Daniel Rosenberg on Muck Rack

Daniel Rosenberg

As seen in: Agricultura, Medium, The Startup, Color Research & Application, Forbes, HuffPost, Nature, Wiley Online Library, Memory Studies, The London Standard, The Wall Street Journal and
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Articles

Angels in Distress, Inc. Launches Free Public Membership to Expand Wildlife Protection Efforts

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By Daniel Rosenberg
| EIN Presswire
Angels in Distress, Inc., announces the launch of its new public membership program. Protecting wildlife is not a task reserved for a select few—it’s a shared responsibility.
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40 Years of the M&A Committee: How 40 Years of Technology Transformation Rewrote the M&A Lawyer’s Playbook

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By Daniel Rosenberg
| ABA Business Law Section
When the founders of the Mergers & Acquisitions Committee first gathered four decades ago, M&A was very different. To mark the forty-year anniversary of the Business Law Section’s M&A Committee, Daniel Rosenberg, chair of the Committee’s Technology in M&A Subcommittee, surveys how technology has reshaped M&A, bringing us to the start of a new technology revolution arguably as significant as all previous ones combined. Late 1980s In the second half of the 1980s, M&A was largely analog.
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Structural basis of the promiscuity of the unusual Fe(II) and 2-oxoglutarate dependent human aspartate/asparagine-β-hydroxylase - Nature Communications

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By Mariska de Munnik, Amelia Brasnett, Tiankun Zhou, William Myers, Yicheng Wang, Kuntal Chatterjee, Anthony Tumber, Stephen Marshall, Philipp Simon, Pierre Aller, Danny Axford, Hiroki Makita, Daniel W. Paley, Vandana Tiwari, Sebastian Dehe, Humberto Sanchez, Daniel Rosenberg, Roberto Alonso-Mori, Asmit Bhowmick, Junko Yano, Vittal K. Yachandra, Jaehyun Park, Sehan Park, Allen M. Orville, Lennart Brewitz, Jan Kern, Christopher J Schofield, Patrick Rabe, Anastasiia Shilova, Alexander T. Stead
| Nature
Abstract Protein-hydroxylation catalysed by Fe(II) and 2-oxoglutarate (2OG) dependent oxygenases is an important regulatory mechanism in human biology. Such oxygenases typically coordinate their Fe(II) cofactor via a conserved triad of an aspartate- or glutamate- and two histidine-residues.
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