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Relevant bibliographies by topics / Formin3

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Academic literature on the topic 'Formin3'

Author: Grafiati

Published: 4 June 2021

Last updated: 5 February 2022

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Journal articles on the topic "Formin3"

1

Ye, Jianrong, Yiyan Zheng, An Yan, et al. "Arabidopsis Formin3 Directs the Formation of Actin Cables and Polarized Growth in Pollen Tubes." Plant Cell 21, no. 12 (2009): 3868–84. http://dx.doi.org/10.1105/tpc.109.068700.

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Tanaka, Hiromasa, Etsuko Takasu, Toshiro Aigaki, Kagayaki Kato, Shigeo Hayashi, and Akinao Nose. "Formin3 is required for assembly of the F-actin structure that mediates tracheal fusion in Drosophila." Developmental Biology 274, no. 2 (2004): 413–25. http://dx.doi.org/10.1016/j.ydbio.2004.07.035.

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Chang, Mee-Sung, and Hyun-Soo Kim. "Exploration of Formen as an Art Therapeutic Component : Focusing on Functions of Formen in Children’s Feeling Dimension." Journal of Arts Psychotherapy 15, no. 1 (2019): 339–65. http://dx.doi.org/10.32451/kjoaps.2019.15.1.339.

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Silkworth, William T., Kristina L. Kunes, Grace C. Nickel, Martin L. Phillips, Margot E. Quinlan, and Christina L. Vizcarra. "The neuron-specific formin Delphilin nucleates nonmuscle actin but does not enhance elongation." Molecular Biology of the Cell 29, no. 5 (2018): 610–21. http://dx.doi.org/10.1091/mbc.e17-06-0363.

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The formin Delphilin binds the glutamate receptor, GluRδ2, in dendritic spines of Purkinje cells. Both proteins play a role in learning. To understand how Delphilin functions in neurons, we studied the actin assembly properties of this formin. Formins have a conserved formin homology 2 domain, which nucleates and associates with the fast-growing end of actin filaments, influencing filament growth together with the formin homology 1 (FH1) domain. The strength of nucleation and elongation varies widely across formins. Additionally, most formins have conserved domains that regulate actin assembly through an intramolecular interaction. Delphilin is distinct from other formins in several ways: its expression is limited to Purkinje cells, it lacks classical autoinhibitory domains, and its FH1 domain has minimal proline-rich sequence. We found that Delphilin is an actin nucleator that does not accelerate elongation, although it binds to the barbed end of filaments. In addition, Delphilin exhibits a preference for actin isoforms, nucleating nonmuscle actin but not muscle actin, which has not been described or systematically studied in other formins. Finally, Delphilin is the first formin studied that is not regulated by intramolecular interactions. We speculate how the activity we observe is consistent with its localization in the small dendritic spines.

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Vizcarra, Christina L., Batbileg Bor, and Margot E. Quinlan. "The Role of Formin Tails in Actin Nucleation, Processive Elongation, and Filament Bundling." Journal of Biological Chemistry 289, no. 44 (2014): 30602–13. http://dx.doi.org/10.1074/jbc.m114.588368.

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Formins are multidomain proteins that assemble actin in a wide variety of biological processes. They both nucleate and remain processively associated with growing filaments, in some cases accelerating filament growth. The well conserved formin homology 1 and 2 domains were originally thought to be solely responsible for these activities. Recently a role in nucleation was identified for the Diaphanous autoinhibitory domain (DAD), which is C-terminal to the formin homology 2 domain. The C-terminal tail of the Drosophila formin Cappuccino (Capu) is conserved among FMN formins but distinct from other formins. It does not have a DAD domain. Nevertheless, we find that Capu-tail plays a role in filament nucleation similar to that described for mDia1 and other formins. Building on this, replacement of Capu-tail with DADs from other formins tunes nucleation activity. Capu-tail has low-affinity interactions with both actin monomers and filaments. Removal of the tail reduces actin filament binding and bundling. Furthermore, when the tail is removed, we find that processivity is compromised. Despite decreased processivity, the elongation rate of filaments is unchanged. Again, replacement of Capu-tail with DADs from other formins tunes the processive association with the barbed end, indicating that this is a general role for formin tails. Our data show a role for the Capu-tail domain in assembling the actin cytoskeleton, largely mediated by electrostatic interactions. Because of its multifunctionality, the formin tail is a candidate for regulation by other proteins during cytoskeletal rearrangements.

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Isogai, Tadamoto, and Metello Innocenti. "New nuclear and perinuclear functions of formins." Biochemical Society Transactions 44, no. 6 (2016): 1701–8. http://dx.doi.org/10.1042/bst20160187.

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Formin family proteins (formins) represent an evolutionary conserved protein family encoded in the genome of a wide range of eukaryotes. Formins are hallmarked by a formin homology 1 (FH1) domain juxtaposed to an FH2 domain whereby they control actin and microtubule dynamics. Not surprisingly, formins are best known as key regulators of the cytoskeleton in a variety of morphogenetic processes. However, mounting evidence implicates several formins in the assembly and organization of actin within and around the nucleus. In addition, actin-independent roles for formins have recently been discovered. In this mini-review, we summarize these findings and highlight the novel nuclear and perinulcear functions of formins. In light of the emerging new biology of formins, we also discuss the fundamental principles governing the versatile activity and multimodal regulation of these proteins.

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Dong, Yuqing, David Pruyne, and Anthony Bretscher. "Formin-dependent actin assembly is regulated by distinct modes of Rho signaling in yeast." Journal of Cell Biology 161, no. 6 (2003): 1081–92. http://dx.doi.org/10.1083/jcb.200212040.

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Formins are actin filament nucleators regulated by Rho-GTPases. In budding yeast, the formins Bni1p and Bnr1p direct the assembly of actin cables, which guide polarized secretion and growth. From the six yeast Rho proteins (Cdc42p and Rho1–5p), we have determined that four participate in the regulation of formin activity. We show that the essential function of Rho3p and Rho4p is to activate the formins Bni1p and Bnr1p, and that activated alleles of either formin are able to bypass the requirement for these Rho proteins. Through a separate signaling pathway, Rho1p is necessary for formin activation at elevated temperatures, acting through protein kinase C (Pkc1p), the major effector for Rho1p signaling to the actin cytoskeleton. Although Pkc1p also activates a MAPK pathway, this pathway does not function in formin activation. Formin-dependent cable assembly does not require Cdc42p, but in the absence of Cdc42p function, cable assembly is not properly organized during initiation of bud growth. These results show that formin function is under the control of three distinct, essential Rho signaling pathways.

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Sherer, Laura A., Mark E. Zweifel, and Naomi Courtemanche. "Dissection of two parallel pathways for formin-mediated actin filament elongation." Journal of Biological Chemistry 293, no. 46 (2018): 17917–28. http://dx.doi.org/10.1074/jbc.ra118.004845.

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Formins direct the elongation of unbranched actin filaments that are incorporated into a diverse set of cytoskeletal structures. Elongation of formin-bound filaments occurs along two parallel pathways. The formin homology 2 (FH2) pathway allows actin monomers to bind directly to barbed ends bound by dimeric FH2 domains. The formin homology 1 (FH1) pathway involves transfer of profilin-bound actin to the barbed end from polyproline tracts located in the disordered FH1 domains. Here, we used a total internal reflection fluorescence (TIRF) microscopy-based fluorescence approach to determine the fraction of actin subunits incorporated via the FH1 and FH2 pathways during filament elongation mediated by two formins. We found that the fraction of filament elongation that occurs via each pathway directly depends on the efficiency of the other pathway, indicating that these two pathways compete with each other for subunit addition by formins. We conclude that this competition allows formins to compensate for changes in the efficiency of one pathway by adjusting the frequency of subunit addition via the other, thus increasing the overall robustness of formin-mediated actin polymerization.

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Kollárová, Eva, Anežka Baquero Forero, Lenka Stillerová, Sylva Přerostová, and Fatima Cvrčková. "Arabidopsis Class II Formins AtFH13 and AtFH14 Can Form Heterodimers but Exhibit Distinct Patterns of Cellular Localization." International Journal of Molecular Sciences 21, no. 1 (2020): 348. http://dx.doi.org/10.3390/ijms21010348.

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Formins are evolutionarily conserved multi-domain proteins participating in the control of both actin and microtubule dynamics. Angiosperm formins form two evolutionarily distinct families, Class I and Class II, with class-specific domain layouts. The model plant Arabidopsis thaliana has 21 formin-encoding loci, including 10 Class II members. In this study, we analyze the subcellular localization of two A. thaliana Class II formins exhibiting typical domain organization, the so far uncharacterized formin AtFH13 (At5g58160) and its distant homolog AtFH14 (At1g31810), previously reported to bind microtubules. Fluorescent protein-tagged full length formins and their individual domains were transiently expressed in Nicotiana benthamiana leaves under the control of a constitutive promoter and their subcellular localization (including co-localization with cytoskeletal structures and the endoplasmic reticulum) was examined using confocal microscopy. While the two formins exhibit distinct and only partially overlapping localization patterns, they both associate with microtubules via the conserved formin homology 2 (FH2) domain and with the periphery of the endoplasmic reticulum, at least in part via the N-terminal PTEN (Phosphatase and Tensin)-like domain. Surprisingly, FH2 domains of AtFH13 and AtFH14 can form heterodimers in the yeast two-hybrid assay—a first case of potentially biologically relevant formin heterodimerization mediated solely by the FH2 domain.

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Bersee, H. E. N., S. Lindstedt, and A. Beukers. "C-4 DIAPHRAGM FORMING OF THERMOSET COMPOSITES(Session: Forming I)." Proceedings of the Asian Symposium on Materials and Processing 2006 (2006): 51. http://dx.doi.org/10.1299/jsmeasmp.2006.51.

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Dissertations / Theses on the topic "Formin3"

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Cristea, Laura G. "The Expression, Identification and Biochemical Characterization of the Extracellular Domain of Arabidopsis AFH2." Ohio University / OhioLINK, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=ohiou1417707960.

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Kulacz, Wojciech. "Regulation of Inverted Formin-1 (INF1) by Microtubule-Affinity Regulating Kinase 2 (MARK2)." Thèse, Université d'Ottawa / University of Ottawa, 2012. http://hdl.handle.net/10393/22801.

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The actin and microtubule cytoskeleton plays a critical role in the establishment of cell polarity. Cell processes like mitosis and migration rely on the reorganization of the cytoskeleton to properly function. One driver of cell polarity is the formin, Inverted Formin-1 (INF1). INF1 is able to induce F-actin formation, activate the Serum Response Factor (SRF) pathway, stabilize microtubules, associate with microtubules, and disperse the Golgi body. Regulation of INF1 is unique, since it does not possess conserved formin regulatory domains. However, INF1 does possess many potential phosphorylation sites. In this study, we demonstrate that INF1’s ability to induce F-actin stress fibers and activate SRF is inhibited by Microtubule-Affinity Regulating Kinase 2 (MARK2). Inhibition of INF1’s actin polymerization activity by MARK2 likely occurs near INF1’s C-terminus. However, MARK2 was unable to inhibit INF1’s ability to stabilize microtubules, associate with microtubules, and disperse the Golgi. Furthermore, we show that INF1 overexpression is associated with primary cilium absence and in some cases, the presence of long cilia, suggesting that INF1 plays a role in primary cilium formation.

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Shouler, Daniel Reginald. "Expanded forming limit testing for sheet forming processes." Thesis, University of Cambridge, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.609473.

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Kerleau, Mikaël. "Régulation biochimique et mécanique de l'assemblage de filaments d'actine par la formine." Thesis, Université Paris-Saclay (ComUE), 2017. http://www.theses.fr/2017SACLS583/document.

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Pour la cellule, l’assemblage du cytosquelette d’actine joue un rôle central dans son déplacement, sa division ou sa morphogenèse. Cette réorganisation est orchestrée par des protéines régulatrices et des contraintes mécaniques. Savoir comment les combinaisons de ces actions biochimiques et physiques régulent les différentes architectures d’actine reste un véritable défi.La formine protéine est un régulateur essentiel de l’actine. Ancrée à la membrane, elle assemble les filaments d’actine (nucléation et élongation) présents dans des architectures linéaires et non branchées. La formine est impliquée notamment dans la génération de filopodes, protrusions guidant la locomotion cellulaire.Une propriété remarquable est sa capacité à suivre processivement le bout barbé d’un filament qu’elle allonge, tout en stimulant son élongation en présence de profiline. La régulation de cette processivité de la formine est encore à clarifier. C’est une caractéristique importante, intervenant dans le contrôle de la longueur des filaments, dont les connaissances sont à approfondir.L’étude de cette processivité est facilitée par l’utilisation d’un outil microfluidique novateur pour l’étude de la dynamique de multiples filaments individuels d’actine in vitro. Au sein d’une chambre en PDMS, les filaments sont ancrés à la surface par un seul bout, le reste s’alignant avec le flux. Nous pouvons précisément y changer l’environnement biochimique,tandis que la friction visqueuse sur les filaments permet d’exercer une tension contrôlée sur chacun d’entre eux.Simultanément à l’action de la formine au bout barbé, j’étudie l’effet d’autres protéines ou de la vitesse d’élongation sur sa processivité, en mesurant son taux de détachement. Par ailleurs nous pouvons reproduire l’ancrage membranaire cellulaire en attachant spécifiquement nos formines à la surface. Dans la chambre, par l’intermédiaire du filament qu’elle allonge, nous pouvons alors exercer des forces et en étudier l’effet sur la formine.Premièrement, j’ai étudié l’impact de la protéine de coiffe (CP) sur l’activité de la formine au bout barbé. La liaison de ces deux protéines aubout barbé a jusqu’ici été considérée mutuellement exclusive. Nous avons observé qu’elles peuvent toutefois se retrouver simultanément liées au bout barbé, au sein d’un complexe à courte durée de vie. Ce complexe ternaire est capable de stopper l’activité du bout barbé même si l’affinité d’une protéine est réduite par la présence de l’autre. Nous proposons qu’une compétition entre la protéine de coiffe et la formine régule la dynamique du bout barbé dans des architectures où les longueurs doivent être hautement contrôlées.J’ai ensuite étudié l’influence de divers facteurs sur la processivité. La processivité est très sensible à la présence du sel et à la fraction demarquage fluorescent utilisée dans nos expériences. Nous avons également observé l’effet de la vitesse d’élongation, qui peut être modifiée en changeant la concentration en actine ou en profiline. D’une part, l’actine réduit la processivité, à n’importe quelle concentration de profiline. D’autre part, la concentration en profiline augmente cette processivité,indépendamment du taux d’élongation. Cela suggère qu’une incorporation de monomère diminue la processivité, tandis que la profiline, par sa présence au bout barbé, l’augmente.Enfin, la tension exercée sur les formines abaisse fortement la processivité : quelques piconewtons réduisent la processivité de plusieurs ordres de grandeurs. Cet effet, purement mécanique, prédomine sur les facteurs biochimiques. Ces résultats nous indiquent que les contraintes mécaniques de tension joueraient un rôle prédominant dans le contexte cellulaire. Cette étude nous aide à construire un modèle plus complet de l’élongation processive par les formines.En conclusion, ce projet permet de mieux comprendre le fonctionnement moléculaire de la formine, en particulier le mécanisme de l’élongation processive et de sa régulation<br>Actin filament assembly plays a pivotal role in cellular processes such as cell motility, morphogenis or division. Elucidating how the actin cytoskeleton is globally controlled remains a complex challenge. We know that it is orchestrated both by actin regulatory proteins and mechanical constraints.The formin protein is an essential actin regulator. Anchored to the cell membrane, it is responsible for the assembly (nucleation and elongation) of actin filaments found in linear and unbranched architectures. It is notably involved in the generation of filopodia protrusions at the leading edge of a motile cell. One important feature is that it processively tracks the barbed end of an actin filament, while stimulating its polymerization in the presence of profilin.Formin processivity and its regulation is not yet completely understood. As an important factor determining the length of the resulting filament, it must be investigated further.A perfect assay to look at formin processivity in vitro is an innovative microfuidics assay coupled to TIRF microscopy, pioneered by the team, to simultaneously track tens of individual filaments. In a designed chamber,filaments are anchored to the surface by one end, and aligned with the solution flow. We can precisely control the biochemical environment of the filaments. Moreover, we can exert and modulate forces on filaments, due to the viscous drag of flowing solutions. By varying chemical conditions during formin action at the barbed end, I investigated how others proteins or the elongation rate can modulate formin processivity, by looking at the detachment rate of formins.Moreover, we can mimic the membrane anchoring in the cell by specifically attaching formins at the surface. In our chamber, through the filament they elongate, we can apply force to formins.In complement to biochemical studies, we then investigate the effect oftension on their processivity.I first investigated the impact of a capping protein on formin action at the barbed end. Their barbed end binding is thought to be mutually exclusive.We measured that the affinity of one protein is reduced by the presence of the other. However we observed they both can bind simultaneously the barbed end, in a transient complex, which block barbed end elongation.Competition of formin and CP would regulate barbed end dynamics in a cell situation where length is tightly controlled.I next studied formin processivity dependence on various parameters. We show that processivity is sensitive to salt and labelling fraction used in our solutions. We also looked at how processivity is affected by the elongation rate, which can either be varied by actin or profilin concentration. On one hand, actin concentration reduces processivity, at any given concentrationsof profilin. On the other hand, raising the concentration of profilin increasesprocessivity, regardless of the elongation rate. This indicates that theincorporation of actin monomers decreases processivity while in contrast,the presence of the profilin at the barbed end increases it.Moreover, tension exerted on formin was observed to largely favor its detachment. In a quantitative matter, the effect of tension prevails over anyothers biochemical factor on processivity : only a few piconewtons decreaseit by several orders of magnitude. This important effect helps us build amore complete model of processive elongation. These results indicate thatmechanical stress is likely to play an important role in a cellular context.In conclusion, this project brings insights into the molecular properties offormin and helps to decipher the mechanism of processive elongation and its regulation

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Ramalingam, Nagendran. "Diaphanous-related formins." Diss., lmu, 2009. http://nbn-resolving.de/urn:nbn:de:bvb:19-106803.

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Grasty, Lawrence Victor. "Shot peen forming." Thesis, University of Cambridge, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.260449.

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Ellison, Samuel C. "Forming Ritual Reality." University of Cincinnati / OhioLINK, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1282576025.

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Sanay, Berkay. "Prediction Of Plastic Instability And Forming Limits In Sheet Metal Forming." Master's thesis, METU, 2010. http://etd.lib.metu.edu.tr/upload/12612486/index.pdf.

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The Forming Limit Diagram (FLD) is a widely used concept to represent the formability of thin metallic sheets. In sheet metal forming processes, plastic instability may occur, leading to defective products. In order to manufacture defect free products, the prediction of the forming limits of sheet metals is a very important issue. FLD&rsquo<br>s can be obtained by several experimental, empirical and theoretical methods. However, the suitability and the accuracy of these methods for a given material may vary. In this study, FLD&rsquo<br>s are predicted by simulating Nakazima test using finite element software Pam-Stamp 2G. Strain propagation phenomenon is used to evaluate the limit strains from the finite element simulations. Two different anisotropic materials, AA2024-O and SAE 1006, are considered throughout the study and for each material, 7 different specimen geometries are analyzed. Furthermore, FLD&rsquo<br>s are predicted by theoretical approaches namely<br>Keeler&rsquo<br>s model, maximum load criteria, Swift-Hill model and Storen-Rice model. At the end of the study, the obtained FLD&rsquo<br>s are compared with the experimental results. It has been found that strain propagation phenomenon results for SAE 1006 are in a good agreement with the experimental results<br>however it is not for AA2024-O. In addition, theoretical models show some variations depending on the material considered. It has been observed that forming limit prediction using strain propagation phenomena with FE method can substantially reduce the time and cost for experimental work and trial and error process.

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Kamal, Manish. "A uniform pressure electromagnetic actuator for forming flat sheets." Connect to resource, 2005. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1127230699.

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Thesis (Ph. D.)--Ohio State University, 2005.<br>Title from first page of PDF file. Document formatted into pages; contains xxi, 261 p.; also includes graphics (some col.). Includes bibliographical references (p. 244-254). Available online via OhioLINK's ETD Center

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Tangirala, Sailesh Kumar. "EXPERIMENTAL AND NUMERICAL INVESTIGATION OF PLASMA-JET FORMING." UKnowledge, 2006. http://uknowledge.uky.edu/gradschool_theses/361.

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Sheet metal forming has found increasing applications in modern industries. To eliminate use of expensive tools during product development, thermal forming, a rapid prototyping process that is flexible enough to decrease costs has been developed. Thermal forming processes use a heat source to perform the required deformation mainly by creating a thermal difference along the thickness of the sheet. Gas flames, lasers and plasma heat sources have been used for sheet metal bending by thermal forming. An alternative to laser and gas flames, plasma-jet forming has been developed that uses a non-transferred plasma arc as a heat source. The plasma-jet forming system uses a highly controllable non-transferred plasma torch as a heat source to create the necessary thermal gradient in the sheet metal that causes the required plastic deformation. Various experiments to produce simple linear bends and other complex shapes have been conducted by using different scanning options and coupling techniques. A computer simulated model using finite element method is being developed to study key parameters affecting this process and also to measure the thermal transient temperature distribution during the process. A predictive model to relate the deformation to the temperature gradient for various materials is being developed. Simulation results that are in accordance to experimental observations will further improve this material forming process to be highly controllable and more accurate

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Books on the topic "Formin3"

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M, Caddell Robert, ed. Metal forming. 3rd ed. Cambridge University Press, 2007.

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Thermo forming. Hanser Publishers, 1987.

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Forming hypotheses. Rosen Pub. Group's PowerKids Press, 2007.

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Filonov, I. P. Mekhanika prot͡s︡essov obkatki. "Nauka i tekhnika", 1985.

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Kiln forming glass. Crowood, 2010.

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Deer, W. A. Rock-forming minerals. 2nd ed. Geological Society, 1997.

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Sheet metal forming. Hilger, 1991.

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Spilsbury, Richard. Forming a band. Capstone Raintree, 2015.

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A, Howie R., and Zussman J, eds. Rock-forming minerals. 2nd ed. Geological Society, 1997.

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Berthoff, Ann E. Forming, thinking, writing. 2nd ed. Boynton/Cook Publishers, 1988.

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Book chapters on the topic "Formin3"

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Olowinsky, Alexander. "Forming." In Tailored Light 2. Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-642-01237-2_12.

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Gooch, Jan W. "Forming." In Encyclopedic Dictionary of Polymers. Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_5240.

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Kumar, Kaushik, Hridayjit Kalita, Divya Zindani, and J. Paulo Davim. "Forming." In Materials Forming, Machining and Tribology. Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-21066-3_4.

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Appel, F., H. Kestler, and H. Clemens. "Forming." In Intermetallic Compounds - Principles and Practice. John Wiley & Sons, Ltd, 2002. http://dx.doi.org/10.1002/0470845856.ch29.

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Rahaman, M. N. "Forming." In Inorganic Reactions and Methods. John Wiley & Sons, Inc., 2007. http://dx.doi.org/10.1002/9780470145333.ch14.

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Rosato, Donald V., and Dominick V. Rosato. "Forming." In Plastics Processing Data Handbook. Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-010-9658-4_5.

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Beiss, P. "Spray forming and continuous forming." In Powder Metallurgy Data. Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/10689123_10.

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Wightwick, Jane, and Mahmoud Gaafar. "Forming questions." In Mastering Arabic Grammar. Macmillan Education UK, 2005. http://dx.doi.org/10.1007/978-1-137-14586-4_9.

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Howie, J. G. R. "Forming ideas." In Research in General Practice. Springer US, 1989. http://dx.doi.org/10.1007/978-1-4899-2981-5_3.

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Mang, Theo. "Forming Lubricants." In Lubricants and Lubrication. Wiley-VCH Verlag GmbH & Co. KGaA, 2017. http://dx.doi.org/10.1002/9783527645565.ch15.

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Conference papers on the topic "Formin3"

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Avrahami, Daniel, and Scott E. Hudson. "Forming interactivity." In the conference. ACM Press, 2002. http://dx.doi.org/10.1145/778712.778735.

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Girard, Patrick, Zohir Benrabah, and Hicham Mir. "Controlling the Forming of Thermoplastics through Forming Power." In SAE 2013 World Congress & Exhibition. SAE International, 2013. http://dx.doi.org/10.4271/2013-01-0602.

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Dang, T., L. M. Tebaay, S. Gies, and A. E. Tekkaya. "Multiple forming tools in incremental forming – Influence of the forming strategies on sheet contour." In ESAFORM 2016: Proceedings of the 19th International ESAFORM Conference on Material Forming. Author(s), 2016. http://dx.doi.org/10.1063/1.4963462.

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Magee, J., K. G. Watkins, and T. Hennige. "Symmetrical laser forming." In ICALEO® ‘97: Proceedings of the Laser Applications in the Medical Devices Industry Conference. Laser Institute of America, 1999. http://dx.doi.org/10.2351/1.5059287.

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5

Matson, Rebecca. "Re-forming information." In the 19th annual international conference. ACM Press, 2001. http://dx.doi.org/10.1145/501516.501540.

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Schuocker, Dieter. "Laser-assisted forming." In High-Power Laser Ablation III. SPIE, 2000. http://dx.doi.org/10.1117/12.407342.

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Alotaibi, T., B. M. Novac, P. Senior, et al. "Magneto-forming studies." In 2017 IEEE 21st International Conference on Pulsed Power (PPC). IEEE, 2017. http://dx.doi.org/10.1109/ppc.2017.8291316.

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Vanier, Luc, Hank Kaczmarski, and Lance Chong. "Forming the dots." In the SIGGRAPH 2003 conference. ACM Press, 2003. http://dx.doi.org/10.1145/965400.965530.

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CÔTÉ, ROBIN. "FORMING ULTRACOLD MOLECULES." In Contributions to Atomic, Molecular, and Optical Physics, Astrophysics, and Atmospheric Physics. PUBLISHED BY IMPERIAL COLLEGE PRESS AND DISTRIBUTED BY WORLD SCIENTIFIC PUBLISHING CO., 2009. http://dx.doi.org/10.1142/9781848164703_0022.

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Li, Ji, and Gary J. Cheng. "Forming limit and fracture mode of microscale laser dynamic forming." In PICALO 2010: 4th Pacific International Conference on Laser Materials Processing, Micro, Nano and Ultrafast Fabrication. Laser Institute of America, 2010. http://dx.doi.org/10.2351/1.5057251.

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Reports on the topic "Formin3"

1

Blue, C. A., V. K. Sikka, Jung-Hoon Chun, and T. Ando. Uniform-droplet spray forming. Office of Scientific and Technical Information (OSTI), 1997. http://dx.doi.org/10.2172/494112.

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2

Switzner, Nathan, and Dick Henry. Spin-forming Project Report. Office of Scientific and Technical Information (OSTI), 2009. http://dx.doi.org/10.2172/952564.

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3

Chow, T. S., T. A. Biesiada, A. Sunwoo, J. Long, T. Anklam, and S. W. Kang. Uranium alloy forming process research. Office of Scientific and Technical Information (OSTI), 1997. http://dx.doi.org/10.2172/507837.

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4

Rhee, M., R. Becker, R. Couch, and M. Li. Modeling Production Plant Forming Processes. Office of Scientific and Technical Information (OSTI), 2004. http://dx.doi.org/10.2172/918410.

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MacCallum, Danny O'Neill, Chung-Nin Channy Wong, Gerald Albert Knorovsky, et al. Laser based micro forming and assembly. Sandia National Laboratories, 2006. http://dx.doi.org/10.2172/899077.

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6

Kohler, Leslie K., Louis F. Aprigliano, and A. S. Rao. Spray Forming Iron Based Amorphous Metals. Defense Technical Information Center, 2003. http://dx.doi.org/10.21236/ada418501.

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7

McHugh, K. Spray forming lead strip. Final report. Office of Scientific and Technical Information (OSTI), 1996. http://dx.doi.org/10.2172/656791.

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Lin, Yashen, Joseph Eto, Brian Johnson, et al. Research Roadmap on Grid-Forming Inverters. Office of Scientific and Technical Information (OSTI), 2020. http://dx.doi.org/10.2172/1721727.

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Cullinan, Timothy Edward. Crystallization dynamics in glass-forming systems. Office of Scientific and Technical Information (OSTI), 2016. http://dx.doi.org/10.2172/1342537.

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10

Nieh, T. G., and J. Wadsworth. Superplasticity and superplastic forming of ceramics. Office of Scientific and Technical Information (OSTI), 1994. http://dx.doi.org/10.2172/10172263.

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