Proceedings of the National Academy of Sciences (P NATL ACAD SCI USA)
PNAS is one of the world's most-cited multidisciplinary scientific serials. Since its establishment in 1915, it continues to publish cutting-edge research reports, commentaries, reviews, perspectives, colloquium papers, and actions of the Academy. Coverage in PNAS spans the biological, physical, and social sciences. PNAS is published biweekly in print, and weekly online in PNAS Early Edition.
- Impact factor9.68Show impact factor historyHide impact factor history
- WebsitePNAS website
Other titlesProceedings of the National Academy of Sciences of the United States of America, PNAS
Material typePeriodical, Internet resource
Document typeJournal / Magazine / Newspaper, Internet Resource
Publications in this journal
[show abstract] [hide abstract]
ABSTRACT: The middle ear ossicles are only rarely preserved in fossil hominins. Here,we report the discovery of a complete ossicular chain (malleus, incus, and stapes) of Paranthropus robustus aswell as additional ear ossicles from Australopithecus africanus. The malleus in both early hominin taxa is clearly human-like in the proportions of the manubrium and corpus, whereas the incus and stapes resemble African and Asian great apes more closely. A deep phylogenetic origin is proposed for the derived malleus morphology, and this may represent one of the earliest human-like features to appear in the fossil record. The anatomical differences found in the early hominin incus and stapes, along with other aspects of the outer, middle, and inner ear, are consistent with the suggestion of different auditory capacities in these early hominin taxa compared with modern humans.Proceedings of the National Academy of Sciences 05/2013; On line:1-5.
Proceedings of the National Academy of Sciences 05/2013;
Article: Multifunctional essentiality of succinate metabolism in adaptation to hypoxia in Mycobacterium tuberculosis[show abstract] [hide abstract]
ABSTRACT: Mycobacterium tuberculosis is a chronic, facultative intracellular pathogen that spends the majority of its decades-long life cycle in a non- or slowly replicating state. However, the bacterium remains poised to resume replicating so that it can transmit itself to a new host. Knowledge of the metabolic adaptations used to facilitate entry into and exit from nonreplicative states remains incomplete. Here, we apply 13C-based metabolomic profiling to characterize the activity of M. tuberculosis tricarboxylic acid cycle during adaptation to and recovery from hypoxia, a physiologically relevant condition associated with nonreplication. We show that, as M. tuberculosis adapts to hypoxia, it slows and remodels its tricarboxylic acid cycle to increase production of succinate, which is used to flexibly sustain membrane potential, ATP synthesis, and anaplerosis, in response to varying degrees of O2 limitation and the presence or absence of the alternate electron acceptor nitrate. This remodeling is mediated by the bifunctional enzyme isocitrate lyase acting in a noncanonical role distinct from fatty acid catabolism. Isocitrate lyase-dependent production of succinate affords M. tuberculosis with a unique and bioenergetically efficient metabolic means of entry into and exit from hypoxia-induced quiescence.Proceedings of the National Academy of Sciences 04/2013;
Article: Parkinson-susceptibility gene DJ-1/PARK7 protects the murine heart from oxidative damage in vivoProceedings of the National Academy of Sciences 03/2013;
Article: An Essential Role for γ-herpesvirus Latency-associated Nuclear Antigen Homolog in an Acute Lymphoproliferative Disease of CattleProceedings of the National Academy of Sciences 03/2013;
Proceedings of the National Academy of Sciences 03/2013;
Proceedings of the National Academy of Sciences 03/2013;
Article: Illuminating the activation mechanisms and allosteric properties of metabotropic glutamate receptorsProceedings of the National Academy of Sciences 03/2013;
Article: An RNA recognition motif-containing protein is required for plastid RNA editing in Arabidopsis and maize[show abstract] [hide abstract]
ABSTRACT: Plant RNA editing modifies cytidines (C) to uridines (U) at specific sites in the transcripts of both mitochondria and plastids. Specific targeting of particular Cs is achieved by pentatricopeptide proteins that recognize cis elements upstream of the C that is edited. Members of the RNA-editing factor interacting protein (RIP) family in Arabidopsis have recently been shown to be essential components of the plant editosome. We have identified a gene that contains a pair of truncated RIP domains (RIP-RIP). Unlike any previously described RIP family member, the encoded protein carries an RNA recognition motif (RRM) at its C terminus and has therefore been named Organelle RRM protein 1 (ORRM1). ORRM1 is an essential plastid editing factor; in Arabidopsis and maize mutants, RNA editing is impaired at particular sites, with an almost complete loss of editing for 12 sites in Arabidopsis and 9 sites in maize. Transfection of Arabidopsis orrm1 mutant protoplasts with constructs encoding a region encompassing the RIP-RIP domain or a region spanning the RRM domain of ORRM1 demonstrated that the RRM domain is sufficient for the editing function of ORRM1 in vitro. According to a yeast two-hybrid assay, ORRM1 interacts selectively with pentatricopeptide transfactors via its RIP-RIP domain. Phylogenetic analysis reveals that the RRM in ORRM1 clusters with a clade of RRM proteins that are targeted to organelles. Taken together, these results suggest that other members of the ORRM family may likewise function in RNA editing.Proceedings of the National Academy of Sciences 03/2013;
Data provided are for informational purposes only. Although carefully collected, accuracy cannot be guaranteed. The impact factor represents a rough estimation of the journal's impact factor and does not reflect the actual current impact factor. Publisher conditions are provided by RoMEO. Differing provisions from the publisher's actual policy or licence agreement may be applicable.
ISSN: 2041-1723, Impact factor: 7.4
ISSN: 1946-6242, Impact factor: 7.8
ISSN: 1873-2968, Impact factor: 4.25
ISSN: 1872-7980, Impact factor: 4.86
International Institute of...
ISSN: 1791-7530, Impact factor: 1.73
ISSN: 1791-3004, Impact factor: 0.42
Ethnikon Hidryma Ereunōn (Greece)
ISSN: 1791-2431, Impact factor: 1.84
International Center for Cancer...
ISSN: 1791-2423, Impact factor: 2.4