Relevant bibliographies by topics / Cashin

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Cashin'

Author: Grafiati
Published: 4 June 2021
Last updated: 2 February 2022

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Journal articles on the topic "Cashin"

1

IVERSON, STEPHANIE DAY. ""Early" Bonnie Cashin, before Bonnie Cashin Designs, Inc." Studies in the Decorative Arts 8, no. 1 (October 2000): 108–24. http://dx.doi.org/10.1086/studdecoarts.8.1.40662762.

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Kim, Injoo, Seung A. Lee, and George F. Sarofeen. "Characteristics of Signature Bonnie Cashin Designs." International Journal of Costume and Fashion 15, no. 1 (June 30, 2015): 51–74. http://dx.doi.org/10.7233/ijcf.2015.15.1.051.

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Kim, Injoo, and Juhyung Woo. "A Study on the Design of Bonnie Cashin." Korean Society of Fashion Design 18, no. 2 (June 30, 2018): 125–43. http://dx.doi.org/10.18652/2018.18.2.8.

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4

Bates, Timothy. "Rejoinder to Sheryll Cashin: Programs as Token Gestures." Economic Development Quarterly 14, no. 3 (August 2000): 250–55. http://dx.doi.org/10.1177/089124240001400303.

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Dallari, Sueli Gandolfi. "Resenha internacional: Universal Health Coverage for inclusive and sustainable development: a synthesis of 11 country case studies." Revista de Direito Sanitário 15, no. 3 (April 14, 2015): 325. http://dx.doi.org/10.11606/issn.2316-9044.v15i3p325-329.

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Resenha sobre a publicação "Universal Health Coverage for inclusive and sustainable development: a synthesis of 11 country case studies", Akiko Maeda, Edson Araujo, Cheryl Cashin, Joseph Harris, Naoki Ikegami, and Michael R. Reich (org.), International Bank for Reconstruction and Development / The World Bank <http://dx.doi.org/10.1596/978-1-4648-0297-3>
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Wang, Cathy. "Place, not race: A new vision of opportunity in America, by Sheryll Cashin." Journal of Urban Affairs 39, no. 4 (May 2, 2017): 586–88. http://dx.doi.org/10.1111/juaf.12271.

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7

Cohen, Joanna. "War Matters: Material Culture in the Civil War Era ed. by Joan E. Cashin." Journal of the Civil War Era 9, no. 4 (2019): 650–52. http://dx.doi.org/10.1353/cwe.2019.0084.

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Woods, Michael E. "War Matters: Material Culture in the Civil War Era ed. by Joan E. Cashin." Register of the Kentucky Historical Society 117, no. 2 (2019): 400–402. http://dx.doi.org/10.1353/khs.2019.0040.

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Sears, Christine E. "War Matters: Material Culture in the Civil War Era ed. by Joan E. Cashin." Journal of Southern History 85, no. 4 (2019): 914–16. http://dx.doi.org/10.1353/soh.2019.0254.

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Omelicheva, Mariya Y., and Olga Avdeyeva. "Teaching with Lecture or Debate? Testing the Effectiveness of Traditional versus Active Learning Methods of Instruction." PS: Political Science & Politics 41, no. 03 (June 18, 2008): 603–7. http://dx.doi.org/10.1017/s1049096508080815.

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Lecture is, arguably, the oldest known instructional technique used in the university setting. Since it was first employed in Plato's Academy, lecture has become an indispensable part of teaching favored across the college and university curriculum. Recently, this time-honored method of instruction has come under attack for its presumed inability to foster higher order cognitive and attitudinal goals (Cashin 1985; Day 1980; Frederick 1999; Renner 1993). Critics of traditional lecture-based formats call for their replacement with active learning approaches that provide students with an opportunity to meaningfully talk, interact, write, read, and reflect on the content, ideas, and issues of an academic subject (Meyers and Jones 1993, 6).
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Dissertations / Theses on the topic "Cashin"

1

KIM, EUN KYUNG. "PATTERN ANALYSIS ON THE WORKS OF BONNIE CASHIN FROM THE 1960S TO THE 1970S." University of Cincinnati / OhioLINK, 2002. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1021996954.

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2

Bute, Martha Jane. "Bonnie Cashin connecting the designer to the designed garment through a material culture analysis of five examples of her work, 1962-1975 /." [Ames, Iowa : Iowa State University], 2007.

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Weng, Yi-Lan. "The Cytoplasmic Adaptor Protein Caskin Participates in LAR-Mediated Motor Axon Guidance." Case Western Reserve University School of Graduate Studies / OhioLINK, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=case1301673851.

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4

Post, Antonie E. [Verfasser]. "Fractionation of bovine casein and enrichment of functional casein peptides / Antonie E. Post." München : Verlag Dr. Hut, 2012. http://d-nb.info/1023435446/34.

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Post, Antonie [Verfasser]. "Fractionation of bovine casein and enrichment of functional casein peptides / Antonie E. Post." München : Verlag Dr. Hut, 2012. http://d-nb.info/1023435446/34.

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6

Shammet, Khalid M. "Proteolytic Activity of Some Milk-Clotting Enzymes on K-casein and K-casein Macropeptide." DigitalCommons@USU, 1989. https://digitalcommons.usu.edu/etd/5371.

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This work reviews studies of bovine K-casein and specifically K-casein macropeptide. Properties of K-casein, its structure and heterogeneity, proteolytic activity of some milk clotting enzymes on K-casein, and K-casein sensitive bonds are discussed. Macropeptides of other species are also presented. The carbohydrate moieties of bovine macropeptide together with their biological and physiological functions are reviewed. Macropeptides were produced by enzymic hydrolysis from whole casein solution using crystalline chymosin (EC 3.4.23.4). Trichloroacetic acid (final concentrations 2, 8 and 12%) was added after 5, 30 and 60 min of incubation to precipitate protein and inactivate the enzyme. The filtrate was then exhaustively dialyzed against distilled water to remove trichloroacetic acid and small molecules. The dialyzate was lyophilized and stored at -20deg;c until required for analysis. These macropeptides were then compared using RP-HPLC with macropeptides obtained from purified K-casein isolates by the same method (15 min incubation). Proteolytic activity of some milk-clotting enzymes (chymosin, Mucor miehei rennet and Endothia parasitica rennet) and some proteinases (trypsin and chymotrypsin) on K-casein and macropeptide isolated from K-casein was followed by RP-HPLC. The milk-clotting enzymes were standardized to the same clotting activity using a Formagraph. Each enzyme was incubated with .5 mix-casein and macropeptide solutions (10 mg in 1 ml .05 MpH 6.6 phosphate buffer) at 37°C for various incubation times. Reactions were stopped by addition .5 ml of 8 Murea containing 10-5 Mpepstatin or .025 ml pepstatin (1 mg pepstatin in 1 ml methanol). These reaction mixtures were separated into fractions using RP-HPLC and chromatograms of the different enzymes compared.
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Zhou, Shuting. "Casein-phenolic interactions in food." Thesis, McGill University, 2011. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=103772.

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Protein-phenolic interactions are common in foods with reported effects on nutritional and functional properties of foods. The objectives of this research were to investigate the casein-phenolic acid interactions in a model system and in chocolate as a processed food product. Casein-phenolic acid interactions were induced by heat incubation of casein with protocatechuic acid or p-coumaric acid at 55 ℃ (pH 7, 2 h); caseins were isolated from milk chocolate and white chocolate by precipitating caseins at its isoelectric point (pH 4.6). Casein-phenolic complexes were identified using polyacrylamide gel electrophoresis (Native- and SDS-PAGE) and reversed-phase high performance liquid chromatography (RP-HPLC). Degree of hydrolysis of casein-phenolic complexes was investigated using tryptic hydrolysis; sodium dodecyl sulfate gel electrophoresis (SDS-PAGE) and reversed-phase high performance liquid chromatography (RP-HPLC) were used to identify the hydrolysates of casein-phenolic complexes. Total phenolic contents of original and defatted milk chocolate and casein isolated from milk chocolate (1.905, 1.644 and 1.018 mg/g respectively) were higher than those of original and defatted white chocolate and casein isolated from white chocolate (1.678, 0.723 and 0.000 mg/g respectively) respectively. Native- and SDS-PAGE results revealed that casein-phenolic interactions were induced by heat incubation and occurred during the processing of milk chocolate; minor changes in the migration of casein fractions and aggregation of casein subunits were observed after heat incubation of casein with protocatechuic acid and in casein isolated from milk chocolate; there is no observed change with Native- and SDS-PAGE electropherograms after casein incubated with p-coumaric acid and in casein isolated from white chocolate. In vitro hydrolysis of casein control (C), casein-protocatechuic acid complex (CPA), casein-p-coumaric acid complex (CCA), casein isolated from milk chocolate (CMC) and casein isolated from white chocolate (CWC) by trypsin showed degree of hydrolysis of 19.3 %, 18.6 %, 17.7 %, 10.4 % and 17.8 % respectively; SDS-PAGE revealed that the three major casein fractions α-, β- and κ-caseins in casein control, casein-protocatechuic acid complex, casein-p-coumaric acid complex and casein isolated from milk chocolate and white chocolate were hydrolyzed. Both protocatechuic acid and p-coumaric acid affected the peptide profiles of casein hydrolysates; the peptide profile of casein isolated from milk chocolate was affected by phenolic compounds.
Les interactions protéine-phénols sont courantes dans les aliments. Les études rapportent que ces interactions affectent les propriétés nutritionnelles et fonctionnelles des aliments. Les objectifs de cette recherche étaient d'étudier les interactions caséine-acides phénols dans un système modèle et dans un produit transformé à base de chocolat. Les interactions caséine-acides phénols ont été induites par la chaleur suite à une incubation de la caséine avec de l'acide protocatéchique ou de l'acide p-coumarique à 55 ℃ (pH 7, 2 h); les caséines ont été isolés du chocolat au lait et chocolat blanc en précipitant les caséines à son point isoélectrique (pH 4,6). Les complexes à base de caséine-phénolique ont été identifiés par électrophorèse en gel de polyacrylamide (non dénaturante et SDS-PAGE) et par la chromatographie en phase liquide à haute performance en phase inversée (CLHP-PI). Le degré d'hydrolyse des complexes caséine-phénoliques a été étudié par hydrolyse tryptique; l'électrophorèse en gel de polyacrylamide contenant du laurylsulfate de sodium (SDS-PAGE) et la chromatographie en phase liquide à haute performance en phase inversée (CLHP-PI) ont servi à identifier les hydrolysats des complexes à base de caséine-phénolique. Le contenu en phénols totaux du chocolat au lait d'origine et sans gras et de la caséine isolée de chocolat au lait (1,905, 1,644 et 1,018 mg / g respectivement) était plus élevé que celui du chocolat blanc original et sans gras et de la caséine isolée de chocolat blanc (1.678, 0.723 et 0,000 mg / g respectivement), respectivement. Les résultats de la chromatographie non dénaturante et SDS-PAGE ont révélé que les interactions caséine-phénols ont été induites par une incubation à la chaleur et sont survenues pendant le procédé du chocolat au lait; des changements mineurs dans la migration des fractions de caséine et de l'agrégation de sous-unités de caséine ont été observés après une incubation à la chaleur de la caséine avec de l'acide protocatéchique et dans la caséine isolée de chocolat au lait; il n'y a pas de changement observé avec les électrophérogrammes non dénaturante et SDS-PAGE après que la caséine ait été incubée avec de l'acide p-coumarique ni avec la caséine isolée à partir de chocolat blanc. L'hydrolyse in vitro de la caséine de contrôle (C), du complexe caséine-acide protocatéchique (CPA), du complexe caséine-acide p-coumarique (CCA), de la caséine isolée du chocolat au lait (CMC) et de la caséine isolée du chocolat blanc (CWC) par la trypsine ont montré un degré d'hydrolyse de 19,3%, 18,6%, 17,7%, 10,4% et 17,8% respectivement; SDS-PAGE a révélé que les trois principales fractions de caséine α-, β- et κ-caséine dans la caséine contrôle, le complexe caséine-acide protocatéchique, le complexe caséine-acide p-coumarique et la caséine isolée du chocolat au lait et du chocolat blanc ont été hydrolysées. L'acide protocatéchique et l'acide p-coumarique ont affecté le profil en peptides de la caséine; le profil en peptides de la caséine isolée de chocolat au lait a été affecté par les composés phénoliques.
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Oommen, Bonney S. "Casein Supramolecules: Structure and Coagulation Properties." DigitalCommons@USU, 2004. https://digitalcommons.usu.edu/etd/5518.

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The changes in quaternary structure of casein supramolecules with various physical and chemical treatments were studied using transmission electron microscopy, and a model to account for the changes is put forth. The effects of casein structure on coagulation properties were also studied. The sample preparation for transmission electron microscopy involved physical methods of fixation and flash freeing to preserve the structure of caseins in the sample. The structure of caseins in sodium and calcium caseinate varied with sodium caseinate not exhibiting any spherical structure as opposed to the spherical structure seen in calcium caseinate, non-fat dried milk and native milk. This difference in structure was carried over to rennet coagulum made from those sources of casein. Addition of calcium and phosphate to sodium and calcium caseinate, respectively, improved their coagulation properties. Hydration parameters such as time and shear of hydration affected the extent of hydration. High shear (733 s-1) or approximately 10 hr of hydration was required to disperse and hydrate the dried milk protein powders. Acidification and treatment with excess EDT A resulted in dissociation of casein supramolecules into various sizes and shapes. Heat treatment of milk in the presence of ethanol also resulted in its dissociation. High heat treatment of milk at various pH levels induced different types of whey protein casein interactions. All these changes can be explained using an irregular supramolecular structure of caseins based on a node and strand network of proteins and calcium phosphate nanoclusters. Such a filigreed sponge-like appearance is seen in native bovine milk and in milk of other species.
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Naressi, Bruna Cristina Machado. "Análise comparativa de genes das caseínas de búfalo /." Jaboticabal, 2015. http://hdl.handle.net/11449/123663.

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Orientador: Maria Elisabete Jorge Amaral
Coorientador: Nedenia Bonvinos Stafuzza
Banca: Rodrigo Pelicioni Savegnago
Banca: Paola Jocelan Scarin Provazzi
Resumo: Dentre as proteínas do leite, as caseínas (alfa-s1, alfa-s2, beta- e kapa-caseína) assumem papel de destaque devido ao alto valor nutritivo e às características físico-químicas que favorecem a fabricação de derivados do leite. Essas proteínas são codificadas pelos genes CSN1S1, CSN1S2, CSN2 e CSN3. A fim de realizar análise comparativa dos genes das caseínas de búfalo, o presente trabalho teve como objetivo a identificação, caracterização e sequenciamento de clones da biblioteca genômica de búfalo, visando analisar a estrutura molecular de genes das caseínas. Dentre os 33.792 clones avaliados, foram identificados dois clones positivos para genes das caseínas, um para o gene CSN1S1 (clone A/2) e outro para o gene CSN3 (clone L/8). Na sequência de DNA obtida a partir do clone A/2, foram identificados os genes CSN1S1 inteiro e CSN2 parcial, enquanto que nas sequências de DNA do clone L/8 identificou-se o gene CSN3 partial. O gene CSN1S1 apresentou 17.008 bp organizados em 19 éxons com tamanhos variando de 24 bp a 380 bp e 18 íntrons com tamanhos de 90 bp a 1.710 bp. As análises comparativas revelaram que os éxons e íntrons desse gene apresentaram conservação acima de 85% entre búfalo e boi. As porções do gene CSN2 identificadas incluíram o éxon 9 e parte do íntron 8, os quais mostraram conservação acima de 98% com as sequências correspondentes em boi. Já as sequências parciais do gene CSN3 abrangeram parte dos íntrons 2 e 3 e o íntron 4 completo, além dos éxons 3, 4 e 5. Estas sequências apresentaram conservação acima de 94% com as correspondentes em boi. As análises de identificação de sequências repetitivas mostraram que 43,83% e 44,98% das sequências de DNA do clone A/2 e L/8, respectivamente, são representadas por elementos retrotransposons. Nas análises comparativas, tanto o gene CSN1S1 quanto o gene CSN3 parcial apresentaram sequências repetitivas búfalo específicas. A sequência...
Abstract: Among milk proteins, the caseins (alpha-s1, alpha-s2, beta- and kappa-casein) play a crucial role considering their high nutritional value and physicochemical characteristics which contribute to the manufacture of dairy products. These proteins are encoded by the CSN1S1, CSN1S2, CSN2 and CSN3 genes, respectively. In order to analyze the buffalo casein genes and compare the sequences with other species, the goal of the present study was to identify, characterize and sequence clones from a buffalo genomic library. A total of 33,792 clones were evaluated, and two clones were identified as positive, one for the CSN1S1 gene (clone A/2) and other for the CSN3 gene (clone L/8). The DNA sequence from clone A/2 identified the whole CSN1S1 and a partial sequence from the CSN2 genes. The DNA sequence from clone L/8 revealed a partial sequence from the CSN3 gene. The CSN1S1 gene presented a total of 17,008 bp organized in 19 exons ranging from 24 bp to 380 bp and 18 introns ranging from 90 bp to 1,710 bp. Comparative analysis showed sequence conservation higher than 85% on exons and introns of the CSN1S1 gene when compared with the cattle gene sequence. The partial sequence from the CSN2 gene included exon 9 and part of intron 8, with conservation higher than 98% when compared with the cattle sequence. The partial sequences of the CSN3 gene included parts of the introns 2 and 3, the whole sequence of intron 4 and exons 3, 4 and 5. These sequences showed conservation higher than 94% with cattle. The identification of repetitive sequences showed that 43.83% of DNA sequence from clone A/2 and 44,98% from clone L/8 were represented by retrotransposable elements. Further comparative analysis showed buffalo specific repetitive sequences in the CSN1S1 gene and the partial CSN3 gene with when compared with other bovids species. The coding sequence of the buffalo CSN1S1 gene showed 98%, 93%, and 90% of identity with the correspondent sequences in cattle ...
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Naressi, Bruna Cristina Machado [UNESP]. "Análise comparativa de genes das caseínas de búfalo." Universidade Estadual Paulista (UNESP), 2015. http://hdl.handle.net/11449/123663.

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Made available in DSpace on 2015-06-17T19:33:34Z (GMT). No. of bitstreams: 0 Previous issue date: 2015-02-02. Added 1 bitstream(s) on 2015-06-18T12:48:23Z : No. of bitstreams: 1 000834199_20160202.pdf: 110591 bytes, checksum: 9b4d763896b837f183fbb81b557d4619 (MD5) Bitstreams deleted on 2016-02-03T15:35:13Z: 000834199_20160202.pdf,. Added 1 bitstream(s) on 2016-02-03T15:35:54Z : No. of bitstreams: 1 000834199.pdf: 1278335 bytes, checksum: 9ed66d4ca576eca0681d0113a356d68a (MD5)
Dentre as proteínas do leite, as caseínas (alfa-s1, alfa-s2, beta- e kapa-caseína) assumem papel de destaque devido ao alto valor nutritivo e às características físico-químicas que favorecem a fabricação de derivados do leite. Essas proteínas são codificadas pelos genes CSN1S1, CSN1S2, CSN2 e CSN3. A fim de realizar análise comparativa dos genes das caseínas de búfalo, o presente trabalho teve como objetivo a identificação, caracterização e sequenciamento de clones da biblioteca genômica de búfalo, visando analisar a estrutura molecular de genes das caseínas. Dentre os 33.792 clones avaliados, foram identificados dois clones positivos para genes das caseínas, um para o gene CSN1S1 (clone A/2) e outro para o gene CSN3 (clone L/8). Na sequência de DNA obtida a partir do clone A/2, foram identificados os genes CSN1S1 inteiro e CSN2 parcial, enquanto que nas sequências de DNA do clone L/8 identificou-se o gene CSN3 partial. O gene CSN1S1 apresentou 17.008 bp organizados em 19 éxons com tamanhos variando de 24 bp a 380 bp e 18 íntrons com tamanhos de 90 bp a 1.710 bp. As análises comparativas revelaram que os éxons e íntrons desse gene apresentaram conservação acima de 85% entre búfalo e boi. As porções do gene CSN2 identificadas incluíram o éxon 9 e parte do íntron 8, os quais mostraram conservação acima de 98% com as sequências correspondentes em boi. Já as sequências parciais do gene CSN3 abrangeram parte dos íntrons 2 e 3 e o íntron 4 completo, além dos éxons 3, 4 e 5. Estas sequências apresentaram conservação acima de 94% com as correspondentes em boi. As análises de identificação de sequências repetitivas mostraram que 43,83% e 44,98% das sequências de DNA do clone A/2 e L/8, respectivamente, são representadas por elementos retrotransposons. Nas análises comparativas, tanto o gene CSN1S1 quanto o gene CSN3 parcial apresentaram sequências repetitivas búfalo específicas. A sequência ...
Among milk proteins, the caseins (alpha-s1, alpha-s2, beta- and kappa-casein) play a crucial role considering their high nutritional value and physicochemical characteristics which contribute to the manufacture of dairy products. These proteins are encoded by the CSN1S1, CSN1S2, CSN2 and CSN3 genes, respectively. In order to analyze the buffalo casein genes and compare the sequences with other species, the goal of the present study was to identify, characterize and sequence clones from a buffalo genomic library. A total of 33,792 clones were evaluated, and two clones were identified as positive, one for the CSN1S1 gene (clone A/2) and other for the CSN3 gene (clone L/8). The DNA sequence from clone A/2 identified the whole CSN1S1 and a partial sequence from the CSN2 genes. The DNA sequence from clone L/8 revealed a partial sequence from the CSN3 gene. The CSN1S1 gene presented a total of 17,008 bp organized in 19 exons ranging from 24 bp to 380 bp and 18 introns ranging from 90 bp to 1,710 bp. Comparative analysis showed sequence conservation higher than 85% on exons and introns of the CSN1S1 gene when compared with the cattle gene sequence. The partial sequence from the CSN2 gene included exon 9 and part of intron 8, with conservation higher than 98% when compared with the cattle sequence. The partial sequences of the CSN3 gene included parts of the introns 2 and 3, the whole sequence of intron 4 and exons 3, 4 and 5. These sequences showed conservation higher than 94% with cattle. The identification of repetitive sequences showed that 43.83% of DNA sequence from clone A/2 and 44,98% from clone L/8 were represented by retrotransposable elements. Further comparative analysis showed buffalo specific repetitive sequences in the CSN1S1 gene and the partial CSN3 gene with when compared with other bovids species. The coding sequence of the buffalo CSN1S1 gene showed 98%, 93%, and 90% of identity with the correspondent sequences in cattle ...
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Books on the topic "Cashin"

1

Cashin, Bonnie. Bonnie Cashin: Practical dreamer. [S.l.]: Museum at the Fashion Institute of Technology, 2000.

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Nicole, Jai. Cashin' out: A novel. Brandywine, MD: Life Changing Books, 2012.

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First lady of the Confederacy: Varina Davis's Civil War / Joan E. Cashin. Cambridge, Mass: Belknap Press of Harvard University Press, 2006.

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Colebank, Susan. Cashing in. New York: Dutton Children's Books, 2009.

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Colebank, Susan. Cashing In. New York: Penguin USA, Inc., 2009.

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Coe, Manchester Alden. Effects of casein imports. [Washington, D.C.]: U.S. Department of Agriculture, Economic Research Service, National Economics Division, 1986.

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McMullan, Margaret. Cashay. Boston: Houghton Mifflin Harcourt, 2009.

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Cashing out death: Gretchen's story. North Charleston, South Carolina]: [CreateSpace], 2013.

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Kerth, Bill. Cashing in on government money. S.l: Lion Pub., 1987.

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Kerth, Bill. Cashing in on government money. S.l: Lion Pub., 1987.

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Book chapters on the topic "Cashin"

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Dalgleish, Douglas G. "Caseins and Casein Micelles at Interfaces." In ACS Symposium Series, 665–76. Washington, DC: American Chemical Society, 1987. http://dx.doi.org/10.1021/bk-1987-0343.ch041.

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Kang, Young, Rafael Jimenez-Flores, and Tom Richardson. "Casein Genes and Genetic Engineering of the Caseins." In Genetic Engineering of Animals, 95–111. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5110-8_9.

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Fox, P. F., and D. M. Mulvihill. "Casein." In Food Gels, 121–73. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0755-3_4.

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Gooch, Jan W. "Casein." In Encyclopedic Dictionary of Polymers, 122. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_1998.

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Pilato, Madison. "Casein." In Encyclopedia of Autism Spectrum Disorders, 531–32. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4419-1698-3_1287.

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Pilato, Madison. "Casein." In Encyclopedia of Autism Spectrum Disorders, 1–2. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4614-6435-8_1287-3.

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Bährle-Rapp, Marina. "Casein." In Springer Lexikon Kosmetik und Körperpflege, 92. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-71095-0_1704.

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Pilato, Madison. "Casein." In Encyclopedia of Autism Spectrum Disorders, 826–27. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-319-91280-6_1287.

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Yoshikawa, Masaaki, Hiroyuki Suganuma, Akira Shiota, Fumito Tani, Hachiro Usui, Kazuyoshi Kurahashi, and Hideo Chiba. "Casoxin D: A bradykinin agonist peptide derived from human casein." In Peptide Chemistry 1992, 572–75. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-1474-5_165.

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Bährle-Rapp, Marina. "Hydrolyzed Casein." In Springer Lexikon Kosmetik und Körperpflege, 268. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-71095-0_4961.

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Conference papers on the topic "Cashin"

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Krishnan, Nanjundi Karthick, Aditya Johri, Ramgopal Chandrasekaran, and Joyojeet Pal. "Cashing out." In ICTD '19: Tenth International Conference on Information and Communication Technologies and Development. New York, NY, USA: ACM, 2019. http://dx.doi.org/10.1145/3287098.3287103.

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Ma, Richard T. B., and Don Towsley. "Cashing in on caching." In CoNEXT '15: Conference on emerging Networking Experiments and Technologies. New York, NY, USA: ACM, 2015. http://dx.doi.org/10.1145/2716281.2836093.

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Akbarli, Elchin, Elshan ismayilov, and Mohammad Masalmah. "The Heaviest and Longest 13 3/8 Full-String Casing Run in the Caspian Sea Region." In SPE Annual Caspian Technical Conference. Society of Petroleum Engineers, 2019. http://dx.doi.org/10.2118/198348-ms.

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Nafikova, Svetlana, Amanmmamet Bugrayev, Salim Taoutaou, Gaygysyz Baygeldiyev, Ilshat Akhmetzianov, Guvanch Gurbanov, and Ihab Eliwa. "Elimination of the Sustained Casing Pressure using Self-Healing Cement in Turkmenistan Section of the Caspian Sea." In SPE Annual Technical Conference and Exhibition. Society of Petroleum Engineers, 2019. http://dx.doi.org/10.2118/195945-ms.

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Akbarli, Elchin, Elshan ismayilov, and Mohammad Masalmah. "The Heaviest and Longest 13 3/8 Full-String Casing Run in the Caspian Sea Region (Azeri)." In SPE Annual Caspian Technical Conference. Society of Petroleum Engineers, 2019. http://dx.doi.org/10.2118/198348-az.

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Simpson, P., and R. Alonso. "Data cashing in IR systems." In the 10th annual international ACM SIGIR conference. New York, New York, USA: ACM Press, 1987. http://dx.doi.org/10.1145/42005.42038.

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Dana Meredith Mears-Leiner and Jeffrey M Catchmark. "Biocompatible Cellulose-Casein-Mineral Composites." In 2011 Louisville, Kentucky, August 7 - August 10, 2011. St. Joseph, MI: American Society of Agricultural and Biological Engineers, 2011. http://dx.doi.org/10.13031/2013.37762.

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Zhang, Xiaoxun, Zhili Guo, Honglei Guo, Huijia Zhu, and Zhong Su. "CasJoin." In the 19th ACM international conference. New York, New York, USA: ACM Press, 2010. http://dx.doi.org/10.1145/1871437.1871714.

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Beaudaux, Julien, Antoine Gallais, Romain Kuntz, Julien Montavont, Thomas Noël, Damien Roth, Fabrice Theoleyre, and Erkan Valentin. "CASINO." In the 8th ACM Conference. New York, New York, USA: ACM Press, 2010. http://dx.doi.org/10.1145/1869983.1870033.

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Kang, Yiyun. "Casting." In SIGGRAPH '18: Special Interest Group on Computer Graphics and Interactive Techniques Conference. New York, NY, USA: ACM, 2018. http://dx.doi.org/10.1145/3202918.3203084.

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Reports on the topic "Cashin"

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Hall, Hanna, Jennifer Krivickas, Elizabeth Meyer, and George Sarofeen. Documenting the Bonnie Cashin Collection. Ames: Iowa State University, Digital Repository, 2014. http://dx.doi.org/10.31274/itaa_proceedings-180814-1108.

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Kim, Injoo. Review and Documentation of Signature Bonnie Cashin Designs. Ames: Iowa State University, Digital Repository, 2014. http://dx.doi.org/10.31274/itaa_proceedings-180814-1099.

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Fielding, Randall Sidney. Glovebox Advanced Casting System Casting Optimization. Office of Scientific and Technical Information (OSTI), March 2016. http://dx.doi.org/10.2172/1262490.

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Makhlouf M. Makhlouf and Diran Apelian. Casting Characteristics of Aluminum Die Casting Alloys. Office of Scientific and Technical Information (OSTI), February 2002. http://dx.doi.org/10.2172/792701.

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Novichkova, Tatiana. Caspian Sea. Edited by Nikolay Komedchikov. Entsiklopediya, January 2012. http://dx.doi.org/10.15356/dm2015-12-02-4.

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Mackowiak, Brady. Casting Development Report for EFF-W Casting Furnace. Office of Scientific and Technical Information (OSTI), September 2017. http://dx.doi.org/10.2172/1482124.

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Wilde, R. (Continuous casting 1985). Office of Scientific and Technical Information (OSTI), June 1985. http://dx.doi.org/10.2172/7171966.

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Makhlouf M. Makhlouf and Diran Apelian. Clean Metal Casting. Office of Scientific and Technical Information (OSTI), February 2002. http://dx.doi.org/10.2172/793152.

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Shapiro, A. B., and W. J. III Comfort. LLNL casting technology. Office of Scientific and Technical Information (OSTI), January 1994. http://dx.doi.org/10.2172/10133336.

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Sabau, Adrian S., and Nick Cannell. Predicting Pattern Tooling and Casting Dimensions for Investment Casting, Phase III. Office of Scientific and Technical Information (OSTI), December 2007. http://dx.doi.org/10.2172/923051.

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