@article {2695,
	title = {Modulating the Mechanical Stability of Extracellular Matrix Protein Tenascin-C in a Controlled and Reversible Fashion},
	journal = {Journal of Molecular Biology},
	volume = {390},
	number = {4},
	year = {2009},
	note = {ISI Document Delivery No.: 477KYTimes Cited: 2Cited Reference Count: 45Zhuang, Shulin Peng, Qing Cao, Yi Li, Hongbin},
	month = {Jul},
	pages = {820-829},
	type = {Article},
	abstract = {Stretching force can induce conformational changes of proteins and is believed to be an important biological signal in the mechanotransduction network. Tenascin-C is a large extracellular matrix protein and is subject to stretching force under its physiological condition. Regulating the mechanical properties of the fibronectin type III domains of tenascin-C will alter its response to mechanical stretching force and thus may provide the possibility of regulating the biological activities of tenascin-C in living cells. However, tuning the mechanical stability of proteins in a rational and systematic fashion remains challenging. Using the third fibronectin type III domain (TNfn3) of tenascin-C as a model system, here we report a successful engineering of a mechanically stronger extracellular matrix protein via engineered metal chelation. Combining steered molecular dynamics simulations, protein engineering and single-molecule atomic force microscopy, we have rationally engineered a bihistidine-based metal chelation site into TNfn3. We used its metal chelation capability to selectively increase the unfolding energy barrier for the rate-limiting step during the mechanical unfolding of TNfn3. The resultant TNfn3 mutant exhibits enhanced mechanical stability. Using a stronger metal chelator, one can convert TNfn3 back to a state of lower mechanical stability. This is the first step toward engineering extracellular matrix proteins with defined mechanical properties, which can be modulated reversibly by external stimuli, and will provide the possibility of using external stimuli to regulate the biological functions of extracellular matrix proteins. (C) 2009 Elsevier Ltd. All rights reserved.},
	keywords = {DYNAMICS, ELASTICITY, ENGINEERING PROTEINS, FNIII DOMAIN, FRAGMENTS, MECHANICAL STABILITY, mechanical unfolding, microscopy, MOLECULE FORCE SPECTROSCOPY, MUSCLE, rational design, recombination, SINGLE PROTEIN, single-molecule force spectroscopy, tenascin},
	isbn = {0022-2836},
	url = {<Go to ISI>://000268519200019},
	author = {Zhuang, S. L. and Peng, Q. and Cao, Y. and Li, H. B.}
}
@article {4706,
	title = {Vanadyl-biguanide complexes as potential synergistic insulin mimics},
	journal = {Journal of Inorganic Biochemistry},
	volume = {76},
	number = {3-4},
	year = {1999},
	note = {ISI Document Delivery No.: 262ZHTimes Cited: 65Cited Reference Count: 27},
	month = {Sep},
	pages = {251-257},
	type = {Article},
	abstract = {Vanadium has well-documented blood-glucose-lowering properties both in vitro and in vivo. The design of new oxovanadium(IV) coordination compounds, intended for use as insulin-enhancing agents in the treatment of diabetes mellitus, can potentially benefit from a synergistic approach, in which the whole complex has more than an additive effect from its component parts. Biguanides, most importantly metformin, are oral hypoglycemic agents used today to treat type 2 diabetes mellitus. In this study, biguanide, metformin, and phenformin, all biguanides, were coordinated to oxovanadium(IV) to form potential insulin-enhancing compounds. Highly colored, air-stable, bis(biguanidato)oxovanadium(IV), [VO(big)(2)], bis(N{\textquoteright},N{\textquoteright}-dimethylbiguanidato)oxovanadium(IV) [VO(metf)(2)], and bis(beta-phenethyl-biguanidato)oxovanadium(IV), [VO(phenf)(2)], were prepared. Solvation with dimethylsulfoxide occurred with VO(metf)(2) to form a six-coordinate complex. Precursor ligands and oxovanadium(IV) coordination complexes were characterized by infrared spectroscopy, mass spectrometry, elemental analyses, magnetic susceptibility, and, where appropriate, H-1 NMR spectroscopy. Biological testing with VO(metf)(2), a representative compound, for insulin-enhancing potential included acute (72 h) administration, both by intraperitoneal (i.p.) injection and by oral gavage (p.o,) in streptozotocin (STZ)-diabetic rats. VO(metf)(2) administration resulted in significant blood-glucose lowering at doses of 0.12 mmol kg(-1) i.p. and 0.60 mmol kg(-1) p.o. (previously established as ED50 doses for organically chelated oxovanadium(IV) complexes); however, no positive associative effects due to the presence of biguanide in the complex were apparent. (C) 1999 Elsevier Science Inc. All rights reserved.},
	keywords = {biguanide, BIS(MALTOLATO)OXOVANADIUM(IV), BMOV, coordination complex, GLUCOSE-LOWERING PROPERTIES, insulin mimic, MECHANISM, METFORMIN, MIMETIC AGENT, MUSCLE, RATS, VANADIUM},
	isbn = {0162-0134},
	url = {<Go to ISI>://000084097800010},
	author = {Woo, L. C. Y. and Yuen, V. G. and Thompson, K. H. and McNeill, J. H. and Orvig, Chris}
}
@article {4312,
	title = {Equus caballus gelsolin - cDNA sequence and protein structural implications},
	journal = {European Journal of Biochemistry},
	volume = {251},
	number = {3},
	year = {1998},
	note = {ISI Document Delivery No.: YV719Times Cited: 4Cited Reference Count: 48},
	month = {Feb},
	pages = {613-621},
	type = {Article},
	abstract = {We have generated and characterized the cDNA from equine smooth muscle that Encodes gelsolin, an actin-modulating protein. Overlapping cDNA clones synthesized by the reverse transcriptaseoplymerase chain reaction and clones isolated from a horse genomic library provided the complete primary structure for the intracellular isoform of gelsolin, while cDNA complemented with protein sequence data produced the full-length primary transcript of the gelsolin isoform found circulating in equine plasma. The deduced amino acid sequences of the intracellular and secreted versions of equine gelsolin infer polypeptides of 731 and 755 residues with apparent molecular masses of 80.7 kDa and 83.2 kDa, respectively. Multiple sequence alignment analysis of equine, human, porcine, and murine orthologs of gelsolin demonstrates prominent similarities among all of these proteins, with the horse and human molecules exhibiting the largest degree of likeness with respect to polypeptide length and overall sequence composition. Both horse and human plasma gelsolins are comprised of 755 amino acids with 94\% of the residues identical, while the degree of sequence identity in the shorter (731 residues) cytoplasmic gelsolins is 95 \%. Analysis of the sequences and structures of the six related domains that comprise gelsolin emphasizes the strong correlation that exists between primary structural conservation among mammalian gelsolins and maintenance of the three-dimensional domain fold characteristic of members of this protein family.},
	keywords = {actin-binding protein, ACTIN-SEVERING PROTEINS, amino acid sequence, AMPLIFICATION, BINDING DOMAIN, cDNA sequence, CLONING, CYTOPLASMIC FORMS, DNA, END, extraction, gelsolin, HORSE PLASMA GELSOLIN, MUSCLE, protein structure},
	isbn = {0014-2956},
	url = {<Go to ISI>://000071855900009},
	author = {Koepf, E. K. and Hewitt, J. and Vo, H. and MacGillivray, R. T. A. and Burtnick, L. D.}
}
@article {3092,
	title = {SPECIATION OF ARSENIC COMPOUNDS BY HPLC WITH HYDRIDE GENERATION ATOMIC-ABSORPTION SPECTROMETRY AND INDUCTIVELY-COUPLED PLASMA-MASS SPECTROMETRY DETECTION},
	journal = {Talanta},
	volume = {41},
	number = {4},
	year = {1994},
	note = {ISI Document Delivery No.: NJ813Times Cited: 94Cited Reference Count: 45},
	month = {Apr},
	pages = {495-502},
	type = {Article},
	abstract = {An arsenic specific detection system utilizing on-line microwave digestion and hydride generation atomic absorption spectrometry (MD/HGAAS) is described for arsenic speciation by using high performance liquid chromatography (HPLC). Both ion exchange chromatography and ion pair chromatography have been studied for the separation of arsenite, arsenate, monomethylarsonic acid (MMAA), dimethylarsinic acid (DMAA), and arsenobetaine (AB). When the commonly used mobile phases, phosphate and carbonate buffers at pH 7.5, are used on an anion exchange column, arsenite and AB co-elute. However, selective determination of these two arsenic compounds can be achieved by using the new detection system. Partial separation between arsenite and AB can be achieved by increasing the mobile phase pH to 10.3 and by using a polymer based anion exchange column. The detection limit obtained by using anion exchange chromatography with MD/HGAAS detection is approximately 10 ng/ml (or 200 pg for a 20-mul sample injection) for arsenite, DMAA and AB, 15 ng/ml (or 300 pg) for MMAA, and 20 ng/ml (or 400 pg) for arsenate. Complete separation of the five arsenic compounds is achieved on a reversed phase C18 column by using sodium heptanesulfonate as ion pair reagent. Comparable resolution between chromatographic peaks is obtained by using MD/HGAAS detection and inductively coupled plasma mass spectrometry (ICPMS) detection.},
	keywords = {ELEMENT-SPECIFIC DETECTOR, IDENTIFICATION, ION CHROMATOGRAPHY, MUSCLE, ORGANOARSENIC COMPOUNDS, PERFORMANCE LIQUID-CHROMATOGRAPHY, QUANTITATION, REFERENCE MATERIAL, SEPARATION, TRACE-ELEMENTS, WATER},
	isbn = {0039-9140},
	url = {<Go to ISI>://A1994NJ81300003},
	author = {Le, X. C. and Cullen, W. R. and Reimer, K. J.}
}
@article {7284,
	title = {INTERACTION OF PLASMA GELSOLIN WITH TROPOMYOSIN},
	journal = {Febs Letters},
	volume = {309},
	number = {1},
	year = {1992},
	note = {ISI Document Delivery No.: JL068Times Cited: 20Cited Reference Count: 17},
	month = {Aug},
	pages = {56-58},
	type = {Article},
	abstract = {Horse plasma gelsolin labelled with benzophenone-4-isothiocyanate can be photochemically cross-linked to rabbit cardiac tropomyosin. The cross-linking proceeds with greater efficiency in calcium-containing buffers. Further evidence for interaction between these proteins is provided by retention of fluorescently labelled gelsolin on tropomyosin-agarose affinity columns and by the ability of tropomyosin to cause an increase in the fluorescence intensity of gelsolin labelled with fluorescein-5-isothiocyanate. Both of these effects require the presence of calcium ions.},
	keywords = {actin, FILAMENTS, gelsolin, MUSCLE, PROTEIN, TROPOMYOSIN},
	isbn = {0014-5793},
	url = {<Go to ISI>://A1992JL06800013},
	author = {Koepf, E. K. and Burtnick, L. D.}
}
@article {6992,
	title = {HYBRIDIZATION OF RABBIT CARDIAC TROPOMYOSIN WITH NONPOLYMERIZABLE TROPOMYOSIN SPECIES},
	journal = {Biochemistry International},
	volume = {23},
	number = {4},
	year = {1991},
	note = {ISI Document Delivery No.: FR332Times Cited: 0Cited Reference Count: 19},
	month = {Mar},
	pages = {801-807},
	type = {Article},
	keywords = {ALPHA-TROPOMYOSIN, AMINO-ACID-SEQUENCE, BETA-TROPOMYOSIN, BINDING, EQUINE PLATELET TROPOMYOSIN, EXCIMER FLUORESCENCE, F-ACTIN, MUSCLE},
	isbn = {0158-5231},
	url = {<Go to ISI>://A1991FR33200022},
	author = {Clark, I. D. and Burtnick, L. D.}
}
