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"The complete atomic structure of the
large ribosomal subunit at 2.4 angstrom resolution,"
by Nenad Ban, Poul Nissen, Jeffrey Hansen, Peter B. Moore, Thomas A. Steitz, Science,
289(5481):905-20, 11 August 2000.
[Howard Hughes Medical Institute and Yale
University, New Haven, CT]
Abstract: "The large ribosomal
subunit catalyzes peptide bond formation and binds initiation, termination,
and elongation factors. We have determined the crystal structure of the large
ribosomal subunit from Haloarcula marismortui at 2.4 angstrom
resolution, and it includes 2833 of the subunit's 3045 nucleotides and 27 of
its 31 proteins. The domains of its RNAs all have irregular shapes and fit
together in the ribosome like the pieces of a three-dimensional jigsaw puzzle
to form a large, monolithic structure. Proteins are abundant everywhere on its
surface except in the active site where peptide bond formation occurs and
where it contacts the small subunit. Most of the proteins stabilize the
structure by interacting with several RNA domains, often using
idiosyncratically folded extensions that reach into the subunit's
interior."
This 2000 report from Science was
cited 47 times in current journal articles indexed by ISI during
March-April 2002. With this latest two-month tally, the report currently ranks
at #4 among biology papers (aside from reviews) published in the last two
years. Prior to the most recent bimonthly count, citations to the paper have
accrued as follows:
January-February 2002: 18 citations
November-December 2001: 35
September-October 2001: 37
July-August 2001: 42
May-June 2001: 32
March-April 2001: 29
January-February 2001: 19
November-December 2000: 10
September-October 2000: 4
July-August 2000: 3
Total citations to date: 276
SOURCE: Hot
Papers Database (Included with a subscription to the ISI print newsletter Science
Watch®, available from the ISI
Research Services Group. Packaged on a CD-ROM that is mailed with each Science
Watch issue, the Hot
Papers Database contains data on hundreds of highly cited papers published
during the last two years. User interface permits searching by author,
organization, journal, field, and more. Total citations, as well as citations
accrued during successive bimonthly periods, can be assessed and graphed. An
updated CD containing the most recent bimonthly data is mailed with every new
issue of Science
Watch,
six times a year. The CD also includes an electronic version of the Science
Watch
issue in HTML format, for personal desktop access.)
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