Search results for: Larry L. David

Items from 1 to 20 out of 45 results

article

Effects of ex vivo blood anticoagulation and preanalytical processing time on the proteome content of platelets

Samuel Tassi Yunga, Austin J. Gower, Alexander R. Melrose, Meghan K. Fitzgerald, more

Journal of Thrombosis and Haemostasis > 20 > 6 > 1437 - 1450

Background Ex vivo assays of platelet function critically inform mechanistic and clinical hematology studies, where effects of divergent blood processing methods on platelet composition are apparent, but unspecified. Objective Here, we evaluate how different blood anticoagulation options and processing times affect platelet function and protein content ex vivo. Methods Parallel blood samples...

article

Cumulative deamidations of the major lens protein γS‐crystallin increase its aggregation during unfolding and oxidation

Calvin J. Vetter, David C. Thorn, Samuel G. Wheeler, Charlie C. Mundorff, more

Protein Science > 29 > 9 > 1945 - 1963

Age‐related lens cataract is the major cause of blindness worldwide. The mechanisms whereby crystallins, the predominant lens proteins, assemble into large aggregates that scatter light within the lens, and cause cataract, are poorly understood. Due to the lack of protein turnover in the lens, crystallins are long‐lived. A major crystallin, γS, is heavily modified by deamidation, in particular at...

article

Identification, Quantification, and System Analysis of Protein N‐ε Lysine Methylation in Anucleate Blood Platelets

Anne D. Rocheleau, Alexander R. Melrose, Jennifer M. Cunliffe, John Klimek, more

PROTEOMICS > 19 > 11 > n/a - n/a

Protein posttranslational modifications critically regulate a range of physiological and disease processes. In addition to tyrosine, serine, and threonine phosphorylation, reversible N‐ε acylation and alkylation of protein lysine residues also modulate diverse aspects of cellular function. Studies of lysine acyl and alkyl modifications have focused on nuclear proteins in epigenetic regulation; however,...

article

Angiogenic and Immunologic Proteins Identified by Deep Proteomic Profiling of Human Retinal and Choroidal Vascular Endothelial Cells: Potential Targets for New Biologic Drugs

Justine R. Smith, Larry L. David, Binoy Appukuttan, Phillip A. Wilmarth

American Journal of Ophthalmology > 2018 > 193 > C > 197-229

Diseases that involve retinal or choroidal vascular endothelial cells are leading causes of vision loss: age-related macular degeneration, retinal ischemic vasculopathies, and noninfectious posterior uveitis. Proteins differentially expressed by these endothelial cell populations are potential drug targets. We used deep proteomic profiling to define the molecular phenotype of human retinal and choroidal...

article

Coordinated responses to individual tumor antigens by IgG antibody and CD8+ T cells following cancer vaccination

Tyler W. Hulett, Shawn M. Jensen, Phillip A. Wilmarth, Ashok P. Reddy, more

Journal for ImmunoTherapy of Cancer > 2018 > 6 > 1 > 1-14

Background One of today’s greatest hurdles for cancer immunotherapy is the absence of information regarding which tumor antigens are already recognized by patients receiving immunotherapies, and whether those therapies then boost or generate an immune response against tumor proteins. For CD8+ T cells in particular, patient-specific immune recognition and responses at the level of individual tumor...

article

γ‐Crystallins of the chicken lens: remnants of an ancient vertebrate gene family in birds

Yingwei Chen, Vatsala Sagar, Hoay‐Shuen Len, Katherine Peterson, more

The FEBS Journal > 283 > 8 > 1516 - 1530

γ‐Crystallins, abundant proteins of vertebrate lenses, were thought to be absent from birds. However, bird genomes contain well‐conserved genes for γS‐ and γN‐crystallins. Although expressed sequence tag analysis of chicken eye found no transcripts for these genes, RT‐PCR detected spliced transcripts for both genes in chicken lens, with lower levels in cornea and retina/retinal pigment epithelium...

article

Identifying Family-Member-Specific Targets of Mono-ARTDs by Using a Chemical Genetics Approach

Ian Carter-O’Connell, Haihong Jin, Rory K. Morgan, Roko Zaja, more

Cell Reports > 2016 > 14 > 3 > 621-631

ADP-ribosyltransferases (ARTD1–16) have emerged as major downstream effectors of NAD⁺ signaling in the cell. Most ARTDs (ARTD7 and 8, 10–12, and 14–17) catalyze the transfer of a single unit of ADP-ribose from NAD⁺ to target proteins, a process known as mono-ADP-ribosylation (MARylation). Progress in understanding the cellular functions of MARylation has been limited by the inability to identify the...

article

Differences in solution dynamics between lens β-crystallin homodimers and heterodimers probed by hydrogen–deuterium exchange and deamidation

Kirsten J. Lampi, Matthew R. Murray, Matthew P. Peterson, Bryce S. Eng, more

Biochimica et Biophysica Acta (BBA) - General Subjects > 2016 > 1860 > 1(PB) > 304-314

Lens transparency is due to the ordered arrangement of the major structural proteins, called crystallins. βB2 crystallin in the lens of the eye readily forms dimers with other β-crystallin subunits, but the resulting heterodimer structures are not known and were investigated in this study.Structures of βA3 and βB2 crystallin homodimers and the βA3/βB2 crystallin heterodimers were probed by measuring...

article

Data detailing the platelet acetyl-lysine proteome

Joseph E. Aslan, Larry L. David, Owen J.T. McCarty

Data in Brief > 2015 > 5 > C > 368-371

Here we detail proteomics data that describe the acetyl-lysine proteome of blood platelets (Aslan et al., 2015 [1]). An affinity purification – mass spectrometry (AP-MS) approach was used to identify proteins modified by Nε-lysine acetylation in quiescent, washed human platelets. The data provide insights into potential regulatory mechanisms of platelet function mediated by protein lysine acetylation...

article

Cotranslational Stabilization of Sec62/63 within the ER Sec61 Translocon Is Controlled by Distinct Substrate-Driven Translocation Events

Brian J. Conti, Prasanna K. Devaraneni, Zhongying Yang, Larry L. David, more

Molecular Cell > 2015 > 58 > 2 > 269-283

The ER Sec61 translocon is a large macromolecular machine responsible for partitioning secretory and membrane polypeptides into the lumen, cytosol, and lipid bilayer. Because the Sec61 protein-conducting channel has been isolated in multiple membrane-derived complexes, we determined how the nascent polypeptide modulates translocon component associations during defined cotranslational translocation...

article

Lens β-crystallins: The role of deamidation and related modifications in aging and cataract

Kirsten J. Lampi, Phillip A. Wilmarth, Matthew R. Murray, Larry L. David

Progress in Biophysics and Molecular Biology > 2014 > 115 > 1 > 21-31

Crystallins are the major proteins in the lens of the eye and function to maintain transparency of the lens. Of the human crystallins, α, β, and γ, the β-crystallins remain the most elusive in their structural significance due to their greater number of subunits and possible oligomer formations. The β-crystallins are also heavily modified during aging. This review focuses on the functional significance...

article

Mechanisms of glucagon degradation at alkaline pH

Nicholas Caputo, Jessica R. Castle, Colin P. Bergstrom, Julie M. Carroll, more

Peptides > 2013 > 45 > Complete > 40-47

Glucagon is unstable and undergoes degradation and aggregation in aqueous solution. For this reason, its use in portable pumps for closed loop management of diabetes is limited to very short periods. In this study, we sought to identify the degradation mechanisms and the bioactivity of specific degradation products. We studied degradation in the alkaline range, a range at which aggregation is minimized...

article

Verification and spatial localization of aquaporin-5 in the ocular lens

Angus C. Grey, Kerry L. Walker, Rosica S. Petrova, Jun Han, more

Experimental Eye Research > 2013 > 108 > Complete > 94-102

Until recently, the lens was thought to express only two aquaporin (AQP) water channels, AQP1 and AQP0. In this study we confirm lenticular AQP5 protein expression by Western blotting and mass spectrometry in lenses from a variety of species. In addition, confocal microscopy was used to map cellular distributions of AQP5 in mouse, rat and human lenses. Tandem mass spectrometry of a human lens membrane...

article

Role of the retinal vascular endothelial cell in ocular disease

Arpita S. Bharadwaj, Binoy Appukuttan, Phillip A. Wilmarth, Yuzhen Pan, more

Progress in Retinal and Eye Research > 2013 > 32 > Complete > 102-180

Retinal endothelial cells line the arborizing microvasculature that supplies and drains the neural retina. The anatomical and physiological characteristics of these endothelial cells are consistent with nutritional requirements and protection of a tissue critical to vision. On the one hand, the endothelium must ensure the supply of oxygen and other nutrients to the metabolically active retina, and...

article

Changes in solvent accessibility of wild-type and deamidated βB2-crystallin following complex formation with αA-crystallin

Kirsten J. Lampi, Cade B. Fox, Larry L. David

Experimental Eye Research > 2012 > 104 > Complete > 48-58

Aberrant protein interactions can lead to aggregation and insolubilization, such as occurs during cataract formation. Deamidation, a prevalent age-related modification in the lens of the eye, decreases stability of the major lens proteins, crystallins. The mechanism of deamidation altering interactions between αA-crystallin and βB2-crystallin was investigated by detecting changes in solvent accessibility...

article

Is protein methylation in the human lens a result of non-enzymatic methylation by S-adenosylmethionine?

Roger J.W. Truscott, Jasminka Mizdrak, Michael G. Friedrich, Michelle Y. Hooi, more

Experimental Eye Research > 2012 > 99 > Complete > 48-54

Since crystallins in the human lens do not turnover, they are susceptible to modification by reactive molecules over time. Methylation is a major post-translational lens modification, however the source of the methyl group is not known and the extent of modification across all crystallins has yet to be determined. Sites of methylation in human lens proteins were determined using HPLC/mass spectrometry...

article

Stable Liquid Glucagon Formulations for Rescue Treatment and Bi-Hormonal Closed-Loop Pancreas

Melanie A. Jackson, Nicholas Caputo, Jessica R. Castle, Larry L. David, more

Current Diabetes Reports > 2012 > 12 > 6 > 705-710

Small doses of glucagon given subcutaneously in the research setting by an automated system prevent most cases of hypoglycemia in persons with diabetes. However, glucagon is very unstable and cannot be kept in a portable pump. Glucagon rapidly forms amyloid fibrils, even within the first day after reconstitution. Aggregation eventually leads to insoluble gels, which occlude pump catheters. Fibrillation...

article

Protein Database and Quantitative Analysis Considerations when Integrating Genetics and Proteomics to Compare Mouse Strains

Suzanne S. Fei, Phillip A. Wilmarth, Robert J. Hitzemann, Shannon K. McWeeney, more

Journal of Proteome Research > 2011 > 10 > 7 > 2905 - 2912

article

On the biomarkers and mechanisms of konzo, a distinct upper motor neuron disease associated with food (cassava) cyanogenic exposure

Roman M. Kassa, Nyamabo L. Kasensa, Victor H. Monterroso, Robert J. Kayton, more

Food and Chemical Toxicology > 2011 > 49 > 3 > 571-578

Konzo is a self-limiting central motor-system disease associated with food dependency on cassava and low dietary intake of sulfur amino acids (SAA). Under conditions of SAA-deficiency, ingested cassava cyanogens yield metabolites that include thiocyanate and cyanate, a protein-carbamoylating agent. We studied the physical and biochemical modifications of rat serum and spinal cord proteins arising...

article

Solvent accessibility of βB2-crystallin and local structural changes due to deamidation at the dimer interface

Takumi Takata, Joshua P. Smith, Brian Arbogast, Larry L. David, more

Experimental Eye Research > 2010 > 91 > 3 > 336-346

In the lens of the eye the ordered arrangement of the major proteins, the crystallins, contributes to lens transparency. Members of the β/γ-crystallin family share common β-sheet rich domains and hydrophobic regions at the monomer–monomer or domain–domain interfaces. Disruption of these interfaces, due to post-translational modifications, such as deamidation, decreases the stability of the crystallins...

Publication date

Last 3 years (1)

Close

Date range setting

Set the date range to filter the displayed results. You can set a starting date, ending date or both. You can enter the dates manually or choose them from the calendar.

From:

To:
Set your own date range

INFONA - science communication portal

Search results for: Larry L. David

Effects of ex vivo blood anticoagulation and preanalytical processing time on the proteome content of platelets

Cumulative deamidations of the major lens protein γS‐crystallin increase its aggregation during unfolding and oxidation

Identification, Quantification, and System Analysis of Protein N‐ε Lysine Methylation in Anucleate Blood Platelets

Angiogenic and Immunologic Proteins Identified by Deep Proteomic Profiling of Human Retinal and Choroidal Vascular Endothelial Cells: Potential Targets for New Biologic Drugs

Coordinated responses to individual tumor antigens by IgG antibody and CD8+ T cells following cancer vaccination

γ‐Crystallins of the chicken lens: remnants of an ancient vertebrate gene family in birds

Identifying Family-Member-Specific Targets of Mono-ARTDs by Using a Chemical Genetics Approach

Differences in solution dynamics between lens β-crystallin homodimers and heterodimers probed by hydrogen–deuterium exchange and deamidation

Data detailing the platelet acetyl-lysine proteome

Cotranslational Stabilization of Sec62/63 within the ER Sec61 Translocon Is Controlled by Distinct Substrate-Driven Translocation Events

Lens β-crystallins: The role of deamidation and related modifications in aging and cataract

Mechanisms of glucagon degradation at alkaline pH

Verification and spatial localization of aquaporin-5 in the ocular lens

Role of the retinal vascular endothelial cell in ocular disease

Changes in solvent accessibility of wild-type and deamidated βB2-crystallin following complex formation with αA-crystallin

Is protein methylation in the human lens a result of non-enzymatic methylation by S-adenosylmethionine?

Stable Liquid Glucagon Formulations for Rescue Treatment and Bi-Hormonal Closed-Loop Pancreas

Protein Database and Quantitative Analysis Considerations when Integrating Genetics and Proteomics to Compare Mouse Strains

On the biomarkers and mechanisms of konzo, a distinct upper motor neuron disease associated with food (cassava) cyanogenic exposure

Solvent accessibility of βB2-crystallin and local structural changes due to deamidation at the dimer interface

Filter options

Publication date

Keywords

Data set

Journal

INFONA - science communication portal

Search results for: Larry L. David

Add recipient

Sending message cancelled

Are you sure you want to cancel sending this message?

Send message

Filter options

Publication date

Date range setting

Set the date range to filter the displayed results. You can set a starting date, ending date or both. You can enter the dates manually or choose them from the calendar.

Keywords

Data set

Journal

Reporting an error / abuse

Sending the report failed

Accessibility options