Showing 1 – 20 of 52
Relevance | Newest | Oldest |
  • JAMA April 27, 2011

    Figure 1: Cellular Localization of CTNNB1 (β-Catenin) and the WNT-CTNNB1 Signaling Pathway

    A, When the WNT signaling pathway is not activated, CTNNB1 is associated primarily with the plasma membrane. CTNNB1 in the cytoplasm binds to a destruction complex formed by AXIN, APC, and the kinases GSK3B and CSNK1A1. Phosphorylation of CTNNB1 in the destruction complex is followed by ubiquitylation and eventual proteosomal degradation. B, Activation of the WNT signaling pathway, as by the presence of WNT, inactivates the destruction complex. CTNNB1 accumulates in the cytoplasm and is translocated into the nucleus, where it acts as a coactivator of transcription of target genes that promote tumor progression. APC indicates adenomatous polyposis coli; BTRC, β-transducing repeat containing; CCND1, cyclin D1; CDH1, cadherin 1; CSNK1A1, casein kinase 1 α 1; CTNNB1, cadherin-associated protein β 1 (β-catenin); DVL, dishevelled homolog (Drosophila); FZD, frizzled homolog 1 (Drosophila); GSK3B, glycogen synthase kinase 3 β; LEF, lymphoid enhancer–binding factor; LRP, low-density lipoprotein receptor–related protein; MYC, v-myc myelocytomatosis viral oncogene homolog (avian); TCF, transcription factor; TLE, transducin-like enhancer of split 1 (E(sp1) homolog, Drosophila); WNT, wingless-type MMTV integration site family.
  • Metaphysical Games: An Imaginary Lecture on Crafting Earth's Biological Future

    Abstract Full Text
    JAMA. 2005; 294(11):1415-1417. doi: 10.1001/jama.294.11.1415
  • Doggy DNA Has Its Day

    Abstract Full Text
    JAMA. 2003; 289(23):3080-3080. doi: 10.1001/jama.289.23.3080-a
  • JAMA November 14, 2001

    Figure 3: Prominent Differentiating Features in the Domain Architectures of Representative Human Proteins

    A protein domain is a structural and functional unit that shows evolutionary conservation and, by convention, is represented as a distinct geometric shape. Thus, proteins are made up of 1 or more such building blocks or "domains" and, depending on the types and numbers of domains, proteins with different biological capabilities are created. Many of these domains have seemingly arbitrary nomenclature that, in many cases, reflects the experimental nuances of their initial description. A library of curated protein domains with their biological descriptions is available through the Pfam and SMART databases.A, The extensive domain shuffling seen in the plasma proteases of the coagulation and complement systems. The "ancient" trypsin family serine protease domain occurs in combination with a myriad of protein interaction domains. Most of these domains are evolutionarily ancient, that is, with the exception of the Gla domain (see below); they are also observed in the fly and the worm. These include: (1) AP: Apple, originally described in the coagulation factors, predicted to possess protein- and/or carbohydrate-binding functions; (2) Kr: Kringle, named after a Danish pastry, has an affinity for lysine-containing peptides; (3) E: epidermal growth factor (EGF)-like; (4) CUB: domain first described in complement proteins and a diverse group of developmental proteins; (5) CCP: complement control protein repeats, also known as "sushi" repeats, first recognized in the complement proteins; and (6) Gla: a hyaluron-binding domain, contains γ-carboxyglutamate residues, and is seen in proteins associated with the extracellular matrix. Of note is the observation that apolipoprotein (a) likely represents a primate-specific evolutionary event. There is a tremendous expansion of the Kringle domain (dashed segment represents a total of 29 copies of the Kringle domain) in a trypsin family serine protease.B, Examples of domain accretion in nuclear regulators in the human compared with the fly. Domain accretion refers to greater numbers of a specific domain in a multidomain protein or addition of new domains to a multidomain protein. These domains include: (1) BTB: broad-complex, tramtrack, and bric-a-brac (a name that reflects its early descriptions in Drosophila), a protein interaction domain; (2) Zf: C2H2 class of DNA-binding zinc finger; (3) KRAB: Kruppel-associated box, a vertebrate-specific nuclear protein interaction domain; (4) HD: histone deacetylase, an important class of chromatin-modifying enzymes; (5) U: ubiquitin finger, a domain that targets proteins for proteolytic degradation. There is a major expansion of the numbers of C2H2 zinc fingers in the BTB or KRAB transcription factor (dashed segment represents a total of 3 copies of the Zf domain) families in the human, a feature that may reflect increased ability to mediate regulatory interactions with DNA.
  • Research With Drosophila Provides Clues to Enhancing Human Memory

    Abstract Full Text
    JAMA. 2000; 284(22):2857-2858. doi: 10.1001/jama.284.22.2857
  • JAMA December 13, 2000

    Figure: Research With Drosophila Provides Clues to Enhancing Human Memory

    This teaching machine is used to isolate memory mutants—flies that cannot associate an odor with electric shock—among the Drosophila studied. About 100 flies enter it at one time.
  • Lords of the Fly Decode Drosophila Genome

    Abstract Full Text
    JAMA. 2000; 283(12):1554-1555. doi: 10.1001/jama.283.12.1554-JMN0322-2-1
  • JAMA March 22, 2000

    Figure: Lords of the Fly Decode Drosophila Genome

    Gerald Rubin, PhD, led the Drosophila Genome Project Group at the University of California, Berkeley, effort to decode the fruit fly genome. The group teamed up with Celera Genomics in Rockville, Md, to sequence virtually the entire genome of the fruit fly. (Photo credit: Paul Fetters for Howard Hughes Medical Institute)
  • Fruit Fly Genome

    Abstract Full Text
    JAMA. 1999; 281(11):978-978. doi: 10.1001/jama.281.11.978-JHA90001-3-1
  • Circadian Clock Boosts Stress-Response Genes During Aging

    Abstract Full Text
    JAMA. 2017; 317(13):1307-1307. doi: 10.1001/jama.2017.3108
  • Ensuring an Innovative and Productive Future for the Next Generation of Scientists: The 2016 Lasker-Koshland Special Achievement Award in Medical Science

    Abstract Full Text
    JAMA. 2016; 316(12):1256-1257. doi: 10.1001/jama.2016.13884

    In this Viewpoint, Lasker Award winner Bruce Albert discusses the current discouraging climate for young investigators seeking funding for basic science research, and the importance of incentivizing innovative research from young scientists.

  • From Egg to Organism: Studies on Embryonic Pattern Formation

    Abstract Full Text
    JAMA. 1991; 266(13):1848-1849. doi: 10.1001/jama.1991.03470130128046
  • Tackling Breast Cancers Resistant to Hormone Therapy

    Abstract Full Text
    JAMA. 2015; 314(17):1788-1788. doi: 10.1001/jama.2015.13935
  • A Guinea Pig's View of Research

    Abstract Full Text
    JAMA. 1982; 247(2):213-213. doi: 10.1001/jama.1982.03320270049026
  • Supporting Biomedical Research: Meeting Challenges and Opportunities at HHMI

    Abstract Full Text
    free access
    JAMA. 2015; 313(2):133-135. doi: 10.1001/jama.2014.16543

    This Viewpoint discusses how the Howard Hughes Medical Institute is responding the challenges and opportunities related to the training of patient-oriented physician-scientists.

  • JAMA October 16, 2013

    Figure 1: Schematic Diagram of Anabolic and Catabolic Pathways Involved in Muscle Protein Homeostasis

    AKT indicates protein kinase B; 4EBP-1, eukaryotic translation initiation factor 4E-binding protein; eEF2, eukaryotic elongation factor 2; eIF2B, eukaryotic initiation factor 2; eIF4E, eukaryotic initiation factor 4E; FOXO-1, forkhead box class O-1; GSK3β, glycogen synthase kinase 3β; IGF1-R, insulin-like growth factor 1 receptor; IκBα, inhibitor of nuclear factor κBα; IKK, inhibitor of nuclear factor κB kinase; IRS1, insulin receptor substrate 1; MAFBx, muscle atrophy f-box-1; mTOR, mammalian target of rapamycin; MURF-1, muscle ring finger protein 1; NFκB, nuclear factor κB; P70s6K, 70-kDa s6 protein kinase; PI3K, phosphoinositide 3-kinase; PIP2, phosphatidylinositol 4,5-bisphosphate, phosphatidylinositol 3,4,5-trisphosphate; PIP3, phosphatidylinositol 3,4,5-trisphosphate; PTEN, phosphatase and tensin homolog deleted on chromosome 10; RPS6, ribosomal protein S6; SMAD2,3, vertebrate homolog of Drosophila protein MAD (mothers against decapentaplegic) and Caenorhabditis elegans protein SMA 2,3; TNFR1, tumor necrosis factor receptor 1.
  • A History of Genetics

    Abstract Full Text
    JAMA. 1966; 197(8):667-667. doi: 10.1001/jama.1966.03110080107049
  • Genetics

    Abstract Full Text
    JAMA. 1962; 182(4):505-505. doi: 10.1001/jama.1962.03050430179035
  • Ciba Foundation Colloquia on Ageing. Volume 5: The Lifespan of Animals

    Abstract Full Text
    JAMA. 1960; 173(8):968-969. doi: 10.1001/jama.1960.03020260108026
  • Ciba Foundation Symposium on Chemistry and Biology of Pteridines

    Abstract Full Text
    JAMA. 1955; 158(9):798-798. doi: 10.1001/jama.1955.02960090092028