Closure to “Structural Damage Detection from Modal Strain Energy Change” by Z. Y. Shi, S. S. Law, and L. M. Zhang

Shi, Zhiyu; Law, S.S.; Zhang, L. M.

doi:10.1061/(asce)0733-9399(2002)128:3(377)

Cited by 108 publications

(187 citation statements)

References 3 publications

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“…ISO brightness of pulp samples36 was measured using a brightness color tester (YQ-Z-48A, Hangzhou Light Instrument Development Co., Ltd.). All reported brightness values represent an average of three separate measurements.…”

Section: Methodsmentioning

confidence: 99%

Xylanase Treatment Suppresses Light- and Heat-Induced Yellowing of Pulp

Zhang

Wang

et al. 2016

Sci Rep

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Xylanase is commonly applied in pulp and paper industries to ease cost-related and environmental pressures. The effect of xylanase treatment on pulp bleaching is well-established, however, few studies were conducted on the effects of xylanase treatment in pulp yellowing, especially the mechanism of pulp yellowing inhibition by xylanase treatment. In this study, pure xylanase (EC 3.2.1.8) was applied to treat wheat straw chemical pulp (CP) and poplar chemi-thermo-mechanical pulp (CTMP) to determine their effects on pulp brightness and on light- and heat-induced yellowing. The xylanase treatment decreased the post-color number of the pulps during light- and heat-induced yellowing. However, differences were observed in the yellowing inhibition between the wheat straw CP and poplar CTMP. The changes in chemical components of pulps after the xylanase treatment, for example, lignin, hemicellulose, and HexA contents, and analysis of UV–vis absorption spectra and Fourier transform infrared-attenuated total reflectance spectrum were used to explore the pulp yellowing inhibition causes by the xylanase treatment.

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Section: Methodsmentioning

confidence: 99%

Xylanase Treatment Suppresses Light- and Heat-Induced Yellowing of Pulp

Zhang

Wang

et al. 2016

Sci Rep

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“…We [32,35] and others [33,40] have reported that cTnI in the circulation is predominantly fragmented and that very little intact TnI is present. The cTnI fragments are complexed with TnC, which are believed to be the predominant TnI forms [42], and also with both TnC and TnT [36,44].…”

Section: Resultsmentioning

confidence: 98%

“…The immunological activity of TnI 88 , is 2.5-and 7-fold higher than that of TnI 153 and rTnI, respectively, suggesting that the TnI fragments are more readily recognized by TnI antibodies than the full length TnI. It is possible that removal of the C-terminal portion of cTnI facilitates the binding of Stratus2 II TnI antibodies to TnI fragments and leads to an increase in the observed immunological activity [40]. The higher immunological activity of the TnI fragments over the intact rTnI is not related to the 1 and 2) and TnI 153 -TnC-TnT (lanes 3 and 4).…”

Section: Resultsmentioning

confidence: 99%

“…We [32] and others [33,36] have shown that patient serum cTnI is predominantly a C-terminal truncated molecule and exists as a complex with TnC and TnT. Various groups [33,35,40] have reported partial degradation from the N-terminal of TnI. In order to understand patient serum TnI, we have generated C-terminal truncated human cTnI fragments from human rTnI and studied their properties.…”

Section: Resultsmentioning

confidence: 99%

“…It is not known which form(s) of the TnI complex mainly contribute to TnI immunoreactivity in each assay. It has been reported [33,35,40] that patient serum TnI undergoes rapid proteolytic cleavage from both the N-terminus and the Cterminus. Seven main TnI fragments were detected with molecular masses from 14 000-28 000 Da, which are likely to form complexes with TnC [33].…”

Section: Resultsmentioning

confidence: 99%

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Biochemical and immunological properties of human cardiac troponin I fragments

Morjana

Clark

Tal

2001

Biotech and App Biochem

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Cardiac troponin I (cTnI) is the inhibitory subunit of the troponin complex and is a biochemical marker for myocardial infarction (MI). It is found in human serum within 4-6 h following MI. One of us has shown [Morjana (1998) Biotechnol. Appl. Biochem. 28, 105-111] that MI patient serum TnI is cleaved at the N- and C-terminals and that the TnI fragments exist as a complex with tropinin C (TnC) and troponin T (TnT). In the present study, we have generated C-terminal truncated TnI fragments and studied their immunological and biochemical properties. Human recombinant TnI (rTnI) expressed in Escherichia coli is cleaved into a major fragment with a molecular mass of 17500 Da using CNBr. The major CNBr fragment contains the first 153 amino acids of human cTnI (TnI153). Cleavage of the rTnI with the endoproteinase Asp-N generates a smaller TnI fragment (TnI88, residues 6-96). TnI153 has higher immunological activity than that of rTnI and lower activity than that of TnI88, as judged by the Stratus II TnI Immunoassay. TnI153 exhibits biochemical and immunological properties similar to those of intact TnI. It binds TnC at a molar ratio of 1:1 and forms a ternary complex with TnC and TnT. TnC enhances the immunological activity of TnI153, but has little effect on the activity of TnI88. The TnI153-TnC complex exhibits higher immunological activity than rTnI-TnC and TnI88-TnC, and much higher activity than free rTnI, TnI153 and TnI88. The presence of TnT has no effect on the immunological activity of the TnI153-TnC complex, suggesting that the addition of TnT does not interfere with TnI153 recognition by TnI monoclonal antibodies. Free TnI153 and TnI88 degrade rapidly in human serum. TnC protects TnI153 from proteolytic degradation, but offers less protection for TnI88. The TnI88-TnC complex lost 80% of its immunological activity after incubation for 2 days in human serum at 37 degrees C. However, there was no loss in the immunological activity of the TnI153-TnC complex under the same conditions. A cTnI fragment (TnI80, residues 1-80), expressed in E. coli as a fusion protein, exhibits immunological activity and stability similar to that of TnI88.

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A Review of 3D Printing Technologies for Soft Polymer Materials

Zhou

2020

Adv Funct Materials

503

311

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Soft polymer materials, which are similar to human tissues, have played critical roles in modern interdisciplinary research. Compared with conventional methods, 3D printing allows rapid prototyping and mass customization and is ideal for processing soft polymer materials. However, 3D printing of soft polymer materials is still in the early stages of development and is facing many challenges including limited printable materials, low printing resolution and speed, and poor functionalities. The present review aims to summarize the ideas to address these challenges. It focuses on three points: 1) how to develop printable materials and make unprintable materials printable, 2) how to choose suitable methods and improve printing resolution, and 3) how to directly construct functional structures/systems with 3D printing. After a brief introduction on this topic, the mainstream 3D printing technologies for printing soft polymer materials are reviewed, with an emphasis on improving printing resolution and speed, choosing suitable printing techniques, developing printable materials, and printing multiple materials. Moreover, the state-of-the-art advancements in multimaterial 3D printing of soft polymer materials are summarized. Furthermore, the revolutions brought about by 3D printing of soft polymer materials for applications similar to biology are highlighted. Finally, viewpoints and future perspectives for this emerging field are discussed.

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Closure to “Structural Damage Detection from Modal Strain Energy Change” by Z. Y. Shi, S. S. Law, and L. M. Zhang

Cited by 108 publications

References 3 publications

Xylanase Treatment Suppresses Light- and Heat-Induced Yellowing of Pulp

Xylanase Treatment Suppresses Light- and Heat-Induced Yellowing of Pulp

Biochemical and immunological properties of human cardiac troponin I fragments

A Review of 3D Printing Technologies for Soft Polymer Materials

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