Search Results - "Pearlman, Samuel M."

A Mechanism for the Evolution of Phosphorylation Sites by Pearlman, Samuel M., Serber, Zach, Ferrell, James E.

“…Protein phosphorylation provides a mechanism for the rapid, reversible control of protein function. Phosphorylation adds negative charge to amino acid side…”
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SAFA: semi-automated footprinting analysis software for high-throughput quantification of nucleic acid footprinting experiments by Das, Rhiju, Laederach, Alain, Pearlman, Samuel M, Herschlag, Daniel, Altman, Russ B

“…Footprinting is a powerful and widely used tool for characterizing the structure, thermodynamics, and kinetics of nucleic acid folding and ligand binding…”
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TagGraph reveals vast protein modification landscapes from large tandem mass spectrometry datasets by Devabhaktuni, Arun, Lin, Sarah, Zhang, Lichao, Swaminathan, Kavya, Gonzalez, Carlos G., Olsson, Niclas, Pearlman, Samuel M., Rawson, Keith, Elias, Joshua E.

“…Although mass spectrometry is well suited to identifying thousands of potential protein post-translational modifications (PTMs), it has historically been…”
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Semiautomated and rapid quantification of nucleic acid footprinting and structure mapping experiments by Laederach, Alain, Das, Rhiju, Vicens, Quentin, Pearlman, Samuel M, Brenowitz, Michael, Herschlag, Daniel, Altman, Russ B

“…We have developed protocols for rapidly quantifying the band intensities from nucleic acid chemical mapping gels at single-nucleotide resolution. These…”
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Semi-automated and rapid quantification of nucleic acid footprinting and structure mapping experiments by Laederach, Alain, Das, Rhiju, Vicens, Quentin, Pearlman, Samuel M., Brenowitz, Michael, Herschlag, Daniel, Altman, Russ B.

“…We have developed protocols for rapidly quantifying the band intensities from nucleic acid chemical mapping gels at single nucleotide resolution. These…”
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A Mechanism for the Evolution of Protein Phosphorylation Sites and Application Towards Improving Phorylation Site Prediction by Pearlman, Samuel M

“…Protein phosphorylation provides a mechanism for the rapid, reversible control of protein function. Phosphorylation adds negative charge to amino acid side…”
Get full text