Catalogue Search | MBRL
Are you sure you want to remove the book from the shelf?
{{itemTitle}}
2,295
result(s) for
"Goldman, Robert"
Sort by:
Tomorrow's God : the Hebrew Lord in an age of science
What is the relationship between the Hebrew Bible and modern science? To answer this question, Robert Goldman invites the reader on a carefully guided intellectual journey spanning centuries of theological, philosophical, and scientific thought, before arriving at his provocative conclusion. He begins with the Hebrew Bible, examining the ancient concepts of \"Olam\" and \"Yahweh,\" whose meanings are often lost in translation. Using these concepts as a lens, he explores Spinoza's \"heretical\" (at the time) theological views, probes Einstein's theory of space-time, and confronts formidable questions about human capacity for evil through the writings of Elie Wiesel and Etty Hillesum. Using simple, accessible language, Goldman ties together these diverse perspectives--as well as those of Plato, Maimonides, Godel, and others--and interweaves them with his own insights. Ultimately, he crafts a hopeful vision of a humankind and a God who are evolving toward one another, fueled by good actions, broader consciousness, and deeper human connection. -- Provided by publisher, page 4 of cover
Book
NETosis proceeds by cytoskeleton and endomembrane disassembly and PAD4-mediated chromatin decondensation and nuclear envelope rupture
Neutrophil extracellular traps (NETs) are web-like DNA structures decorated with histones and cytotoxic proteins that are released by activated neutrophils to trap and neutralize pathogens during the innate immune response, but also form in and exacerbate sterile inflammation. Peptidylarginine deiminase 4 (PAD4) citrullinates histones and is required for NET formation (NETosis) in mouse neutrophils. While the in vivo impact of NETs is accumulating, the cellular events driving NETosis and the role of PAD4 in these events are unclear. We performed high-resolution time-lapse microscopy of mouse and human neutrophils and differentiated HL-60 neutrophil-like cells (dHL-60) labeled with fluorescent markers of organelles and stimulated with bacterial toxins or Candida albicans to induce NETosis. Upon stimulation, cells exhibited rapid disassembly of the actin cytoskeleton, followed by shedding of plasma membrane microvesicles, disassembly and remodeling of the microtubule and vimentin cytoskeletons, ER vesiculation, chromatin decondensation and nuclear rounding, progressive plasma membrane and nuclear envelope (NE) permeabilization, nuclear lamin meshwork and then NE rupture to release DNA into the cytoplasm, and finally plasma membrane rupture and discharge of extracellular DNA. Inhibition of actin disassembly blocked NET release. Mouse and dHL-60 cells bearing genetic alteration of PAD4 showed that chromatin decondensation, lamin meshwork and NE rupture and extracellular DNA release required the enzymatic and nuclear localization activities of PAD4. Thus, NETosis proceeds by a stepwise sequence of cellular events culminating in the PAD4-mediated expulsion of DNA.
Journal Article
The company you keep
Jim Grant is a public interest lawyer and single father raising his daughter in the tranquil suburbs of Albany, New York. Grant's world is turned upside down when a brash young reporter exposes his true identity as a former 1970s antiwar radical fugitive wanted for murder.
DVD
The molecular architecture of lamins in somatic cells
Cryo-electron tomography reveals a detailed view of the structural organization of the lamin meshwork within the lamina of the mammalian cell nucleus.
The structure of the nuclear lamina
In the cell nucleus, the lamina is a mesh of intermediate filament proteins called lamins that connects the nuclear envelope to chromatin. It provides structural stability to the nucleus and has a role in chromatin organization, gene transcription and DNA replication. Ohad Medalia and colleagues use cryo-electron tomography to investigate the structural organization of the lamina in the mammalian nucleus. Their analysis of individual lamin filaments provides information on the appearance and macromolecular assembly of these filaments, and finds some notable structural differences from other elements of the cytoskeleton.
The nuclear lamina is a fundamental constituent of metazoan nuclei. It is composed mainly of lamins, which are intermediate filament proteins that assemble into a filamentous meshwork, bridging the nuclear envelope and chromatin
1
,
2
,
3
,
4
. Besides providing structural stability to the nucleus
5
,
6
, the lamina is involved in many nuclear activities, including chromatin organization, transcription and replication
7
,
8
,
9
,
10
. However, the structural organization of the nuclear lamina is poorly understood. Here we use cryo-electron tomography to obtain a detailed view of the organization of the lamin meshwork within the lamina. Data analysis of individual lamin filaments resolves a globular-decorated fibre appearance and shows that A- and B-type lamins assemble into tetrameric filaments of 3.5 nm thickness. Thus, lamins exhibit a structure that is remarkably different from the other canonical cytoskeletal elements. Our findings define the architecture of the nuclear lamin meshworks at molecular resolution, providing insights into their role in scaffolding the nuclear lamina.
Journal Article
Renovating Value
HGTV has perfected stories about creating and capturing value in the housing market.But according to Robert Goldman, this lifestyle network's beloved flagship programs, Flip or Flop, Property Brothers, and Fixer Upper-- where people revitalize modern spaces and reinvent property values--offer \"fairy tales\" in the wake of the 2008 economic crisis.
eBook
High stretchability, strength, and toughness of living cells enabled by hyperelastic vimentin intermediate filaments
In many developmental and pathological processes, including cellular migration during normal development and invasion in cancer metastasis, cells are required to withstand severe deformations. The structural integrity of eukaryotic cells under small deformations has been known to depend on the cytoskeleton including actin filaments (F-actin), microtubules (MT), and intermediate filaments (IFs). However, it remains unclear how cells resist severe deformations since both F-actin and microtubules yield or disassemble under moderate strains. Using vimentin containing IFs (VIFs) as a model for studying the large family of IF proteins, we demonstrate that they dominate cytoplasmic mechanics and maintain cell viability at large deformations. Our results show that cytoskeletal VIFs form a stretchable, hyperelastic network in living cells. This network works synergistically with other cytoplasmic components, substantially enhancing the strength, stretchability, resilience, and toughness of cells. Moreover, we find the hyperelastic VIF network, together with other quickly recoverable cytoskeletal components, forms a mechanically robust structure which can mechanically recover after damage.
Journal Article
A Non–D2-Receptor-Binding Drug for the Treatment of Schizophrenia
In a randomized trial involving schizophrenic patients with acute psychosis, a new oral drug that does not have a dopamine D2-receptor–binding mechanism of action led to a greater reduction in the severity of overall symptoms than placebo over 4 weeks. The incidence of extrapyramidal symptoms was 3% with the new drug, a finding similar to that with placebo.
Journal Article
Neutrophil-induced genomic instability impedes resolution of inflammation and wound healing
Neutrophil (PMN) infiltration of the intestinal mucosa is a hallmark of tissue injury associated with inflammatory bowel diseases (IBDs). The pathological effects of PMNs are largely attributed to the release of soluble mediators and reactive oxygen species (ROS). We identified what we believe is a new, ROS-independent mechanism whereby activated tissue-infiltrating PMNs release microparticles armed with proinflammatory microRNAs (miR-23a and miR-155). Using IBD clinical samples, and in vitro and in vivo injury models, we show that PMN-derived miR-23a and miR-155 promote accumulation of double-strand breaks (DSBs) by inducing lamin B1-dependent replication fork collapse and inhibition of homologous recombination (HR) by targeting HR-regulator RAD51. DSB accumulation in injured epithelium led to impaired colonic healing and genomic instability. Targeted inhibition of miR-23a and miR-155 in cultured intestinal epithelial cells and in acutely injured mucosa decreased the detrimental effects of PMNs and enhanced tissue healing responses, suggesting that this approach can be used in therapies aimed at resolution of inflammation, in wound healing, and potentially to prevent neoplasia.
Journal Article
Nuclear lamin isoforms differentially contribute to LINC complex-dependent nucleocytoskeletal coupling and whole-cell mechanics
The ability of a cell to regulate its mechanical properties is central to its function. Emerging evidence suggests that interactions between the cell nucleus and cytoskeleton influence cell mechanics through poorly understood mechanisms. Here we conduct quantitative confocal imaging to show that the loss of A-type lamins tends to increase nuclear and cellular volume while the loss of B-type lamins behaves in the opposite manner. We use fluorescence recovery after photobleaching, atomic force microscopy, optical tweezer microrheology, and traction force microscopy to demonstrate that A-type lamins engage with both F-actin and vimentin intermediate filaments (VIFs) through the linker of nucleoskeleton and cytoskeleton (LINC) complexes to modulate cortical and cytoplasmic stiffness as well as cellular contractility in mouse embryonic fibroblasts (MEFs). In contrast, we show that B-type lamins predominantly interact with VIFs through LINC complexes to regulate cytoplasmic stiffness and contractility. We then propose a physical model mediated by the lamin–LINC complex that explains these distinct mechanical phenotypes (mechanophenotypes). To verify this model, we use dominant negative constructs and RNA interference to disrupt the LINC complexes that facilitate the interaction of the nucleus with the F-actin and VIF cytoskeletons and show that the loss of these elements results in mechanophenotypes like those observed in MEFs that lack A- or B-type lamin isoforms. Finally, we demonstrate that the loss of each lamin isoform softens the cell nucleus and enhances constricted cell migration but in turn increases migration-induced DNA damage. Together, our findings uncover distinctive roles for each of the four major lamin isoforms in maintaining nucleocytoskeletal interactions and cellular mechanics.
Journal Article
