Geographic information systems and coastal planning in Australia

The objective of this paper is to demonstrate the ability of visualization and simulation techniques to aid and simulate current and future directions in coastal planning. The process of visualization will interrogate the coastal cities of Portland, Apollo Bay, Anglesea and Hobsons Bay in south-eastern Australian coastal seaboard through a progression of projections and simulated forecasts from 2014 to 2050 to see if a process(s) or methodology could help in planning the future growth of coastal settlements. The analysis uses Geographic Information Systems (GIS) associated with planning application software.

1987 Yearbook

TOC: Clubs & Organizations…18 / Current Events & Music…30 / Faculty & Staff…33 / Activities & Events… / Honors & Graduation…65 / Graduates…75 / Yearbook Credits…111 / A Thank You…112 YEARBOOK COMMITTEE: Project Director, Vincent Banrey; Asst. Project Director, Catherine Whan; Editors (1986): Maricruz Saunders; (1987): Juan Jimenez, GloryAnn Torres; LAYOUT DESIGNERS: Vincent Banrey, Stephanie Bowen, Yvonne Brown, Jacqui Fernandez, Milton Ferreira, Omar Harris, Cornelius Huskins, Juan Jimenez, Wayne Keane, Richard Massie, Victoria Pamias, Richard Provost, Maricruz Saunders, GloryAnn Torres, Pedro Torres, Joan Walker, Catherine Whan. PHOTOGRAPHERS: John Carrero, Young Baek Choi, Randy Fader-Smith, Milton Ferreira, Roger Ince, Juan Jimenez, Umoja Kwanguvu, Seymour Lerman, Clinton Linton, Richard Provost, Jaidee amsinghani, Maricruz Saunders, Frank Tocco, GloryAnn Torres, Catherine Whan, Alan Young. ARTISTS: Cover Design: Madeline Vega; Endsheets: Oscar "DJ Ozzie" Ramirez; Division Pages: Jose Marti; International LaGuardia: Jacqui Fernandez; Illustrations: Richard Massie, Jacqui Fernandez, Madeline Vega. WRITERS: Yasmin Ahmed, Vincent Banrey, Warren Gardner, Juan Jimenez, Umoja Kwanguvu, Luis Merchant, Victoria Pamias, Richard Provost, Christiana Somerville, GloryAnn Torres, Joan Walker, Catherine Whan. SIGNIFICANT OTHERS: Word Processing: Blanca Arbito, Edward Hollins, Catherine Whan. Vincent Banrey Spread: developed by Blanca Arbito, Edward Hollins and GloryAnn Torres, Jacqui Fernandez, Catherine Whan. Creative Consultant: Edward Hollins. Promotions: George Condors. SPECIAL THANKS TO: Frank and Seymour of Classic Studios; Chuck Lindsey, Photo Workshop Instructor; Ted Schiffman of Taylor Publishing Co.; Dan Horn and Thurston Reyes of LaGuardia Theatre; and the Recreation staff. ALAN BERMAN IN MEMORIAM: Sketch, Tom Fink; Alan Speaking, Brian Gallagher; Remembering Dr. Alan Berman, Tuzyline Allan.

1988 Yearbook

Vol. 7; Sept. 1988; 109 p. b&w, color photographs TOC: Life at LaGuardia…2 / Activities and Events…17 / Faculty and Staff…33 / Activities at LaGuardia…49 / Graduation…71 Yearbook Committee Credits: Faculty Advisor, Vincent Banrey; Project Director, Catherine Whan; Editors: Alexandra Gomez, Juan Jimenez, GloryAnn Torres; Asst. Editor, Kenny Rosa; LAYOUT: Vincent Banrey, Marino "Tito" Cabrera, Shirley Chance, George Condors, Milton Ferreira, Maria Flores, Alexandra Gomez, Ana Lisa Gonzalez, Bernadette Henry, Juan Jimenez, Alejandro Meneses, Richard Provost, Kenny Rosa, Maria Sanchez, GloryAnn Torres, Catherine Whan, Alan O. Young; PHOTOGRAPHY: Peter Abbate, Sandra Acres, Young Baek Choi, Randy Fader Smith, Milton Ferriera, Alexandra Gomez, Juan Jimenez, Seymour Lerman, Chuck Lindsey, Victoria Pamias, Richard Provost, Alan Scribner, Frank Tocco, GloryAnn Torres, Catherine Whan. ART: Jose Marti (Cover Design and Division Pages); Martin Carrichner, Jose Marti (Endsheet Design), Arnold Escalera, Jacqui Fernandez, Richard Massey, Alejandro Meneses; WRITING: Anthony Archer, Alexandra Bastidas, Joie Fadde, Alexandra Gomez, Ana Lisa Gonzalez, Doreen Hansen, Bernadette Henry, Sarah Hudson, Juan Jimenez, Donna Libert, Cathy Passiglia, Jody Pincus, Richard Provost, Kenny Rosa, Maria Sanchez, Alan Scribner, Christiana Sommerville, GloryAnn Torres, Catherine Whan, Alan O. Young; SPECIAL THANKS: Blanca Arbito, Classic Studios, Edward Hollins, Umoja Kwanguvu, Kelly Johnson and the LaGuardia Archives, Andrew Saluga and Recreation Staff, Ted Schiffman of Taylor Publishing.

Preferential infection sites of Cysticercus bovis in cattle experimentally infected with Taenia saginata eggs

The preferential sites of infection of Cysticercus bovis were evaluated in the skeletal muscle and entrails of 25 cattle that were experimentally infected with Taenia saginata (2 x 10(4) eggs). Two other animals were not inoculated (control). Ninety days after inoculation, all the cattle were euthanized. The carcasses were deboned and dissected into 26 anatomical sections (masseter muscles, brain, tongue, esophagus, heart, diaphragm, lungs, liver, kidneys, spleen, top sirloin butt, bottom sirloin butt, outside round, top (inside) round, transversus abdominus, top sirloin cap, strip loin, full tenderloin, eye of round, knuckle, shoulder clod, foreshank, shank, chuck, back ribs, and tail muscles). The dissected tissues were sliced into 5 mm sections. From the 25 cattle, 9258 C. bovis (cysticerci) were recovered; 75.02% (6946) of these were recovered from skeletal muscles and 24.98% (2312) from the entrails. A high parasitism level was found in the shoulder clod (12.55%), heart (11.02%), liver (9.48%), masseter muscles (8.51%), chuck (8.25%), strip loin and full tenderloin (7.26%), knuckle (6.63%), and back ribs (5.53%), totaling 69.23% (5738) of all of the detected cysticerci. on the other hand, there was a low C. bovis parasitism level in the brain, spleen, tail muscles, kidneys, esophagus, and diaphragm, representing just 3.9% of the total number of cysticerci. Given these results, we conclude that specific skeletal musculature regions, such as the shoulder blade, chuck, strip loin and full tenderloin, knuckle, back ribs and top round, which are not officially examined in many countries, are effective sites to efficiently screen C. bovis infection. To date, these regions have not been considered as preferential sites of C. bovis infection. Based on our work, however, these regions deserve greater attention from health inspectors because they contained a greater number of Cysticercus than the other regions of carcasses that are parasitized by T. saginata larvae. (c) 2010 Elsevier Ltd. All rights reserved.

Distribution of Taenia saginata metacestodes: a comparison of routine meat inspection and carcase dissection results in experimentally infected calves

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Perfis de polietileno reciclado carregado com fibra de açaí

Foram obtidos perfis tubulares porosos de polietileno (PE) e de polietileno/fibra de açaí (PE/PA) 80/20 extrudados a partir de partículas granuladas de polietileno de alta densidade reciclado de embalagens pós-consumo de 600 μm, e deste com fibra de açaí de 300 μm. Para o processamento das peças foi desenvolvida uma extrusora mono-rosca de bancada, com sistema mecânico acionado por um motor elétrico de ½ CV (0,37 kw) controlado por um inversor de freqüência, com canhões, roscas, matriz e sistema de aquecimento substituíveis. Para permitir uma visualização didática de condições de operação do equipamento de modo simplificado foram realizados testes com parafina em canhão de vidro variando-se a velocidade de rotação do parafuso e perfil de temperatura, ajustando vazão mássica e pressão na saída. Para a extrusão dos perfis porosos foram realizados ensaios reológicos de PE e PE/FA sendo selecionado rosca, barril e matriz de alumínio; rosca com passo de 9 mm e relação comprimento diâmetro (L/D) 22, composta de um elemento misturador e um elemento de flutuação na zona de controle de vazão; ângulo entre o filete e o eixo da rosca 17º, folga entre a rosca e o barril 0,15 mm; rotação de 1,3 rpm; aquecimento ao longo do canhão de 120ºC; matriz tubular com 21 mm de diâmetro interno e mandril de 19 mm de diâmetro externo. Os perfis PE e PE/FA apresentaram poros com diâmetros médios de 0,7 e 0,6 mm; densidade relativa à água a 28ºC de 0,77 e 0,73; módulo de elasticidade de 1,002 e 2,601 GPa e máximo inchamento aparente do extrudado de 100 e 80%.

Óleo de linhaça na dieta de fêmeas e machos castrados Nelore x Canchim, terminados em confinamento

Pós-graduação em Zootecnia - FCAV

Serving Rural Nebraska Panhandle

I'm going to jump right into my topic tonight - Chuck Hibberd asked me to talk briefly about my ideas on serving rural Nebraska before our open-discussion. And serving rural Nebraska is a topic on which I have a great deal to say! So I'm going to talk fast here for 12 minutes or so, and then I'm looking forward to hearing what you have to say.

Analysis of three Xanthomonas axonopodis pv. citri effector proteins in pathogenicity and their interactions with host plant proteins

Xanthomonas axonopodis pv. citri, the bacterium responsible for citrus canker, uses effector proteins secreted by a type III protein secretion system to colonize its hosts. Among the putative effector proteins identified for this bacterium, we focused on the analysis of the roles of AvrXacE1, AvrXacE2 and Xac3090 in pathogenicity and their interactions with host plant proteins. Bacterial deletion mutants in avrXacE1, avrXacE2 and xac3090 were constructed and evaluated in pathogenicity assays. The avrXacE1 and avrXacE2 mutants presented lesions with larger necrotic areas relative to the wild-type strain when infiltrated in citrus leaves. Yeast two-hybrid studies were used to identify several plant proteins likely to interact with AvrXacE1, AvrXacE2 and Xac3090. We also assessed the localization of these effector proteins fused to green fluorescent protein in the plant cell, and observed that they co-localized to the subcellular spaces in which the plant proteins with which they interacted were predicted to be confined. Our results suggest that, although AvrXacE1 localizes to the plant cell nucleus, where it interacts with transcription factors and DNA-binding proteins, AvrXacE2 appears to be involved in lesion-stimulating disease 1-mediated cell death, and Xac3090 is directed to the chloroplast where its function remains to be clarified.

The 3D structure and function of digestive cathepsin L-like proteinases of Tenebrio molitor larval midgut

Cathepsin L-like proteinases (CAL) are major digestive proteinases in the beetle Tenebrio molitor. Procathepsin Ls 2 (pCAL2) and 3 (pCAL3) were expressed as recombinant proteins in Escherichia coil, purified and activated under acidic conditions. Immunoblot analyses of different T. molitor larval tissues demonstrated that a polyclonal antibody to pCAL3 recognized pCAL3 and cathepsin L 3 (CAD) only in the anterior two-thirds of midgut tissue and midgut luminal contents of T. molitor larvae. Furthermore, immunocytolocalization data indicated that pCAL3 occurs in secretory vesicles and microvilli in anterior midgut Therefore CAL3, like cathepsin L 2 (CAL2), is a digestive enzyme secreted by T. molitor anterior midgut CAD hydrolyses Z-FR-MCA and Z-RR-MCA (typical cathepsin substrates), whereas CAL2 hydrolyses only Z-FR-MCA. Active site mutants (pCAL2C25S and pCAL3C265) were constructed by replacing the catalytic cysteine with serine to prevent autocatalytic processing. Recombinant pCAL2 and pCAL3 mutants (pCAL2C25S and pCAL3C26S) were prepared, crystallized and their 3D structures determined at 1.85 and 2.1 angstrom, respectively. While the overall structure of these enzymes is similar to other members of the papain superfamily, structural differences in the S2 subsite explain their substrate specificities. The data also supported models for CAL trafficking to lysosomes and to secretory vesicles to be discharged into midgut contents. (C) 2012 Elsevier Ltd. All rights reserved.

Dynamic complex formation between HD-GYP, GGDEF and PilZ domain proteins regulates motility in Xanthomonas campestris

RpfG is a member of a class of wide spread bacterial two-component regulators with an HD-GYP cyclic di-GMP phosphodiesterase domain. In the plant pathogen Xanthomonas campestris, RpfG together with the sensor kinase RpfC regulates multiple factors as a response to the cell-to-cell Diffusible Signalling Factor (DSF). A dynamic physical interaction of RpfG with two diguanylate cyclase (GGDEF) domain proteins controls motility. Here we show that, contrary to expectation, regulation of motility by the GGDEF domain proteins does not depend upon their cyclic di-GMP synthetic activity. Furthermore we show that the complex of RpfG and GGDEF domain proteins recruits a specific PilZ domain adaptor protein, and this complex then interacts with the pilus motor proteins PilU and PiIT. The results support a model in which DSF signalling influences motility through the highly regulated dynamic interaction of proteins that affect pilus action. A specific motif that we identify to be required for HD-GYP domain interaction is conserved in a number of GGDEF domain proteins, suggesting that regulation via interdomain interactions is of broad relevance.

Calcium Binding to Leptospira Outer Membrane Antigen LipL32 Is Not Necessary for Its Interaction with Plasma Fibronectin, Collagen Type IV, and Plasminogen

LipL32 is the most abundant outer membrane protein from pathogenic Leptospira and has been shown to bind extracellular matrix (ECM) proteins as well as Ca2+. Recent crystal structures have been obtained for the protein in the apo-and Ca2+-bound forms. In this work, we produced three LipL32 mutants (D163-168A, Q67A, and S247A) and evaluated their ability to interact with Ca2+ and with ECM glycoproteins and human plasminogen. The D163-168A mutant modifies aspartate residues involved in Ca2+ binding, whereas the other two modify residues in a cavity on the other side of the protein structure. Loss of calcium binding in the D163-D168A mutant was confirmed using intrinsic tryptophan fluorescence, circular dichroism, and thermal denaturation whereas the Q67A and S247A mutants presented the same Ca2+ affinity as the wild-type protein. We then evaluated if Ca2+ binding to LipL32 would be crucial for its interaction with collagen type IV and plasma proteins fibronectin and plasminogen. Surprisingly, the wild-type protein and all three mutants, including the D163-168A variant, bound to these ECM proteins with very similar affinities, both in the presence and absence of Ca2+ ions. In conclusion, calcium binding to LipL32 may be important to stabilize the protein, but is not necessary to mediate interaction with host extracellular matrix proteins.

Extracytoplasmic function (ECF) sigma factor σF is involved in Caulobacter crescentus response to heavy metal stress

Background The α-proteobacterium Caulobacter crescentus inhabits low-nutrient environments and can tolerate certain levels of heavy metals in these sites. It has been reported that C. crescentus responds to exposure to various heavy metals by altering the expression of a large number of genes. Results In this work, we show that the ECF sigma factor σF is one of the regulatory proteins involved in the control of the transcriptional response to chromium and cadmium. Microarray experiments indicate that σF controls eight genes during chromium stress, most of which were previously described as induced by heavy metals. Surprisingly, σF itself is not strongly auto-regulated under metal stress conditions. Interestingly, σF-dependent genes are not induced in the presence of agents that generate reactive oxygen species. Promoter analyses revealed that a conserved σF-dependent sequence is located upstream of all genes of the σF regulon. In addition, we show that the second gene in the sigF operon acts as a negative regulator of σF function, and the encoded protein has been named NrsF (Negative regulator of sigma F). Substitution of two conserved cysteine residues (C131 and C181) in NrsF affects its ability to maintain the expression of σF-dependent genes at basal levels. Furthermore, we show that σF is released into the cytoplasm during chromium stress and in cells carrying point mutations in both conserved cysteines of the protein NrsF. Conclusion A possible mechanism for induction of the σF-dependent genes by chromium and cadmium is the inactivation of the putative anti-sigma factor NrsF, leading to the release of σF to bind RNA polymerase core and drive transcription of its regulon.