Relevant bibliographies by topics / Synergistic Scaffolding

Academic literature on the topic 'Synergistic Scaffolding'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Contents

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Synergistic Scaffolding.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Synergistic Scaffolding"

1

Dajkovic, Alex, Sebastien Pichoff, Joe Lutkenhaus, and Denis Wirtz. "ZAPA Controls the Scaffolding Function of FtsZ Through Three Synergistic Activities." Biophysical Journal 98, no. 3 (January 2010): 9a. http://dx.doi.org/10.1016/j.bpj.2009.12.054.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Matsuoka, Satoshi, Hideaki Yukawa, Masayuki Inui, and Roy H. Doi. "Synergistic Interaction of Clostridium cellulovorans Cellulosomal Cellulases and HbpA." Journal of Bacteriology 189, no. 20 (August 10, 2007): 7190–94. http://dx.doi.org/10.1128/jb.00842-07.

Full text
Abstract:
ABSTRACT Clostridium cellulovorans, an anaerobic bacterium, produces a small nonenzymatic protein called HbpA, which has a surface layer homology domain and a type I cohesin domain similar to those found in the cellulosomal scaffolding protein CbpA. In this study, we demonstrated that HbpA could bind to cell wall fragments from C. cellulovorans and insoluble polysaccharides and form a complex with cellulosomal cellulases endoglucanase B (EngB) and endoglucanase L (EngL). Synergistic degradative action of the cellulosomal cellulase and HbpA complexes was demonstrated on acid-swollen cellulose, Avicel, and corn fiber. We propose that HbpA functions to bind dockerin-containing cellulosomal enzymes to the cell surface and complements the activity of cellulosomes.
APA, Harvard, Vancouver, ISO, and other styles
3

Koukiekolo, Roger, Hee-Yeon Cho, Akihiko Kosugi, Masayuki Inui, Hideaki Yukawa, and Roy H. Doi. "Degradation of Corn Fiber by Clostridium cellulovorans Cellulases and Hemicellulases and Contribution of Scaffolding Protein CbpA." Applied and Environmental Microbiology 71, no. 7 (July 2005): 3504–11. http://dx.doi.org/10.1128/aem.71.7.3504-3511.2005.

Full text
Abstract:
ABSTRACT Clostridium cellulovorans, an anaerobic bacterium, degrades native substrates efficiently by producing an extracellular enzyme complex called the cellulosome. All cellulosomal enzyme subunits contain dockerin domains that can bind to hydrophobic domains termed cohesins which are repeated nine times in CbpA, the nonenzymatic scaffolding protein of C. cellulovorans cellulosomes. In this study, the synergistic interactions of cellulases (endoglucanase E, EngE; endoglucanase L, EngL) and hemicellulases (arabinofuranosidase A, ArfA; xylanase A, XynA) were determined on the degradation of corn fiber, a natural substrate containing mainly xylan, arabinan, and cellulose. The degradation by XynA and ArfA of cellulose/arabinoxylan was greater than that of corn fiber and resulted in 2.6-fold and 1.4-fold increases in synergy, respectively. Synergistic effects were observed in increments in both simultaneous and sequential reactions with ArfA and XynA. These synergistic enzymes appear to represent potential rate-limiting enzymes for efficient hemicellulose degradation. When mini-cellulosomes were constructed from the cellulosomal enzymes (XynA and EngL) and mini-CbpA with cohesins 1 and 2 (mini-CbpA1&2) and mini-CbpA with cohesins 5 and 6 (mini-CbpA5&6), higher activity was observed than that for the corresponding enzymes alone. Based on the degradation of different types of celluloses and hemicelluloses, the interaction between cellulosomal enzymes (XynA and EngL) and mini-CbpA displayed a diversity that suggests that dockerin-cohesin interaction from C. cellulovorans may be more selective than random.
APA, Harvard, Vancouver, ISO, and other styles
4

Jiao, Yan, Yao Zheng, Ping Chen, Mietek Jaroniec, and Shi-Zhang Qiao. "Molecular Scaffolding Strategy with Synergistic Active Centers To Facilitate Electrocatalytic CO2 Reduction to Hydrocarbon/Alcohol." Journal of the American Chemical Society 139, no. 49 (December 2017): 18093–100. http://dx.doi.org/10.1021/jacs.7b10817.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Murashima, Koichiro, Akihiko Kosugi, and Roy H. Doi. "Synergistic Effects on Crystalline Cellulose Degradation between Cellulosomal Cellulases from Clostridium cellulovorans." Journal of Bacteriology 184, no. 18 (September 15, 2002): 5088–95. http://dx.doi.org/10.1128/jb.184.18.5088-5095.2002.

Full text
Abstract:
ABSTRACT Clostridium cellulovorans produces a multienzyme cellulose-degrading complex called the cellulosome. In this study, we determined the synergistic effects on crystalline cellulose degradation by three different recombinant cellulosomes containing either endoglucanase EngE, endoglucanase EngH, or exoglucanase ExgS bound to mini-CbpA, a part of scaffolding protein CbpA. EngE, EngH, and ExgS are classified into the glycosyl hydrolase families 5, 9, and 48, respectively. The assembly of ExgS and EngH with mini-CbpA increased the activity against insoluble cellulose 1.5- to 3-fold, although no effects on activity against soluble cellulose were observed. These results indicated that mini-CbpA could help cellulase components degrade insoluble cellulose but not soluble cellulose. The mixture of the cellulosomes containing ExgS and EngH showed higher activity and synergy degrees than the other cellulosome mixtures, indicating the synergistic effect between EngH and ExgS was the most dominant effect among the three mixtures for crystalline cellulose degradation. Reactions were also performed by adding different cellulosomes in a sequential manner. When ExgS was used for the initial reaction followed by EngE and EngH, almost no synergistic effect was observed. On the other hand, when EngE or EngH was used for the first reaction followed by ExgS, synergistic effects were observed. These results indicated that the initial reactions by EngH and/or EngE promoted cellulose degradation by ExgS.
APA, Harvard, Vancouver, ISO, and other styles
6

Jeon, Sang Duck, Ji Eun Lee, Su Jung Kim, Sung Hyun Park, Gi-Wook Choi, and Sung Ok Han. "Unique Contribution of the Cell Wall-Binding Endoglucanase G to the Cellulolytic Complex in Clostridium cellulovorans." Applied and Environmental Microbiology 79, no. 19 (July 19, 2013): 5942–48. http://dx.doi.org/10.1128/aem.01400-13.

Full text
Abstract:
ABSTRACTThe cellulosomes produced byClostridium cellulovoransare organized by the specific interactions between the cohesins in the scaffolding proteins and the dockerins of the catalytic components. Using a cohesin biomarker, we identified a cellulosomal enzyme which belongs to the glycosyl hydrolase family 5 and has a domain of unknown function 291 (DUF291) with functions similar to those of the surface layer homology domain inC. cellulovorans. The purified endoglucanase G (EngG) had the highest synergistic degree with exoglucanase (ExgS) in the hydrolysis of crystalline cellulose (EngG/ExgS ratio = 3:1; 1.71-fold). To measure the binding affinity of the dockerins in EngG for the cohesins of the main scaffolding protein, a competitive enzyme-linked interaction assay was performed. Competitors, such as ExgS, reduced the percentage of EngG that were bound to the cohesins to less than 20%; the results demonstrated that the cohesins prefer to bind to the common cellulosomal enzymes rather than to EngG. Additionally, in surface plasmon resonance analysis, the dockerin in EngG had a relatively weak affinity (30- to 123-fold) for cohesins compared with the other cellulosomal enzymes. In the cell wall affinity assay, EngG anchored to the cell surfaces ofC. cellulovoransusing its DUF291 domain. Immunofluorescence microscopy confirmed the cell surface display of the EngG complex. These results indicated that inC. cellulovorans, EngG assemble into both the cellulolytic complex and the cell wall complex to aid in the hydrolysis of cellulose substrates.
APA, Harvard, Vancouver, ISO, and other styles
7

Kurenova, Elena V., Sartaj Singh Sanghera, Jianqun Liao, Michael Yemma, and William G. Cance. "Demonstration of the efficacy of compound CFAK-C4 targeting FAK-VEGFR3 protein-protein interaction in gastric cancer." Journal of Clinical Oncology 31, no. 15_suppl (May 20, 2013): e22143-e22143. http://dx.doi.org/10.1200/jco.2013.31.15_suppl.e22143.

Full text
Abstract:
e22143 Background: While the emerging data strongly suggest that FAK is an excellent target for developmental therapeutics of cancer, kinase inhibitors of FAK have shown crossreactivity with other protein kinases and toxicity in preclinical and clinical studies. It is known that FAK acts pleiotropically, as a kinase and as a scaffolding protein, and our goal is to explore targeting the scaffolding function of FAK to inhibit protein-protein interactions important for tumor progression. Previously, we have shown that FAK physically interacts with VEGFR3 and we identified small molecule inhibitor CFAK-C4 that targets this site of interaction. Both of these kinases are overexpressed in gastric cancers and were found to be independent poor prognostic factors. The prognosis of patients with gastric cancer remains unfavorable and molecular based treatments are necessary for a potential breakthrough in the therapy of this disease. We hypothesize that FAK-VEGFR3 interaction provides essential survival signals for gastric tumor growth and that simultaneous inhibition of these signals will inhibit tumor progression. Methods: Effects of CFAK-C4 on gastric cancer cell lines AGS and NCI-N87 were examined by MTT assay (viability), colony formation assay and Western blotting (phosphorylation, apoptosis). Subcutaneous mouse model was used to demonstrate effect of CFAK-C4 in vivo. Results: CFAK-C4 specifically blocked phosphorylation of VEGFR3 and FAK, directly inhibited cell viability (p<0.05), increased cell detachment and inhibited colony formation in a dose-dependent manner (range 1-100µM). CFAK-C4 (50mg/kg, IP) effectively caused tumor regression in vivo, when administered alone and its effects were synergistic (p<0.05) with chemotherapy. In vivo effects of C4 were confirmed by a decrease in tumor FAK and VEGFR3 phosphorylation, and disruption of their complexes. Conclusions: In this study we have shown that CFAK-C4 inhibits FAK-VEGFR3 signaling in gastric cancer cells and affects tumor growth. This result demonstrates that targeting the scaffolding function of FAK is a unique approach of highly-specific molecular-targeted therapy and can be used to develop oral-based cancer therapeutics.
APA, Harvard, Vancouver, ISO, and other styles
8

Mohan, Maradumane L., Arunachal Chatterjee, Swetha Ganapathy, Sromona Mukherjee, Sowmya Srikanthan, George P. Jolly, Rohit S. Anand, and Sathyamangla V. Naga Prasad. "Noncanonical regulation of insulin-mediated ERK activation by phosphoinositide 3-kinase γ." Molecular Biology of the Cell 28, no. 22 (November 2017): 3112–22. http://dx.doi.org/10.1091/mbc.e16-12-0864.

Full text
Abstract:
Classically Class IB phosphoinositide 3-kinase (PI3Kγ) plays a role in extracellular signal–regulated kinase (ERK) activation following G-protein coupled receptor (GPCR) activation. Knock-down of PI3Kγ unexpectedly resulted in loss of ERK activation to receptor tyrosine kinase agonists such as epidermal growth factor or insulin. Mouse embryonic fibroblasts (MEFs) or primary adult cardiac fibroblasts isolated from PI3Kγ knock-out mice (PI3KγKO) showed decreased insulin-stimulated ERK activation. However, expression of kinase-dead PI3Kγ resulted in rescue of insulin-stimulated ERK activation. Mechanistically, PI3Kγ sequesters protein phosphatase 2A (PP2A), disrupting ERK–PP2A interaction, as evidenced by increased ERK–PP2A interaction and associated PP2A activity in PI3KγKO MEFs, resulting in decreased ERK activation. Furthermore, β-blocker carvedilol-mediated β-arrestin-dependent ERK activation is significantly reduced in PI3KγKO MEF, suggesting accelerated dephosphorylation. Thus, instead of classically mediating the kinase arm, PI3Kγ inhibits PP2A by scaffolding and sequestering, playing a key parallel synergistic step in sustaining the function of ERK, a nodal enzyme in multiple cellular processes.
APA, Harvard, Vancouver, ISO, and other styles
9

Moses, Joseph Christakiran, Mainak Dey, K. Bavya Devi, Mangal Roy, Samit Kumar Nandi, and Biman B. Mandal. "Synergistic Effects of Silicon/Zinc Doped Brushite and Silk Scaffolding in Augmenting the Osteogenic and Angiogenic Potential of Composite Biomimetic Bone Grafts." ACS Biomaterials Science & Engineering 5, no. 3 (February 15, 2019): 1462–75. http://dx.doi.org/10.1021/acsbiomaterials.8b01350.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Walthers, Christopher M., and Stephanie K. Seidlits. "Gene Delivery Strategies to Promote Spinal Cord Repair." Biomarker Insights 10s1 (January 2015): BMI.S20063. http://dx.doi.org/10.4137/bmi.s20063.

Full text
Abstract:
Gene therapies hold great promise for the treatment of many neurodegenerative disorders and traumatic injuries in the central nervous system. However, development of effective methods to deliver such therapies in a controlled manner to the spinal cord is a necessity for their translation to the clinic. Although essential progress has been made to improve efficiency of transgene delivery and reduce the immunogenicity of genetic vectors, there is still much work to be done to achieve clinical strategies capable of reversing neurodegeneration and mediating tissue regeneration. In particular, strategies to achieve localized, robust expression of therapeutic transgenes by target cell types, at controlled levels over defined time periods, will be necessary to fully regenerate functional spinal cord tissues. This review summarizes the progress over the last decade toward the development of effective gene therapies in the spinal cord, including identification of appropriate target genes, improvements to design of genetic vectors, advances in delivery methods, and strategies for delivery of multiple transgenes with synergistic actions. The potential of biomaterials to mediate gene delivery while simultaneously providing inductive scaffolding to facilitate tissue regeneration is also discussed.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Book chapters on the topic "Synergistic Scaffolding"

1

Kitagawa, Midori, Paul Fishwick, Mary Urquhart, Michael Kesden, Rosanna Guadagno, Kieth Gryder, Ngoc Tran, Alex Najera, and Diego Ochoa. "Scaffolding, State-Based Modeling, and Multiple Representation: User Interface Concepts Implemented in an Interactive Online Learning Environment for Synergistic Learning of Physics and Computational Thinking." In Communications in Computer and Information Science, 57–64. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-031-06391-6_8.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Synergistic Scaffolding' for particular source types:
Journal articles
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography