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Structural Characterization of Lens Crystallins and the Perspectives on the Evolution and Biosynthetic Applications of Enzymatic Crystallins (2013)

Chiou, Shyh‐Horng [Verfasser]

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UID:

(DE-101)1317408470

Format: Online-Ressource

ISSN: 2192-6549

Content: Abstract: This account describes work in our laboratory on lens crystallins during the past decade. The major classes of crystallins are reviewed. A systematic and detailed analysis of the kinetic properties of two presumably structural proteins with stable enzymatic activities revealed subtle differences in kinetic mechanisms of these enzyme crystallins and their corresponding cellular enzymes. Bioorganic synthesis based on ϵ‐ and δ‐crystallins isolated from avian and reptilian lenses, two crystallins possessing lactate dehydrogenase and argininosuccinate lyase respectively, provides an efficient and practical tool for enantioselective synthesis of valuable organic intermediates. Understanding the crystallin diversity at the molecular and cellular levels constitutes a major goal of crystallin research, as it provides the framework to unravel the complex process underlying the evolution of lens crystallins in general and may provide insight into their biological significance.

In: volume:39

In: number:6

In: year:2013

In: pages:721-730

In: extent:10

In: Zhongguo-Huaxuehui 〈Taiwan〉, Journal of the Chinese Chemical Society, Malden, Mass. : Wiley-Blackwell, 1954-, 39, Heft 6 (2013), 721-730 (gesamt 10), 2192-6549

Language: English

DOI: 10.1002/jccs.199200108

URN: urn:nbn:de:101:1-2024012705012705538800

URL: https://doi.org/10.1002/jccs.199200108

URL: https://nbn-resolving.org/urn:nbn:de:101:1-2024012705012705538800

URL: https://d-nb.info/1317408470/34

URL: https://doi.org/10.1002/jccs.199200108

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Rapid Protein Hydrolysis by Microwave Irradiation Using Heat‐Resistant Teflon‐Pyrex Tubes (2013)

Chiou, Shyh‐Horng [Verfasser]

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UID:

(DE-101)1322023085

Format: Online-Ressource

ISSN: 2192-6549

Content: Abstract: A rapid peptide‐bond hydrolysis by means of microwave irradiation is introduced for the facile preparation of protein hydrolysates used for amino acid analysis. The optimal hydrolysis condition has been determined using several enzymes with known amino acid compositions. The effects of hydrolysis time on the recovery of various labile and hydrophobic amino acids are also exemplified in the microwave heating of standard amino acids. The method has been applied to the complete amino acid analysis with a single nonvolatile solvent of methanesulfonic acid with good recovery of tryptophan and half‐cystine. It provides a radical expedition of protein and peptide hydrolysis via commercial microwave ovens and specially‐designed Teflon‐Pyrex tubes, circumventing the tedious procedures using vacuum‐sealed pyrex lubes heating at 110°C for more than 24 h. This novel type of microwave chemistry associated with rapid peptide‐bond cleavage is of great potential in the automation of the complete process of amino acid analysis starting from the preparation of protein hydrolysates.

In: volume:36

In: number:5

In: year:2013

In: pages:435-442

In: extent:8

In: Zhongguo-Huaxuehui 〈Taiwan〉, Journal of the Chinese Chemical Society, Malden, Mass. : Wiley-Blackwell, 1954-, 36, Heft 5 (2013), 435-442 (gesamt 8), 2192-6549

Language: English

DOI: 10.1002/jccs.198900060

URN: urn:nbn:de:101:1-2024022905292989849209

URL: https://doi.org/10.1002/jccs.198900060

URL: https://nbn-resolving.org/urn:nbn:de:101:1-2024022905292989849209

URL: https://d-nb.info/1322023085/34

URL: https://doi.org/10.1002/jccs.198900060

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The protein sequence homology of γ-crystallins among major vertebrate classes and their DNA sequence homology to heat-shock protein genes (1988)

Chiou, Shyh-Horng [Verfasser] ; SpringerLink (Online service)

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UID:

(DE-101)1308589905

Format: Online-Ressource, 1 online resource.

ISSN: 1875-8355

In: volume:7

In: number:4

In: day:1

In: month:8

In: year:1988

In: pages:527-534

In: date:8.1988

In: The protein journal, Dordrecht : Springer Science + Business Media B.V., 2004-, 7, Heft 4 (1.8.1988), 527-534, 8.1988, 1875-8355

Language: English

DOI: 10.1007/BF01024894

URN: urn:nbn:de:101:1-2023110413121085805328

URL: https://doi.org/10.1007/BF01024894

URL: https://nbn-resolving.org/urn:nbn:de:101:1-2023110413121085805328

URL: https://d-nb.info/1308589905/34

URL: https://doi.org/10.1007/BF01024894

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Structural Characterization of Venom Toxins by Physical Methods and the Perspectives on Structure‐Function Correlation of Proteins (2013)

Chiou, Shyh‐Horng [Verfasser] ; Wu, Shih‐Hsiung [Verfasser]

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UID:

(DE-101)1311684816

Format: Online-Ressource

ISSN: 2192-6549

Content: Abstract: This account describes work in our laboratories on the application of physical methods to the structural studies of various toxins during the past few years. A general review of background and the meaningful results obtained from these approaches are described. The results are compared with updated information on related subjects carried out at other laboratories. Examples of structural studies on some small toxins present abundantly in Formosan cobra (Naja naja atra), one of the indigenous toxic snakes in Taiwan, are given with the emphasis on the identification and characterization of complex toxic protein components based on near‐infrared Fourier transform Raman Spectroscopy. We will also describe our initial efforts in solving the solution structures of several small proteins and peptides by means of two‐dimensional nuclear magnetic resonance (2D‐NMR) and computer‐simulated modeling. The structural information obtained by these modem physical techniques provides the framework for unraveling the complex structure‐activity relationships engendered by these biomolecules.

In: volume:44

In: number:3

In: year:2013

In: pages:337-348

In: extent:12

In: Zhongguo-Huaxuehui 〈Taiwan〉, Journal of the Chinese Chemical Society, Malden, Mass. : Wiley-Blackwell, 1954-, 44, Heft 3 (2013), 337-348 (gesamt 12), 2192-6549

Language: English

DOI: 10.1002/jccs.199700051

URN: urn:nbn:de:101:1-2023113004365298268610

URL: https://doi.org/10.1002/jccs.199700051

URL: https://nbn-resolving.org/urn:nbn:de:101:1-2023113004365298268610

URL: https://d-nb.info/1311684816/34

URL: https://doi.org/10.1002/jccs.199700051

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Enhancement of Chemical Reactions by Microwave Irradiation (2013)

Chen, Shui‐Tein [Verfasser] ; Chiou, Shyh‐Horng [Verfasser] ; Wang, Kung‐Tsung [Verfasser]

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UID:

(DE-101)1317421108

Format: Online-Ressource

ISSN: 2192-6549

Content: Abstract: Microwaves are low electromagnetic energy which induce molecular perturbation by stimulation of ionic diffusion and by enhancement of dipole rotation without causing rearrangement of molecular structures. Microwave energy irradiated on the samples in various liquid media is lost or absorbed to the samples by the following two mechanisms: ionic conduction and dipole rotation. These two effects take place simultaneously to account for the phenomenon of rapid heating associated with many practical applications of microwave irradiation. In contrast to conventional heating, the salient feat ure of “dipole rotation” constitutes one efficient form of “molecular agitation” or “molecular stirring” which can be explored for many aspects in chemical reactions. We will discuss some of the useful application of “molecular agitation” by means of microwave irradiation such as: 1. rapid hydrolysis of proteins and peptides, 2. selective hydrolysis of aspartyl peptide bond, 3. the racemization of amino acids, 4. rapid hydrolysis of sugars, 5. continuous‐flow process of microwave reactions, and 6. the enhancement of coupling reactions in peptide synthesis.

In: volume:38

In: number:1

In: year:2013

In: pages:85-91

In: extent:7

In: Zhongguo-Huaxuehui 〈Taiwan〉, Journal of the Chinese Chemical Society, Malden, Mass. : Wiley-Blackwell, 1954-, 38, Heft 1 (2013), 85-91 (gesamt 7), 2192-6549

Language: English

DOI: 10.1002/jccs.199100015

URN: urn:nbn:de:101:1-2024012708200235981930

URL: https://doi.org/10.1002/jccs.199100015

URL: https://nbn-resolving.org/urn:nbn:de:101:1-2024012708200235981930

URL: https://d-nb.info/1317421108/34

URL: https://doi.org/10.1002/jccs.199100015

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From Chemistry to Translational Medicine: The Application of Proteomics to Cancer Biomarker Discovery and Diagnosis (2015)

Chiou, Shyh‐Horng [Verfasser] ; Huang, Chun‐Hao [Verfasser] ; Liang, Shih‐Shin [Verfasser]

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UID:

(DE-101)1276343876

Format: Online-Ressource

ISSN: 2192-6549

Content: Abstract: The study of complex protein mixtures and their interactions in cells and tissues has been difficult due to the tedious process involved in their characterization and analysis. The recent emergence of fast‐evolving and state‐of‐the‐art proteomics methodologies has provided a rapid and scalable platform for understanding the comprehensive proteome profiles from complex whole tissues or cells of various biological sources. Therefore, proteomics has been increasingly valuable to examine real‐time changes in protein expression of various tissues or body fluids from patients with various diseases, especially cancer, resulting in the identification of clinically useful biomarkers for diagnosis, prognosis and disease staging. In this review, we focus on potential biomarkers for (1) Helicobacter pylori‐associated gastric cancer, (2) hepatocellular carcinoma (HCC), and (3) renal cell carcinoma (RCC). In addition to the conventional gel‐based proteomics (1‐D or 2‐D gels), we have utilized a more advanced proteomic approach by incorporating stable isotope dimethyl labelling and shotgun proteomics strategy in combination with nanoliquid chromatography and tandem mass spectrometry (nanoLC‐MS/MS) to better characterize the biomarkers in several cancer tissues. By establishing a high‐throughput proteomics platform based on multiple reaction monitoring (MRM), we have successfully detected and analyzed potential protein markers at low concentrations in various normal and tumor tissues. This platform not only highlights the utility of proteomics for biomarker discovery but also can be uniquely applied to disease‐oriented translational medicine for diagnosis of diverse types of cancers and other diseases.

In: volume:62

In: number:3

In: year:2015

In: pages:217-226

In: extent:10

In: Zhongguo-Huaxuehui 〈Taiwan〉, Journal of the Chinese Chemical Society, Malden, Mass. : Wiley-Blackwell, 1954-, 62, Heft 3 (2015), 217-226 (gesamt 10), 2192-6549

Language: English

DOI: 10.1002/jccs.201400350

URN: urn:nbn:de:101:1-2022122206040662452434

URL: https://doi.org/10.1002/jccs.201400350

URL: https://nbn-resolving.org/urn:nbn:de:101:1-2022122206040662452434

URL: https://d-nb.info/1276343876/34

URL: https://doi.org/10.1002/jccs.201400350

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Physicochemical characterization of γ-crystallins from bovine lens—Hydrodynamic and biochemical properties (1988)

Chiou, Shyh-Horng [Verfasser] ; Azari, Parviz [Verfasser] ; Himmel, Michael E. [Verfasser] ; [et al.]

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UID:

(DE-101)1308591217

Format: Online-Ressource, 1 online resource.

ISSN: 1875-8355

In: volume:7

In: number:1

In: day:1

In: month:2

In: year:1988

In: pages:67-80

In: date:2.1988

In: The protein journal, Dordrecht : Springer Science + Business Media B.V., 2004-, 7, Heft 1 (1.2.1988), 67-80, 2.1988, 1875-8355

Language: English

DOI: 10.1007/BF01025415

URN: urn:nbn:de:101:1-2023110413141523088361

URL: https://doi.org/10.1007/BF01025415

URL: https://nbn-resolving.org/urn:nbn:de:101:1-2023110413141523088361

URL: https://d-nb.info/1308591217/34

URL: https://doi.org/10.1007/BF01025415

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Sequence Characterization of γ-Crystallins from Lip Shark (Chiloscyllium colax): Existence of Two cDNAs Encoding γ-Crystallins of Mammalian and Teleostean Classes (1997)

Chuang, Ming-Hong [Verfasser] ; Pan, Fu-Ming [Verfasser] ; Chiou, Shyh-Horng [Verfasser] ; [et al.]

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UID:

(DE-101)1196087784

Format: Online-Ressource , online resource.

ISSN: 1573-4943 , 1875-8355

In: volume:16

In: number:4

In: pages:299-307

In: date:5.1997

In: The protein journal, Dordrecht : Springer Science + Business Media B.V., 2004-, 16, Heft 4, 299-307, 5.1997, 1875-8355

Language: English

DOI: 10.1023/A:1026309126725

URN: urn:nbn:de:101:1-2019100102132519351562

URL: https://doi.org/10.1023/A:1026309126725

URL: https://nbn-resolving.org/urn:nbn:de:101:1-2019100102132519351562

URL: https://d-nb.info/1196087784/34

URL: https://doi.org/10.1023/A:1026309126725

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Proteomic analysis of proteins expressed by Helicobacter pylori under oxidative stress (2005)

Chuang, Ming‐Hong [Verfasser] ; Wu, Ming‐Shiang [Verfasser] ; Lin, Jou‐Town [Verfasser] ; [et al.]

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UID:

(DE-101)1299823378

Format: Online-Ressource

ISSN: 1615-9861

In: volume:5

In: number:15

In: year:2005

In: pages:3895-3901

In: extent:7

In: Proteomics, Weinheim : Wiley VCH, [2001]-, 5, Heft 15 (2005), 3895-3901 (gesamt 7), 1615-9861

Language: English

DOI: 10.1002/pmic.200401232

URN: urn:nbn:de:101:1-2023082205532790962441

URL: https://doi.org/10.1002/pmic.200401232

URL: https://nbn-resolving.org/urn:nbn:de:101:1-2023082205532790962441

URL: https://d-nb.info/1299823378/34

URL: https://doi.org/10.1002/pmic.200401232

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Characterization of γ-crystallin from the eye lens of bullfrog: Complexity of γ-crystallin multigene family as revealed by sequence comparison among different amphibian species (1996)

Lu, Shao-Fan [Verfasser] ; Pan, Fu-Ming [Verfasser] ; Chiou, Shyh-Horng [Verfasser] ; [et al.]

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UID:

(DE-101)1308447310

Format: Online-Ressource, 1 online resource.

ISSN: 1875-8355

In: volume:15

In: number:1

In: day:1

In: month:1

In: year:1996

In: pages:103-113

In: date:1.1996

In: The protein journal, Dordrecht : Springer Science + Business Media B.V., 2004-, 15, Heft 1 (1.1.1996), 103-113, 1.1996, 1875-8355

Language: English

DOI: 10.1007/BF01886816

URN: urn:nbn:de:101:1-2023110308570945484683

URL: https://doi.org/10.1007/BF01886816

URL: https://nbn-resolving.org/urn:nbn:de:101:1-2023110308570945484683

URL: https://d-nb.info/1308447310/34

URL: https://doi.org/10.1007/BF01886816

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