677 research outputs found
Motion of the sub-satellite point for 24-hour orbits
Subsatellite path for 24-hour orbits affected by changes in eccentricity, inclination, and argument of perigee - orbital path of syncom i
Teaching Breast Self-Examination in the High School
Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/73530/1/j.1746-1561.1977.tb01051.x.pd
Working with simple machines
A set of examples is provided that illustrate the use of work as applied to
simple machines. The ramp, pulley, lever and hydraulic press are common
experiences in the life of a student and their theoretical analysis therefore
makes the abstract concept of work more real. The mechanical advantage of each
of these systems is also discussed so that students can evaluate their
usefulness as machines.Comment: 9 pages, 4 figure
Direct reaction measurements with a 132Sn radioactive ion beam
The (d,p) neutron transfer and (d,d) elastic scattering reactions were
measured in inverse kinematics using a radioactive ion beam of 132Sn at 630
MeV. The elastic scattering data were taken in a region where Rutherford
scattering dominated the reaction, and nuclear effects account for less than 8%
of the cross section. The magnitude of the nuclear effects was found to be
independent of the optical potential used, allowing the transfer data to be
normalized in a reliable manner. The neutron-transfer reaction populated a
previously unmeasured state at 1363 keV, which is most likely the
single-particle 3p1/2 state expected above the N=82 shell closure. The data
were analyzed using finite range adiabatic wave calculations and the results
compared with the previous analysis using the distorted wave Born
approximation. Angular distributions for the ground and first excited states
are consistent with the previous tentative spin and parity assignments.
Spectroscopic factors extracted from the differential cross sections are
similar to those found for the one neutron states beyond the benchmark
doubly-magic nucleus 208Pb.Comment: 22 pages, 7 figure
The magic nature of 132Sn explored through the single-particle states of 133Sn
Atomic nuclei have a shell structure where nuclei with 'magic numbers' of
neutrons and protons are analogous to the noble gases in atomic physics. Only
ten nuclei with the standard magic numbers of both neutrons and protons have so
far been observed. The nuclear shell model is founded on the precept that
neutrons and protons can move as independent particles in orbitals with
discrete quantum numbers, subject to a mean field generated by all the other
nucleons. Knowledge of the properties of single-particle states outside nuclear
shell closures in exotic nuclei is important for a fundamental understanding of
nuclear structure and nucleosynthesis (for example the r-process, which is
responsible for the production of about half of the heavy elements). However,
as a result of their short lifetimes, there is a paucity of knowledge about the
nature of single-particle states outside exotic doubly magic nuclei. Here we
measure the single-particle character of the levels in 133Sn that lie outside
the double shell closure present at the short-lived nucleus 132Sn. We use an
inverse kinematics technique that involves the transfer of a single nucleon to
the nucleus. The purity of the measured single-particle states clearly
illustrates the magic nature of 132Sn.Comment: 19 pages, 5 figures and 4 table
Biodegradable nanomats produced by electrospinning : expanding multifunctionality and potential for tissue engineering
With increasing interest in nanotechnology, development of nanofibers (n-fibers) by using the
technique of electrospinning is gaining new momentum. Among important potential applications of
n-fiber-based structures, scaffolds for tissue-engineering represent an advancing front. Nanoscaffolds
(n-scaffolds) are closer to natural extracellular matrix (ECM) and its nanoscale fibrous structure.
Although the technique of electrospinning is relatively old, various improvements have been
made in the last decades to explore the spinning of submicron fibers from biodegradable polymers
and to develop also multifunctional drug-releasing and bioactive scaffolds. Various factors can
affect the properties of resulting nanostructures that can be classified into three main categories,
namely: (1) Substrate related, (2) Apparatus related, and (3) Environment related factors. Developed
n-scaffolds were tested for their cytocompatibility using different cell models and were seeded
with cells for to develop tissue engineering constructs. Most importantly, studies have looked at the
potential of using n-scaffolds for the development of blood vessels. There is a large area ahead
for further applications and development of the field. For instance, multifunctional scaffolds that
can be used as controlled delivery system do have a potential and have yet to be investigated for
engineering of various tissues. So far, in vivo data on n-scaffolds are scarce, but in future reports
are expected to emerge. With the convergence of the fields of nanotechnology, drug release and
tissue engineering, new solutions could be found for the current limitations of tissue engineering
scaffolds, which may enhance their functionality upon in vivo implantation. In this paper electrospinning
process, factors affecting it, used polymers, developed n-scaffolds and their characterization
are reviewed with focus on application in tissue engineering
PAK6-mediated phosphorylation of PPP2R2C regulates LRRK2-PP2A complex formation
Mutations in leucine-rich repeat kinase 2 (LRRK2) are a common cause of inherited and sporadic Parkinson's disease (PD) and previous work suggests that dephosphorylation of LRRK2 at a cluster of heterologous phosphosites is associated to disease. We have previously reported subunits of the PP1 and PP2A classes of phosphatases as well as the PAK6 kinase as regulators of LRRK2 dephosphorylation. We therefore hypothesized that PAK6 may have a functional link with LRRK2's phosphatases. To investigate this, we used PhosTag gel electrophoresis with purified proteins and found that PAK6 phosphorylates the PP2A regulatory subunit PPP2R2C at position S381. While S381 phosphorylation did not affect PP2A holoenzyme formation, a S381A phosphodead PPP2R2C showed impaired binding to LRRK2. Also, PAK6 kinase activity changed PPP2R2C subcellular localization in a S381 phosphorylation-dependent manner. Finally, PAK6-mediated dephosphorylation of LRRK2 was unaffected by phosphorylation of PPP2R2C at S381, suggesting that the previously reported mechanism whereby PAK6-mediated phosphorylation of 14-3-3 proteins promotes 14-3-3-LRRK2 complex dissociation and consequent exposure of LRRK2 phosphosites for dephosphorylation is dominant. Taken together, we conclude that PAK6-mediated phosphorylation of PPP2R2C influences the recruitment of PPP2R2C to the LRRK2 complex and PPP2R2C subcellular localization, pointing to an additional mechanism in the fine-tuning of LRRK2 phosphorylation.</p
Sex bias in biopsy samples collected from free-ranging dolphins
Author Posting. © The Author(s), 2009. This is the author's version of the work. It is posted here by permission of Springer for personal use, not for redistribution. The definitive version was published in European Journal of Wildlife Research 56 (2010): 151-158, doi:10.1007/s10344-009-0299-7.Biological samples of free-ranging dolphins are increasingly used to gain information on
population structure and ecology. In small cetaceans, the gender of individuals usually cannot
be determined at sea, and population sex ratio has to be inferred indirectly. We used
molecular sexing to determine the gender of 340 biopsy samples of bottlenose dolphins,
Tursiops truncatus, spotted dolphins, Stenella frontalis, and common dolphins, Delphinus
delphis, collected around the Azores and Madeira. Sex ratio was globally skewed in favor of
males, and differed between species and archipelagos. Skew was probably influenced by the
selectivity of biopsy collectors and seasonal or year-round predominance of males in natural
populations. Skew was also influenced by sampling duration and intensity. In the Azores,
when several samples were successively collected within the same group, the proportion of
female samples decreased as a function of sample order. This trend indicated a tendency for
females to increasingly avoid the boat while samples were being collected. It showed that
males and females reacted differently to the perturbation caused by the biopsy sampling
process (i.e. sample collection and driving style).Portuguese Foundation for
Science and Technology (FCT) and the FEDER program for funding the CETAMARH
(POCTI/BSE/38991/01) and the GOLFINICHO (POCI/BIA-BDE/61009/2004) projects,
S.Q.'s post-doctoral grants (IMAR/FCT- PDOC-006/2001-MoleGen and
SFRH/BPD/19680/2004), M.A.S.'s doctoral (SFRH/BD/8609/2002) and post-doctoral
(SFRH/BPD/29841/2006) grants, S.M.'s investigation assistant grant
(CETAMARHII/POCTI/BSE/38991/2001) and I.C.'s investigation assistant grants
(IMAR/FCT/GOLFINICHO/001/2005 and IMAR/FCT/GOLFINICHO/004/2006). FCT for its pluri-annual funding to Research Unit #531 and the EU funded
program Interreg IIIb for funding the MACETUS project (MAC/4.2/M10) as well as R.P. and S.M.’s grants (IMAR/INTERREGIIIb/MACETUS/MAC1/2)
PAK6-mediated phosphorylation of PPP2R2C regulates LRRK2-PP2A complex formation
Mutations in leucine-rich repeat kinase 2 (LRRK2) are a common cause of inherited and sporadic Parkinson's disease (PD) and previous work suggests that dephosphorylation of LRRK2 at a cluster of heterologous phosphosites is associated to disease. We have previously reported subunits of the PP1 and PP2A classes of phosphatases as well as the PAK6 kinase as regulators of LRRK2 dephosphorylation. We therefore hypothesized that PAK6 may have a functional link with LRRK2's phosphatases. To investigate this, we used PhosTag gel electrophoresis with purified proteins and found that PAK6 phosphorylates the PP2A regulatory subunit PPP2R2C at position S381. While S381 phosphorylation did not affect PP2A holoenzyme formation, a S381A phosphodead PPP2R2C showed impaired binding to LRRK2. Also, PAK6 kinase activity changed PPP2R2C subcellular localization in a S381 phosphorylation-dependent manner. Finally, PAK6-mediated dephosphorylation of LRRK2 was unaffected by phosphorylation of PPP2R2C at S381, suggesting that the previously reported mechanism whereby PAK6-mediated phosphorylation of 14-3-3 proteins promotes 14-3-3-LRRK2 complex dissociation and consequent exposure of LRRK2 phosphosites for dephosphorylation is dominant. Taken together, we conclude that PAK6-mediated phosphorylation of PPP2R2C influences the recruitment of PPP2R2C to the LRRK2 complex and PPP2R2C subcellular localization, pointing to an additional mechanism in the fine-tuning of LRRK2 phosphorylation.</p
PAK6-mediated phosphorylation of PPP2R2C regulates LRRK2-PP2A complex formation
Mutations in leucine-rich repeat kinase 2 (LRRK2) are a common cause of inherited and sporadic Parkinson's disease (PD) and previous work suggests that dephosphorylation of LRRK2 at a cluster of heterologous phosphosites is associated to disease. We have previously reported subunits of the PP1 and PP2A classes of phosphatases as well as the PAK6 kinase as regulators of LRRK2 dephosphorylation. We therefore hypothesized that PAK6 may have a functional link with LRRK2's phosphatases. To investigate this, we used PhosTag gel electrophoresis with purified proteins and found that PAK6 phosphorylates the PP2A regulatory subunit PPP2R2C at position S381. While S381 phosphorylation did not affect PP2A holoenzyme formation, a S381A phosphodead PPP2R2C showed impaired binding to LRRK2. Also, PAK6 kinase activity changed PPP2R2C subcellular localization in a S381 phosphorylation-dependent manner. Finally, PAK6-mediated dephosphorylation of LRRK2 was unaffected by phosphorylation of PPP2R2C at S381, suggesting that the previously reported mechanism whereby PAK6-mediated phosphorylation of 14-3-3 proteins promotes 14-3-3-LRRK2 complex dissociation and consequent exposure of LRRK2 phosphosites for dephosphorylation is dominant. Taken together, we conclude that PAK6-mediated phosphorylation of PPP2R2C influences the recruitment of PPP2R2C to the LRRK2 complex and PPP2R2C subcellular localization, pointing to an additional mechanism in the fine-tuning of LRRK2 phosphorylation.</p
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