency stimulation, decreased complex spike firing, and reduced the p42/44MAPK-mediated phosphorylation of the A-type potassium channel Kv4.2. These changes correlated with impaired spatial memory and context discrimination. These results indicate that Rap1 couples cAMP signaling to a selective membrane-associated pool of p42/44MAPK to control excitability of pyramidal cells, the early and late phases of LTP, and the storage of spatial memory.
0 Communities
1 Members
0 Resources
41 MeSH Terms