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  • Down Syndrome—New Prospects for an Ancient Disorder

    Abstract Full Text
    JAMA. 2010; 303(24):2525-2526. doi: 10.1001/jama.2010.842
  • Ancestry and Pathology in King Tutankhamun's Family

    Abstract Full Text
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    JAMA. 2010; 303(7):638-647. doi: 10.1001/jama.2010.121
  • JAMA February 17, 2010

    Figure 1: Microsatellite Data of Mummies Thought to Belong to the Tutankhamun Kindred

    The length of each microsatellite allele was determined in base pairs and converted by software into the number of actual reiterations of repeat motifs at the corresponding locus. All established genotypes differ from those of the laboratory staff and the ancient control group. Note that allele origins in KV21A and KV21B are suggestive and do not serve as proof of relationship with the Amenhotep III and Thuya lineages. See online interactive kinship analysis and pedigree.aIdentified as Tiye. See eAppendix for additional commentary.bIdentified as Akhenaten. See eAppendix for additional commentary. cData replication was successfully performed in the second Cairo laboratory.
  • JAMA November 18, 2009

    Figure: Computed Tomographic Examples of Atherosclerosis in Ancient Egyptian Mummies and a Contemporary Human

    A, Axial computed tomographic (CT) image demonstrating calcification in the wall of the thoracic aorta (arrowhead) at the level of the aortic arch in the mummy of Lady Rai, who lived during the early 18th Egyptian dynasty (mummy No. 8). B, Calcification in the wall of the abdominal aorta (arrowhead) in the mummy of Tjanefer, a man who lived during the third intermediate period (mummy No. 5). C, Longitudinal CT view of the leg demonstrating the superficial femoral artery with a calcified plaque (arrowhead) in the mummy of a woman who lived during the 18th dynasty (mummy No. 14). The density at this location measured 1530 Hounsfield units. The view of a CT angiogram of the living individual demonstrates a calcified plaque in a similiar location with a comparable density measurement to mummy No. 14.
  • Computed Tomographic Assessment of Atherosclerosis in Ancient Egyptian Mummies

    Abstract Full Text
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    JAMA. 2009; 302(19):2091-2094. doi: 10.1001/jama.2009.1641
  • JAMA December 12, 2007

    Figure 2: Magnetic Resonance Image of an Ancient Egyptian Mummy

    Magnetic resonance–based 3-dimensional reconstruction (virtual coronal cut through mid-face) of an ancient Egyptian mummy head. Differences in signal densities of external/internal lamina (yellow arrowheads) vs diploetic bone and the high signal of embalming-related substances in the orbits and the mouth cavity (black arrowheads) are visible. MRI technical data: see Figure 1.
  • JAMA December 12, 2007

    Figure 1: Magnetic Resonance Image and Computed Tomography Image of an Ancient Egyptian Mummy

    An ancient Egyptian mummy head, mid-sagittal plane. A, Bright signal of presumed resin (embalming liquid) relative to adjoining prevertebral tissue (yellow arrowheads) in comparison with multislice computed tomography scan image (B). Greater range of signal in the 2 locations of embalming substances, prevertebral and intracranial/occipital (black arrowhead), is visible by magnetic resonance imaging (A) in comparison with computed tomography scan (B). The brain was removed during embalming. MRI technical data: transmit receive knee coil; transverse relaxation time, 20 milliseconds; echo time, 100 microseconds; field of view, 282 mm3; acquisition time, 21.9 minutes.
  • Clinical Magnetic Resonance Imaging of Ancient Dry Human Mummies Without Rehydration

    Abstract Full Text
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    JAMA. 2007; 298(22):2618-2620. doi: 10.1001/jama.298.22.2618-b
  • 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.
  • Publishers Debate Future of Online Journals

    Abstract Full Text
    JAMA. 2000; 284(8):943-944. doi: 10.1001/jama.284.8.943
  • An Ancient Nation Braces to Fight AIDS

    Abstract Full Text
    JAMA. 2000; 283(5):593-595. doi: 10.1001/jama.283.5.593-JMN0202-3-1
  • Tuberculosis—Battling an Ancient Scourge

    Abstract Full Text
    JAMA. 1999; 282(21):1996-1996. doi: 10.1001/jama.282.21.1996
  • A History of Medicine, vol 1: Primitive and Ancient Medicine

    Abstract Full Text
    JAMA. 1992; 267(20):2818-2819. doi: 10.1001/jama.1992.03480200126040
  • History of Chinese Medicine: Being a Chronicle of Medical Happenings in China from Ancient Times to the Present Period

    Abstract Full Text
    JAMA. 1937; 108(24):2068-2068. doi: 10.1001/jama.1937.02780240060029
  • History of Chinese Medicine: Being a Chronicle of Medical Happenings in China from Ancient Times to the Present Period.

    Abstract Full Text
    JAMA. 1933; 101(1):72-73. doi: 10.1001/jama.1933.02740260074036
  • ANCIENT EGYPTIANS AND MODERN MEDICINE

    Abstract Full Text
    JAMA. 2011; 305(15):1602-1602. doi: 10.1001/jama.2011.430
  • Ancient Egyptian Medicine

    Abstract Full Text
    JAMA. 2003; 290(6):826-827. doi: 10.1001/jama.290.6.826-a
  • ANCIENT PROBLEMS OF PHARMACY AND THEIR WARNING

    Abstract Full Text
    JAMA. 2011; 305(7):722-722. doi: 10.1001/jama.285.6.700
  • History of Medicine: Greek Medicine, vol 2

    Abstract Full Text
    JAMA. 1995; 274(22):1815-1816. doi: 10.1001/jama.1995.03530220081049