Analayzing power of the 12C(d,p) and 12C(d,n) reaction

Drenckhahn, W.; Feigel, A.; Finckh, E.; Gademann, G.; Rüskamp, K.; Wangler, M.; Zeml, L.

doi:10.1063/1.32622

Cited by 4 publications

(9 citation statements)

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“…(3);F igure 4A], we obtaineda na ctivation energy of E a = (56 AE 4) kJ mol À1 ( % 23 k B T)f or the actin association at the pointed end and in diluted buffer.D renckhahn and Pollard measured E a = (36 AE 6) kJ mol À1 for filamente longation at both ends. [45] These data indicatet hat as lightly higher activation energy is neededf or initial binding and for the G-to-F transformationa tt he pointed end compared with the barbed end. This would be consistentw ith ar ecently suggested modelt hat the G-to-F-transition is induced by ap ulling movement of the d-loop upon its own docking to the hydrophobic cleft of the neighboring subunit, which differs at both ends.…”

Section: Resultsmentioning

confidence: 87%

“…[17,21,43,44] In vitro, the elongation of actin has been previously shown to be weakly dependent on the viscosity,a nd thus not diffusion limiteda tt he pointede nd, but at the barbed end. [45] In contrast to synthetic and often inert polymers, globular proteins exhibit ac hemically heterogeneous surface, allowing local intermolecular interactions such as electrostatic interactions, hydrogenb onding, or attraction mediated by the hydrophobic effect. Hence, to mimic such cellular environments in vitro, we used the proteins bovine serum albumin(BSA) andlysozymea sp rotein crowding agents.…”

Section: Resultsmentioning

confidence: 99%

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Kinetic Insights into the Elongation Reaction of Actin Filaments as a Function of Temperature, Pressure, and Macromolecular Crowding

Gao

Winter

2015

ChemPhysChem

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Actin polymerization is an essential process in eukaryotic cells that provides a driving force for motility and mechanical resistance for cell shape. By using preformed gelsolin-actin nuclei and applying stopped-flow methodology, we quantitatively studied the elongation kinetics of actin filaments as a function of temperature and pressure in the presence of synthetic and protein crowding agents. We show that the association of actin monomers to the pointed end of double-stranded helical actin filaments (F-actin) proceeds via a transition state that requires an activation energy of 56 kJ mol(-1) for conformational and hydration rearrangements, but exhibits a negligible activation volume, pointing to a compact transition state that is devoid of packing defects. Macromolecular crowding causes acceleration of the F-actin elongation rate and counteracts the deteriorating effect of pressure. The results shed new light on the combined effect of these parameters on the polymerization process of actin, and help us understand the temperature and pressure sensitivity of actin polymerization under extreme conditions.

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Section: Resultsmentioning

confidence: 87%

Section: Resultsmentioning

confidence: 99%

Kinetic Insights into the Elongation Reaction of Actin Filaments as a Function of Temperature, Pressure, and Macromolecular Crowding

Gao

Winter

2015

ChemPhysChem

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“…F-actin was, again, concentrated in the mesangial regions but with marked As in previous studies, we again demonstrated that podocytes possess abundant vimentin-containing interalterations in its disposition. As compared with agemediate filaments that coalesce as dense bundles into matched controls, F-actin-containing fibers in diabetic the cells' processes [36,[40][41][42]. Following the primary glomeruli were virtually absent or ostensibly disorgaand secondary processes, vimentin bundles from the same nized (Fig.…”

Section: Resultsmentioning

confidence: 99%

F-actin fiber distribution in glomerular cells: Structural and functional implications

Cortés

Méndez

Riser

et al. 2000

Kidney International

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Mesangial cells, but not podocytes, contain a cytoskeleton capable of contraction that is disorganized in long-term diabetes. Together with previous observations, the distribution of this cytoskeleton suggests that mesangial cell contraction may be involved in the redistribution of glomerular capillary blood flow, but not substantially in the modulation of glomerular distention. Disorganization of stress fibers may be a cause of hyperfiltration in diabetes.

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“…Furthermore, it has become clear that the slit diaphragm, transmembrane receptors for components of glomerular basement membrane, and integral membrane proteins on the apical surface of the podocyte such as podocalyxin are coupled to the actin cytoskeleton through cross-linking proteins, and that these connections subserve signaling between the extracellular environment and the podocyte [16]. While the cell body and primary processes of the podocyte contain all three types of cytoskeletal elements [17], the foot process is reported to contain only the microfilament [18]. The elements of intermediate filaments (vimentin), microtubules (a-and b-tubulin), and microfilaments (b-actin, and myosin) were all identified in this study.…”

Section: Discussionmentioning

confidence: 99%

Two‐dimensional electrophoretic profiling of normal human kidney glomerulus proteome and construction of an extensible markup language (XML)‐based database

et al. 2005

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To contribute to physiology and pathophysiology of the glomerulus of human kidney, we have launched a proteomic study of human glomerulus, and compiled a profile of proteins expressed in the glomerulus of normal human kidney by two-dimensional gel electrophoresis (2-DE) and identification with matrix-assisted laser desorption/ionization-time of flight mass spectrometry (MALDI-TOF MS) and/or liquid chromatography-tandem mass spectrometry (LC-MS/MS). Kidney cortices with normal appearance were obtained from patients under surgical nephrectomy due to renal tumor, and glomeruli were highly purified by a standard sieving method followed by picking-up under a phase-contrast microscope. The glomerular proteins were separated by 2-DE with 24 cm immobilized pH gradient strips in the 3-10 range in the first dimension and 26 x 20 cm sodium dodecyl sulfate polyacrylamide electrophoresis gels of 12.5% in the second dimension. Gels were silver-stained, and valid spots were processed for identification through an integrated robotic system that consisted of a spot picker, an in-gel digester, and a MALDI-TOF MS and / or a LC-MS/MS. From 2-DE gel images of glomeruli of four subjects with no apparent pathologic manifestations, a synthetic gel image of normal glomerular proteins was created. The synthetic gel image contained 1713 valid spots, of which 1559 spots were commonly observed in the respective 2-DE gels. Among the 1559 spots, 347 protein spots, representing 212 proteins, have so far been identified, and used for the construction of an extensible markup language (XML)-based database. The database is deposited on a web site (http://www.sw.nec.co.jp/bio/rd/hgldb/index.html) in a form accessible to researchers to contribute to proteomic studies of human glomerulus in health and disease.

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Analayzing power of the 12C(d,p) and 12C(d,n) reaction

Cited by 4 publications

References 0 publications

Kinetic Insights into the Elongation Reaction of Actin Filaments as a Function of Temperature, Pressure, and Macromolecular Crowding

Kinetic Insights into the Elongation Reaction of Actin Filaments as a Function of Temperature, Pressure, and Macromolecular Crowding

F-actin fiber distribution in glomerular cells: Structural and functional implications

Two‐dimensional electrophoretic profiling of normal human kidney glomerulus proteome and construction of an extensible markup language (XML)‐based database

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