Showing 91 - 100 of 5709 Items
Date: 2007-07-01
Creator: Patsy S. Dickinson, Jake S. Stevens, Szymon Rus, Henry R. Brennan, Christopher C., Goiney, Christine M. Smith, Lingjun Li, David W. Towle, Andrew E. Christie
Access: Open access
- In arthropods, a group of peptides possessing a -Y(SO3H)GHM/ LRFamide carboxy-terminal motif have been collectively termed the sulfakinins. Sulfakinin isoforms have been identified from numerous insect species. In contrast, members of this peptide family have thus far been isolated from just two crustaceans, the penaeid shrimp Penaeus monodon and Litopenaeus vannamei. Here, we report the identification of a cDNA encoding prepro-sulfakinin from the American lobster Homarus americanus. Two sulfakinin-like sequences were identified within the open-reading frame of the cDNA. Based on modifications predicted by peptide modeling programs, and on homology to the known isoforms of sulfakinin, particularly those from shrimp, the mature H. americanus sulfakinins were hypothesized to be pEFDEY(SO3H)GHMRFamide (Hoa-SK I) and GGGEY(SO3H)DDY(SO3H)GHLRFamide (Hoa-SK II). Hoa-SK I is identical to one of the previously identified shrimp sulfakinins, while Hoa-SK II is a novel isoform. Exogenous application of either synthetic Hoa-SK I or Hoa-SK II to the isolated lobster heart increased both the frequency and amplitude of spontaneous heart contractions. In preparations in which spontaneous contractions were irregular, both peptides increased the regularity of the heartbeat. Our study provides the first molecular characterization of a sulfakinin-encoding cDNA from a crustacean, as well as the first demonstration of bioactivity for native sulfakinins in this group of arthropods.
- Embargo End Date: 2026-05-20
Date: 2021-01-01
Creator: Molly Margaret Moore
Access: Embargoed
Date: 1993-01-01
Creator: M. Procario, S. Yang, D. S. Akerib, B. Barish, M., Chadha, S. Chan, D. F. Cowen, G. Eigen, J. S. Miller, J. Urheim, A. J. Weinstein, D. Acosta, M. Athanas, G. Masek, B. Ong, H. Paar, M. Sivertz, A. Bean, J. Gronberg, R. Kutschke, S. Menary, R. J. Morrison, S. Nakanishi, H. N. Nelson, T. K. Nelson, J. D. Richman, H. Tajima, D. Schmidt, D. Sperka, M. S. Witherell, R. Ballest
Access: Open access
- Using the CLEO II detector at CESR we have studied D0 decays into final states with a K̄0 or K̄*0, and have measured branching ratios for the decay modes D0→(K̄0K̄*0)π0,η, η′. These results are compared with predictions of various charm decay models, and contributions of final-state interactions are discussed. © 1993 The American Physical Society.
Date: 1993-01-01
Creator: R. Ammar, S. Ball, P. Baringer, D. Coppage, N., Copty, R. Davis, N. Hancock, M. Kelly, N. Kwak, H. Lam, Y. Kubota, M. Lattery, J. K. Nelson, S. Patton, D. Perticone, R. Poling, V. Savinov, S. Schrenk, R. Wang, M. S. Alam, I. J. Kim, B. Nemati, J. J. O'Neill, H. Severini, C. R. Sun, M. M. Zoeller, G. Crawford, M. Daubenmeir, R. Fulton, D. Fujino, K. K. Gan
Access: Open access
- We have observed the decays B0→K*(892)0γ and B-→K*(892)-γ, which are evidence for the quark-level process b→sγ. The average branching fraction is (4.5±1.5±0.9) ×10-5. This value is consistent with standard model predictions from electromagnetic penguin diagrams. © 1993 The American Physical Society.
Date: 2008-03-01
Creator: Aimee M. Eldridge, Deborah S. Wuttke
Access: Open access
- The Saccharomyces cerevisiae protein Cdc13 tightly and specifically binds the conserved G-rich single-stranded overhang at telomeres and plays an essential role in telomere end-protection and length regulation. The 200 residue DNA-binding domain of Cdc13 (Cdc13-DBD) binds an 11mer single-stranded representative of the yeast telomeric sequence [Tel11, d(GTGTGGGTGTG)] with a 3 pM affinity and specificity for three bases (underlined) at the 5′ end. The structure of the Cdc13-DBD bound to Tel11 revealed a large, predominantly aromatic protein interface with several unusual features. The DNA adopts an irregular, extended structure, and the binding interface includes a long (∼30 amino acids) structured loop between strands β2-β3 (L2-3) of an OB-fold. To investigate the mechanism of ssDNA binding, we studied the free and bound states of Cdc13-DBD using NMR spectroscopy. Chemical shift changes indicate that the basic topology of the domain, including L2-3, is essentially intact in the free state. Changes in slow and intermediate time scale dynamics, however, occur in L2-3, while conformational changes distant from the DNA interface suggest an induced fit mechanism for binding in the 'hot spot' for binding affinity and specificity. These data point to an overall binding mechanism well adapted to the heterogeneous nature of yeast telomeres. © 2008 The Author(s).
Date: 2020-01-01
Creator: Rebecca Berman
Access: Access restricted to the Bowdoin Community
Date: 2009-02-01
Creator: José Burillo, Sean Cleary, Melanie Stein, Jennifer Taback
Access: Open access
- We discuss metric and combinatorial properties of Thompson's group T, including normal forms for elements and unique tree pair diagram representatives. We relate these properties to those of Thompson's group F when possible, and highlight combinatorial differences between the two groups. We define a set of unique normal forms for elements of T arising from minimal factorizations of elements into natural pieces. We show that the number of carets in a reduced representative of an element of T estimates the word length, that F is undistorted in T, and we describe how to recognize torsion elements in T. © 2008 American Mathematical Society Reverts to public domain 28 years from publication.
Date: 2013-01-01
Creator: Sarah Montross, Shu-Chin Tsui
Access: Open access
- "This brochure accompanies an exhibition of the same name at the Bowdoin College Museum of Art, Brunswick, Maine, from September 27 through December 22, 2013"--Back of cover flap
Date: 1910-01-01
Access: Open access
- Bowdoin College Bulletin no. 25