Instruments of Commerce and Knowledge: Probe Microscopy, 1980-2000

Longstanding debates about the role of the university in national culture and the global economy have entered a new phase in the past decade in most industrialized, and several industrializing, countries. One important focus of this debate is corporate involvement in academic scientific research. Proponents of the academic capitalism say that corporate involvement makes the university leaner, more agile, better able to respond to the needs of the day. Critics say that corporate involvement leaves society without the independent, critical voices traditionally lodged in universities. I argue that a science and technology studies perspective, using case studies of research communities, can push this debate in directions envisioned by neither proponents nor critics. I use the development and commercialization of the scanning tunneling microscope and the atomic force microscope as an example of how research communities continually redraw the line between corporate and academic institutions.

Some Experiments on the Utilization of Rice Straw in Papermaking

I. A Brief Description of Rice Straw The botanical name for rice straw is Oryza sativa. Rice is a well-known cereal and is the staple food of hundreds of millions of people. According to R. J. Rochevica, cultivated rice, including all numerous varieties, originated from will species, which are indigenous to Africa, India, and Indo-China (6)

The Squares

When ungroovy scientists did groovy science: how non-activist scientists and engineers adapted their work to a rapidly changing social and political landscape. In The Squares, Cyrus Mody shows how, between the late 1960s and the early 1980s, some scientists and engineers who did not consider themselves activists, New Leftists, or members of the counterculture accommodated their work to the rapidly changing social and political landscape of the time. These “square scientists,” Mody shows, began to do many of the things that the counterculture urged: turn away from military-industrial funding, become more interdisciplinary, and focus their research on solving problems of civil society. During the period Mody calls “the long 1970s,” ungroovy scientists were doing groovy science. Mody offers a series of case studies of some of these collective efforts by non-activist scientists to use their technical knowledge for the good of society. He considers the region around Santa Barbara and the interplay of public universities, think tanks, established firms, new companies, philanthropies, and social movement organizations. He looks at Stanford University's transition from Cold War science to commercialized technoscience; NASA's search for a post-Apollo mission; the unsuccessful foray into solar energy by Nobel laureate Jack Kilby; the “civilianization” of the US semiconductor industry; and systems engineer Arthur D. Hall's ill-fated promotion of automated agriculture

Boston Hospitality Review: Winter 2019

TABLE OF CONTENTS: "Training: The Necessity of Error Management Training in the Hospitality Industry" by Priyanko Guchait; "Trends: Green Hotels: An Overview" by Minu Agarwal and Prashant Das; "Tourism: Panacea or peril? The implications of Neolocalism as a more intrusive form of tourism" by Makarand Mody and Kyle Koslowsky; "Restaurants: How Can Single-Unit Restaurants Strive for Powerful Online Presence?" by Leora Lanz and Jenna Berry; "Retention: Why Hoteliers Stay and Go: Future Oriented Thinking" by Sean McGinley; "Service Recovery: Failure is Not Fatal: Actionable Insights on Service Failure and Recovery for the Hospitality Industry" by Lisa C. Wan and Elisa Chan; "Research: A Detailed Study of the Expected and Actual Use of Hotel Amenities" by Chekitan S. Dev and Prateek Kumar

PD‐1 inhibition in congenital pigment synthesizing metastatic melanoma

A newborn female child was born with a congenital pigment synthesizing melanoma of the scalp. Further workup revealed metastatic disease within the liver, lungs, and left tibia. Whole exome sequencing was performed on multiple samples that revealed one somatic mutation, lysine methyltransferase 2C (KMT2C), at low allelic frequency but no v‐Raf murine sarcoma viral oncogene homolog B (BRAF), NF‐1 mutation. Programmed death ligand 1 was moderately expressed. Treatment was initiated with the programmed cell death protein 1 inhibitor nivolumab. The patient tolerated this treatment well with minimal toxicity. She is now over a year out from initial diagnosis, continuing on nivolumab, with stable disease.Peer Reviewedhttps://deepblue.lib.umich.edu/bitstream/2027.42/139985/1/pbc26702.pdfhttps://deepblue.lib.umich.edu/bitstream/2027.42/139985/2/pbc26702_am.pd

Resolving the Fast Kinetics of Cooperative Binding: Ca2+ Buffering by Calretinin

Cooperativity is one of the most important properties of molecular interactions in biological systems. It is the ability to influence ligand binding at one site of a macromolecule by previous ligand binding at another site of the same molecule. As a consequence, the affinity of the macromolecule for the ligand is either decreased (negative cooperativity) or increased (positive cooperativity). Over the last 100 years, O2 binding to hemoglobin has served as the paradigm for cooperative ligand binding and allosteric modulation, and four practical models were developed to quantitatively describe the mechanism: the Hill, the Adair-Klotz, the Monod-Wyman-Changeux, and the Koshland-Némethy-Filmer models. The predictions of these models apply under static conditions when the binding reactions are at equilibrium. However, in a physiological setting, e.g., inside a cell, the timing and dynamics of the binding events are essential. Hence, it is necessary to determine the dynamic properties of cooperative binding to fully understand the physiological implications of cooperativity. To date, the Monod-Wyman-Changeux model was applied to determine the kinetics of cooperative binding to biologically active molecules. In this model, cooperativity is established by postulating two allosteric isoforms with different binding properties. However, these studies were limited to special cases, where transition rates between allosteric isoforms are much slower than the binding rates or where binding and unbinding rates could be measured independently. For all other cases, the complex mathematical description precludes straightforward interpretations. Here, we report on calculating for the first time the fast dynamics of a cooperative binding process, the binding of Ca2+ to calretinin. Calretinin is a Ca2+-binding protein with four cooperative binding sites and one independent binding site. The Ca2+ binding to calretinin was assessed by measuring the decay of free Ca2+ using a fast fluorescent Ca2+ indicator following rapid (<50-μs rise time) Ca2+ concentration jumps induced by uncaging Ca2+ from DM-nitrophen. To unravel the kinetics of cooperative binding, we devised several approaches based on known cooperative binding models, resulting in a novel and relatively simple model. This model revealed unexpected and highly specific nonlinear properties of cellular Ca2+ regulation by calretinin. The association rate of Ca2+ with calretinin speeds up as the free Ca2+ concentration increases from cytoplasmic resting conditions (∼100 nM) to approximately 1 μM. As a consequence, the Ca2+ buffering speed of calretinin highly depends on the prevailing Ca2+ concentration prior to a perturbation. In addition to providing a novel mode of action of cellular Ca2+ buffering, our model extends the analysis of cooperativity beyond the static steady-state condition, providing a powerful tool for the investigation of the dynamics and functional significance of cooperative binding in general

Role of Post‐Acute Care in Readmissions for Preexisting Healthcare‐Associated Infections

Peer Reviewedhttps://deepblue.lib.umich.edu/bitstream/2027.42/153607/1/jgs16208.pdfhttps://deepblue.lib.umich.edu/bitstream/2027.42/153607/2/jgs16208_am.pd

Leadership Lessons: Developing Mentoring Infrastructure for GEMSSTAR Scholars

Peer Reviewedhttps://deepblue.lib.umich.edu/bitstream/2027.42/149305/1/jgs15787_am.pdfhttps://deepblue.lib.umich.edu/bitstream/2027.42/149305/2/jgs15787.pd