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  1. Article

    Open Access

    A resource database for protein kinase substrate sequence-preference motifs based on large-scale mass spectrometry data

    Protein phosphorylation is one of the most prevalent posttranslational modifications involved in molecular control of cellular processes, and is mediated by over 520 protein kinases in humans and other mammals...

    Brian G. Poll, Kirby T. Leo, Venky Deshpande in Cell Communication and Signaling (2024)

  2. Article

    Open Access

    Signaling mechanisms in renal compensatory hypertrophy revealed by multi-omics

    Loss of a kidney results in compensatory growth of the remaining kidney, a phenomenon of considerable clinical importance. However, the mechanisms involved are largely unknown. Here, we use a multi-omic approa...

    Hiroaki Kikuchi, Chung-Lin Chou, Chin-Rang Yang, Lihe Chen in Nature Communications (2023)

  3. Article

    Open Access

    Identification of Daboia siamensis venome using integrated multi-omics data

    Snakebite, classified by World Health Organization as a neglected tropical disease, causes more than 100,000 deaths and 2 million injuries per year. Currently, available antivenoms do not bind with strong spec...

    Thammakorn Saethang, Poorichaya Somparn, Sunchai Payungporn in Scientific Reports (2022)

  4. Article

    Open Access

    Bayesian analysis of dynamic phosphoproteomic data identifies protein kinases mediating GPCR responses

    A major goal in the discovery of cellular signaling networks is to identify regulated phosphorylation sites (“phosphosites”) and map them to the responsible protein kinases. The V2 vasopressin receptor is a G-...

    Kirby T. Leo, Chung-Lin Chou, Chin-Rang Yang in Cell Communication and Signaling (2022)

  5. Article

    Open Access

    NGS-Integrator: An efficient tool for combining multiple NGS data tracks using minimum Bayes’ factors

    Next-generation sequencing (NGS) is widely used for genome-wide identification and quantification of DNA elements involved in the regulation of gene transcription. Studies that generate multiple high-throughpu...

    Bronte Wen, Hyun Jun Jung, Lihe Chen, Fahad Saeed, Mark A. Knepper in BMC Genomics (2020)

  6. Article

    Open Access

    Phosphorylation Changes in Response to Kinase Inhibitor H89 in PKA-Null Cells

    Protein phosphorylation, mediated by protein kinases, plays a crucial role in cellular regulation. One of the most important protein kinases is protein kinase A (PKA). N-[2-p-bromocinnamylamino-ethyl]-5-isoqui...

    Kavee Limbutara, Andrew Kelleher, Chin-Rang Yang in Scientific Reports (2019)

  7. Article

    Open Access

    Systems-level analysis reveals selective regulation of Aqp2 gene expression by vasopressin

    Vasopressin-mediated regulation of renal water excretion is defective in a variety of water balance disorders in humans. It occurs in part through long-term mechanisms that regulate the abundance of the aquapo...

    Pablo C. Sandoval, J’Neka S. Claxton, Jae Wook Lee, Fahad Saeed in Scientific Reports (2016)

  8. No Access

    Protocol

    Peptide Labeling Using Isobaric Tagging Reagents for Quantitative Phosphoproteomics

    Isobaric tagging reagents have become an invaluable tool for multiplexed quantitative proteomic analysis. These reagents can label multiple, distinct peptide samples from virtually any source material (e.g., t...

    Lei Cheng, Trairak Pisitkun, Mark A. Knepper, Jason D. Hoffert in Phospho-Proteomics (2016)

  9. No Access

    Article

    Exploiting thread-level and instruction-level parallelism to cluster mass spectrometry data using multicore architectures

    Modern mass spectrometers can produce large numbers of peptide spectra from complex biological samples in a short time. A substantial amount of redundancy is observed in these data sets from peptides that may ...

    Fahad Saeed, Jason D. Hoffert in Network Modeling Analysis in Health Inform… (2014)

  10. No Access

    Article

    Vasopressin and the regulation of aquaporin-2

    Water excretion is regulated in large part through the regulation of osmotic water permeability of the renal collecting duct epithelium. Water permeability is controlled by vasopressin through regulation of th...

    Justin L. L. Wilson, Carlos A. Miranda in Clinical and Experimental Nephrology (2013)

  11. Article

    Open Access

    PhosSA: Fast and accurate phosphorylation site assignment algorithm for mass spectrometry data

    Phosphorylation site assignment of high throughput tandem mass spectrometry (LC-MS/MS) data is one of the most common and critical aspects of phosphoproteomics. Correctly assigning phosphorylated residues help...

    Fahad Saeed, Trairak Pisitkun, Jason D Hoffert, Sara Rashidian in Proteome Science (2013)

  12. No Access

    Protocol

    Isolation and Purification of Exosomes in Urine

    Exosomes represent an important and readily isolated subset of the urinary proteome that has the potential to shed much insight on the health status of the kidney. Each segment of the nephron sheds exosomes in...

    Patricia A. Gonzales, Hua Zhou, Trairak Pisitkun, Nam Sun Wang in The Urinary Proteome (2010)

  13. No Access

    Article

    Molecular coin slots for urea

    Membrane-bound protein channels that allow only urea to pass through are vital to the kidney's ability to conserve water. Crystal structures show that the channels select urea molecules by passing them through...

    Mark A. Knepper, Joseph A. Mindell in Nature (2009)

  14. No Access

    Article

    Courier service for ammonia

    Physiological studies in mice demonstrate a surprising role for a kidney protein related to the rhesus factor of red blood cells. Similar research would aid further annotation of mammalian genomes.

    Mark A. Knepper in Nature (2008)

  15. No Access

    Article

    Vasopressin: friend or foe?

    Vasopressin plays a vital part in homeostasis by regulating water excretion in the kidney. But it seems that vasopressin also dampens the inflammatory response to uropathogenic Escherichia coli—a finding that add...

    Mark A Knepper, Robert A Star in Nature Medicine (2008)

  16. No Access

    Chapter

    Regulation of Renal Aquaporins and Sodium Transporters During Vasopressin-Escape in the Rat

    Several clinical conditions, e.g., congestive heart failure and cirrhosis are associated with inappropriately elevated vasopressin levels relative to serum osmolality (Bichet et al., 1992). In addition, ectopic p...

    Carolyn A. Ecelbarger, Takashi Murase in Molecular Biology and Physiology of Water … (2000)

  17. No Access

    Chapter

    Oxytocin: One of the Factors for Regulating AQP2 Localization and Urinary AQP2 Excretion

    Aquaporin-2 (AQP2), an essential water channel for urinary concentration, is mainly located in the apical plasma membrane of collecting duct epithelial cells, and vasopressin is the major factor for regulation...

    ** Suk Han, Un Sil Jeon, Kwon Wook Joo in Molecular Biology and Physiology of Water … (2000)

  18. No Access

    Chapter

    Studies of Renal Aquaporin-2 Expression during Renal Escape from Vasopressin-Induced Antidiuresis

    In animal models of the syndrome of inappropriate antidiuresis (SIADH), sustained administration of vasopressin and water results in free-water retention and progressive hyponatremia for several days, which is...

    Joseph G. Verbalis, Takashi Murase, Carolyn A. Ecelbarger in Vasopressin and Oxytocin (1998)

  19. No Access

    Chapter

    Ultramicro-Analysis of Tubular Fluid by Continuous-Flow Methodology

    The measurement of net transepithelial fluxes in isolated perfused tubule experiments requires highly sensitive analytical methods, capable of precise determination of solute concentrations in 1–30 nanoliter s...

    Mark A. Knepper in Nephrology (1991)

  20. No Access

    Chapter

    Urinary Concentrating and Diluting Processes

    Body fluid osmolality is normally maintained within narrow bounds through the control of body water balance. Water intake is regulated to some degree by the thirst mechanism.(1) However, the chief means by whi...

    Mark A. Knepper, John L. Stephenson in Membrane Transport Processes in Organized Systems (1987)

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