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  • Worm Findings May Offer Clues to Blocking Reperfusion Injury

    Abstract Full Text
    JAMA. 2013; 310(5):470-470. doi: 10.1001/jama.2013.178404
  • Scientists Celebrate Successes, New Tools in Fight Against Human Parasitic Worms

    Abstract Full Text
    JAMA. 2013; 310(1):19-20. doi: 10.1001/jama.2013.7665
  • Helminth Infections and HIV

    Abstract Full Text
    JAMA. 2012; 308(11):1081-1081. doi: 10.1001/2012.jama.11948
  • The Voyage Continues: Darwin and Medicine at 200 Years

    Abstract Full Text
    JAMA. 2009; 301(6):663-665. doi: 10.1001/jama.2009.102
  • JAMA October 17, 2007

    Figure: Elephantiasis Parasite Genome

    Scientists have produced a draft genome of Brugia malayi, a parasitic worm that causes lymphatic filariasis, or elephantiasis.
  • JAMA July 3, 2002

    Figure: Reference Magnetic Resonance Images for Classifying White Matter Lesions (Grades 1-8)

    Grading of white matter lesions (WMLs) was based on the total volume of periventricular and subcortical white matter signal abnormalities on spin density–weighted axial images. The reference images above are example slices derived from complete scans showing successively increasing WMLs ranging from barely detectable, discontinuous lesions located along the periventricular rim (grade 1), progressing to thick, continuous, shaggy lesions along the periventricular rim with mild subcortical involvement (grade 4), and finally to confluent periventricular lesions and involvement of most of the centrum semiovale (grade 8). Studies with no WMLs were graded 0; those with WMLs worse than grade 8 were graded 9. The worm-shaped shadows, most apparent in the grade 8 image, are artifact.
  • JAMA November 14, 2001

    Figure 4: Representative Examples of the Major Differences Between the Predicted Protein Sets of the Human Compared With the Fly and the Worm

    The numbers of proteins containing the specified Pfam domain or protein family for each of the animal genomes were derived by computational analysis. Representative protein domains or protein families that show a 2-fold or greater expansion in the human were categorized into cellular processes (eg, developmental regulators; neural structure and function; or hemostasis, complement system, and immune response) for representation. A detailed biological description of each of these protein domains may be obtained from the Pfam or SMART databases. TGF-β indicates transforming growth factor-β; TSP, thrombospondin; CCP, complement control protein; and TIR, toll interleukin receptor.Notable examples from this list of proteins that are unique to the human (when compared with the fly and worm) include connexins (constitutive subunits of intercellular channels, providing the structural basis for electrical coupling); neuropilin, a key mediator in axonal guidance along with the semaphorins and plexin molecules; fibronectin type 1 (FN1) domain, a fibrin-binding domain found in certain proteins of the coagulation cascade; fibronectin type 2 (FN2) domain, a collagen-binding domain found in a diverse set of hemostatic regulators; membrane-attack complex/perforin (MACPF), a domain found in certain complement proteins; C1q, a domain found in complement 1q and in many collagens; cytokines and tumor necrosis factor (TNF), 2 of the central families of secreted proteins that mediate a wide spectrum of immune-related functions.*Voltage-gated (VG) ion channels include VG-sodium, -calcium, and -potassium channels.
  • 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.
  • JAMA January 28, 1998

    Figure: To Die or Not to Die: An Overview of Apoptosis and Its Role in Disease

    Figure 1.—The apoptotic program is conserved in evolution. A, Tissue-specific signals activate ced-4, which activates ced-3, leading to cell death. If activated, ced-9 can inhibit apoptosis by inhibiting ced-4's activation of ced-3 (and possibly by directly inhibiting ced-3), as indicated by dashed arrow. B, A wide array of factors commit a mammalian cell to die, but the downstream apoptotic machinery is conserved (worm genes homologous to mammalian apoptotic genes are shown in parentheses). Arrows indicate positive interactions; blunted arrows, negative interactions.
  • Efficacy of Current Drugs Against Soil-Transmitted Helminth Infections: Systematic Review and Meta-analysis

    Abstract Full Text
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    JAMA. 2008; 299(16):1937-1948. doi: 10.1001/jama.299.16.1937
  • Helminth Infection During Pregnancy and Development of Infantile Eczema

    Abstract Full Text
    JAMA. 2005; 294(16):2028-2034. doi: 10.1001/jama.294.16.2032-c
  • Helminthic Infections Among Peace Corps Volunteers in Nepal

    Abstract Full Text
    JAMA. 1990; 263(3):373-374. doi: 10.1001/jama.1990.03440030056016
  • The Question of a Helminthic Cause of Preeclampsia

    Abstract Full Text
    JAMA. 1983; 250(21):2970-2972. doi: 10.1001/jama.1983.03340210068030
  • THE CHANGING DISTRIBUTION OF HELMINTHIC DISEASES IN THE UNITED STATES

    Abstract Full Text
    JAMA. 1957; 164(2):121-126. doi: 10.1001/jama.1957.02980020001001
  • Veterinary Helminthology and Entomology: The Diseases of Domesticated Animals Caused by Helminth and Arthropod Parasites

    Abstract Full Text
    JAMA. 1939; 112(6):575-575. doi: 10.1001/jama.1939.02800060091038
  • Veterinary Helminthology and Entomology: The Diseases of Domesticated Animals Caused by Helminth and Arthropod Parasites

    Abstract Full Text
    JAMA. 1935; 105(4):307-307. doi: 10.1001/jama.1935.02760300067031
  • HELMINTHIC THERAPY

    Abstract Full Text
    JAMA. 1927; 88(22):1747-1747. doi: 10.1001/jama.1927.02680480057030
  • A CONTRIBUTION TO HELMINTHIC THERAPY

    Abstract Full Text
    JAMA. 1927; 88(12):903-905. doi: 10.1001/jama.1927.02680380027011
  • Photomicrographs of Spirochetes, Entamebas, Plasmodia Trypanosomes, Leishmania, Negri Bodies and Parasitic Helminths.

    Abstract Full Text
    JAMA. 1913; 61(13_part_1):1064-1064. doi: 10.1001/jama.1913.04350130058037