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12,093 result(s) for "Hoffman, David"
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Longer trips to court cause evictions
Studying ∼200,000 evictions filed against ∼300,000 Philadelphians from 2005 to 2021, we focus on the role of transit to court in preventing tenants from asserting their rights. In this period, nearly 40% of tenants facing eviction were ordered to leave their residences because they did not show up to contest cases against them and received a default judgment. Controlling for a variety of potential confounds at the tenant and landlord level, we find that residents of private tenancies with longer transit travel time to the courthouse were more likely to default. A 1-h increase in estimated travel time increases the probability of default by between 3.8% and 8.6% points across different model specifications. The effect holds after adjusting for direct distance to the court, unobserved landlord characteristics, and even baseline weekend travel time. However, it is absent in public housing evictions, where timing rules are significantly laxer, and during the COVID-19 pandemic, when tenants had the opportunity to be present virtually. We estimate that had all tenants been equally able to get to the court in 10 min, there would have been 4,000 to 9,000 fewer default evictions over the sample period. We replicate this commuting effect in another dataset of over 800,000 evictions from Harris County, Texas. These results open up a new way to study the physical determinants of access to justice, illustrating that the location and accessibility of a courthouse can affect individual case outcomes. We suggest that increased use of video technology in court may reduce barriers to justice.
Motion of VAPB molecules reveals ER–mitochondria contact site subdomains
To coordinate cellular physiology, eukaryotic cells rely on the rapid exchange of molecules at specialized organelle–organelle contact sites 1 , 2 . Endoplasmic reticulum–mitochondrial contact sites (ERMCSs) are particularly vital communication hubs, playing key roles in the exchange of signalling molecules, lipids and metabolites 3 , 4 . ERMCSs are maintained by interactions between complementary tethering molecules on the surface of each organelle 5 , 6 . However, due to the extreme sensitivity of these membrane interfaces to experimental perturbation 7 , 8 , a clear understanding of their nanoscale organization and regulation is still lacking. Here we combine three-dimensional electron microscopy with high-speed molecular tracking of a model organelle tether, Vesicle-associated membrane protein (VAMP)-associated protein B (VAPB), to map the structure and diffusion landscape of ERMCSs. We uncovered dynamic subdomains within VAPB contact sites that correlate with ER membrane curvature and undergo rapid remodelling. We show that VAPB molecules enter and leave ERMCSs within seconds, despite the contact site itself remaining stable over much longer time scales. This metastability allows ERMCSs to remodel with changes in the physiological environment to accommodate metabolic needs of the cell. An amyotrophic lateral sclerosis-associated mutation in VAPB perturbs these subdomains, likely impairing their remodelling capacity and resulting in impaired interorganelle communication. These results establish high-speed single-molecule imaging as a new tool for mapping the structure of contact site interfaces and reveal that the diffusion landscape of VAPB at contact sites is a crucial component of ERMCS homeostasis. High-speed molecular tracking is integrated with three-dimensional electron microscopy to map the diffusion distribution and ultrastructure of endoplasmic reticulum-mitochondria contact sites, revealing the ability of high-speed single-molecule imaging to map contact site interface structures and corresponding diffusion landscapes.
The billion dollar spy : a true story of Cold War espionage and betrayal
\"While getting into his car on the evening of February 16, 1978, the chief of the CIA's Moscow station was handed an envelope by an unknown Russian. Its contents stunned the Americans: details of top-secret Soviet research and development in military technology that was totally unknown to the United States. From 1979 to 1985, Adolf Tolkachev, an engineer at a military research center, cracked open the secret Soviet military research establishment, using his access to hand over tens of thousands of pages of material about the latest advances in aviation technology, alerting the Americans to possible developments years in the future. He was one of the most productive and valuable spies ever to work for the United States in the four decades of global confrontation with the Soviet Union. Tolkachev took enormous personal risks, but so did his CIA handlers. Moscow station was a dangerous posting to the KGB's backyard. The CIA had long struggled to recruit and run agents in Moscow, and Tolkachev became a singular breakthrough. With hidden cameras and secret codes, and in face-to-face meetings with CIA case officers in parks and on street corners, Tolkachev and the CIA worked to elude the feared KGB. Drawing on previously secret documents obtained from the CIA, as well as interviews with participants, Hoffman reveals how the depredations of the Soviet state motivated one man to master the craft of spying against his own nation until he was betrayed to the KGB by a disgruntled former CIA trainee. No one has ever told this story before in such detail, and Hoffman's deep knowledge of spycraft, the Cold War, and military technology makes him uniquely qualified to bring readers this real-life espionage thriller\"--Provided by publisher.
DEFEATING THE EMPIRE OF FORMS
For generations, contract scholars have waged a faint-hearted campaign against form contracts. It’s widely believed that adhesive forms are unread and chock-full of terms that courts will not, or should not, enforce. Most think that the market for contract terms is broken, for both employees and consumer adherents. And yet forms are so embedded in our economy that it’s hard to imagine modern commercial life without them. Scholars thus push calibrated, careful solutions that walk a deeply rutted path. Notwithstanding hundreds of proposals calling for their retrenchment, the empire of forms has continued to advance into new areas of social life: we now click to agree to more written contracts every few days than our grandparents did in their entire lives. This Article argues that the swelling scope of the empire of forms is itself a social problem, and it demands both a new diagnosis and a structural reform. Forms are everywhere in our lives because we’ve brought them with us in our pockets, and on our devices. Contract law hasn’t changed to make forms more valuable; the cost of contracting has fallen to make them ever cheaper to distribute. This encourages their distribution even though they individually are less valuable to firms. All the while, cheap forms externalize too many harms and threaten important legal values which we should defend. What’s needed is a remedy that cuts off the supply of cheap forms at its source and returns us to a world with fewer written contracts. I offer that reform with a proposed state law: the statute of frauds flipped upside-down. It would make low-stakes written-form contracts, directed at either employees or consumers, simply unenforceable. I defend the statute against charges that it is worse medicine than the mass contracting disease it seeks to cure.
Correlative three-dimensional super-resolution and block-face electron microscopy of whole vitreously frozen cells
Cells need to compartmentalize thousands of distinct proteins, but the nanoscale spatial relationship of many proteins to overall intracellular ultrastructure remains poorly understood. Correlated light and electron microscopy approaches can help. Hoffman et al. combined cryogenic super-resolution fluorescence microscopy and focused ion beam–milling scanning electron microscopy to visualize protein-ultrastructure relationships in three dimensions across whole cells. The fusion of the two imaging modalities enabled identification and three-dimensional segmentation of morphologically complex structures within the crowded intracellular environment. The researchers observed unexpected relationships within a variety of cell types, including a web-like protein adhesion network between juxtaposed cerebellar granule neurons. Science , this issue p. eaaz5357 Cryogenic super-resolution fluorescence and electron microscopy reveals protein-ultrastructure relationships in whole cells. Within cells, the spatial compartmentalization of thousands of distinct proteins serves a multitude of diverse biochemical needs. Correlative super-resolution (SR) fluorescence and electron microscopy (EM) can elucidate protein spatial relationships to global ultrastructure, but has suffered from tradeoffs of structure preservation, fluorescence retention, resolution, and field of view. We developed a platform for three-dimensional cryogenic SR and focused ion beam–milled block-face EM across entire vitreously frozen cells. The approach preserves ultrastructure while enabling independent SR and EM workflow optimization. We discovered unexpected protein-ultrastructure relationships in mammalian cells including intranuclear vesicles containing endoplasmic reticulum–associated proteins, web-like adhesions between cultured neurons, and chromatin domains subclassified on the basis of transcriptional activity. Our findings illustrate the value of a comprehensive multimodal view of ultrastructural variability across whole cells.
Position-specific carbon stable isotope analysis of glyphosate: isotope fingerprinting of molecules within a mixture
Glyphosate [N-(phosphonomethyl) glycine] is a widely used herbicide and a molecule of interest in the environmental sciences, due to its global use in agriculture and its potential impact on ecosystems. This study presents the first position-specific carbon isotope (13C/12C) analyses of glyphosates from multiple sources. In contrast to traditional isotope ratio mass spectrometry (IRMS), position-specific analysis provides 13C/12C ratios at individual carbon atom positions within a molecule, rather than an average carbon isotope ratio across a mixture or a specific compound. In this work, glyphosate in commercial herbicides was analyzed with only minimal purification, using a nuclear magnetic resonance (NMR) spectroscopy method that detects 1H nuclei with bonds to either 13C or 12C, and isolates the signals of interest from other signals in the mixture. Results demonstrate that glyphosate from different sources can have significantly different intramolecular 13C/12C distributions, which were found to be spread over a wide range, with δ13C Vienna Peedee Belemnite (VPDB) values of −28.7 to −57.9‰. In each glyphosate, the carbon with a bond to the phosphorus atom was found to be depleted in 13C compared to the carbon at the C2 position, by 4 to 10‰. Aminomethylphosphonic acid (AMPA) was analyzed for method validation; AMPA contains only a single carbon position, so the 13C/12C results provided by the NMR method could be directly compared with traditional isotope ratio mass spectrometry. The glyphosate mixtures were also analyzed by IRMS to obtain their average 13C/12C ratios, for comparison with our position-specific results. This comparison revealed that the IRMS results significantly disguise the intramolecular isotope distribution. Finally, we introduce a 31P NMR method that can provide a position-specific 13C/12C ratio for carbon positions with a C-P chemical bond, and the results obtained by 1H and 31P for C3 carbon agree with one another within their analytical uncertainty. These analytical tools for position-specific carbon isotope analysis permit the isotopic fingerprinting of target molecules within a mixture, with potential applications in a range of fields, including the environmental sciences and chemical forensics.