Search Results - "Smith, Jean B"

Mass spectrometric quantification of acetylation at specific lysines within the amino-terminal tail of histone H4 by Smith, Christine M, Gafken, Philip R, Zhang, Zhongli, Gottschling, Daniel E, Smith, Jean B, Smith, David L

“…Electrospray ionization mass spectrometry, a leading method for the quantification of biomolecules, is useful for the analysis of posttranslational…”
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The Major in vivo Modifications of the Human Water-insoluble Lens Crystallins are Disulfide Bonds, Deamidation, Methionine Oxidation and Backbone Cleavage by Hanson, Stacy R.A, Hasan, Azeem, Smith, David L, Smith, Jean B

“…This investigation of the water-insoluble crystallins from human lenses has used multiple chromatographic separations to obtain proteins of sufficient purity…”
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Human β-crystallins modified by backbone cleavage, deamidation and oxidation are prone to associate by Zhang, Zhongli, Smith, David L., Smith, Jean B.

“…Information about β-crystallins and their post-translational modifications has been scarce because of difficulties in isolating the individual β-crystallins…”
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Enhanced C-terminal truncation of αA- and αB-crystallins in diabetic lenses by THAMPI, Prajitha, HASSAN, Azeem, SMITH, Jean B, ABRAHAM, Edathara C

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Unexpected products from the reaction of the synthetic cross-linker 3,3′-dithiobis(sulfosuccinimidyl propionate), DTSSP with peptides by Swaim, Catherine L, Smith, Jean B, Smith, David L

“…Synthetic cross-linking reagents, such as 3,3′-dithiobis(sulfosuccinimidyl propionate), DTSSP, can react with sidechains of amino acids that are within close…”
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Deamidation in Human γS-Crystallin from Cataractous Lenses Is Influenced by Surface Exposure by Lapko, Veniamin N, Purkiss, Andrew G, Smith, David L, Smith, Jean B

“…A major component of human nuclear cataracts is water-insoluble, high molecular weight protein. A significant component of this protein is disulfide bonded…”
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Methylation and carbamylation of human γ‐crystallins by Lapko, Veniamin N., Smith, David L., Smith, Jean B.

“…Accessible sulfhydryls of cysteine residues are likely sites of reaction in long‐lived proteins such as human lens crystallins. Disulfide bonding between…”
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S-Methylated Cysteines in Human Lens γS-Crystallins by Lapko, Veniamin N, Smith, David L, Smith, Jean B

“…The proteins of the eye lens, which do not turn over throughout life, undergo many modifications, some of which lead to senile cataract. We describe a…”
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Solution Structure and Dynamics of a Heat Shock Protein Assembly Probed by Hydrogen Exchange and Mass Spectrometry by Wintrode, Patrick L, Friedrich, Kenneth L, Vierling, Elizabeth, Smith, Jean B, Smith, David L

“…The solution conformation and dynamics of the 16.9 kDa small heat shock protein from wheat have been studied using a combination of hydrogen/deuterium…”
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Thermal stability of human α‐crystallins sensed by amide hydrogen exchange by Hasan, Azeem, Yu, Jiong, Smith, David L., Smith, Jean B.

“…The α‐crystallins, αA and αB, are major lens structural proteins with chaperone‐like activity and sequence homology to small heat‐shock proteins. As yet, their…”
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α-Crystallin Regions Affected by Adenosine 5‘-Triphosphate Identified by Hydrogen−Deuterium Exchange by Hasan, Azeem, Smith, David L, Smith, Jean B

“…ATP interaction with lens α-crystallins leading to enhanced chaperone activity is not yet well understood. One model for chaperone activity of small heat shock…”
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Resistance of Human βB2-crystallin to in vivo Modification by Zhang, Zhongli, David, Larry L, Smith, David L, Smith, Jean B

“…Post-translational modifications and/or structural changes induced by modifications are likely causes of the decrease in crystallin solubility associated with…”
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In Vivo Modification of the C-Terminal Lysine of Human Lens αB-Crystallin by LIN, PEIPING, SMITH, DAVID L, SMITH, JEAN B

“…Both the structural and chaperone-like properties of lens α-crystallins have been implicated in maintaining lens transparency. Modifications of lens…”
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A Gene for High Urinary Kallikrein May Protect Against Hypertension in Utah Kindreds by Berry, Thomas D, Hasstedt, Sandra J, Hunt, Steven C, Wu, Lily L, Smith, Jean B, Ash, Owen K, Kuida, Hiroshi, Williams, Roger R

“…The inheritance of 12-hour overnight total urinary kallikrein excretion and its association with family history of essential hypertension were studied in 405…”
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Associations of Three Erythrocyte Cation Transport Systems with Plasma Lipids in Utah Subjects by HUNT, STEVEN C, WILLIAMS, ROGER R, SMITH, JEAN B, ASH, K OWEN

“…To investigate the pathophysiology of essential hypertension, detailed biochemical and clinical variables were collected and analyzed for 2091 Utah subjects…”
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Site-specific glycation of lens crystallins by ascorbic acid by Ortwerth, B J, Slight, S H, Prabhakaram, M, Sun, Y, Smith, J B

“…The oxidation of ascorbic acid leads to the formation of several compounds which are capable of reacting with protein amino groups via a Maillard reaction…”
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Sodium-lithium countertransport in erythrocytes of hypertension prone families in Utah by Williams, R R, Hunt, S C, Kuida, H, Smith, J B, Ash, K O

“…Sodium-lithium countertransport was measured in July 1980-December 1982 in 841 persons from 48 Utah families prone to hypertension. Mean countertransport in 54…”
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Increased sodium-lithium countertransport in erythrocytes of pregnant women by Worley, R J, Hentschel, W M, Cormier, C, Nutting, S, Pead, G, Zelenkov, K, Smith, J B, Ash, K O, Williams, R R

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Red-Cell Sodium-Lithium Countertransport and Fractional Excretion of Lithium in Normal and Hypertensive Humans by Weinberger, Myron H, Smith, Jean B, Fineberg, Naomi S, Luft, Friedrich C

“…To examine the relations between erythrocyte sodium-lithium countertransport and renal proximal tubular sodium handling, we measured countertransport, and then…”
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Modifications of human βA1/βA3‐crystallins include S‐methylation, glutathiolation, and truncation by Lapko, Veniamin N., Cerny, Ronald L., Smith, David L., Smith, Jean B.

“…Disulfide bonding of lens crystallins contributes to the aggregation and insolubilization of these proteins that leads to cataract. A high concentration of…”
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