Gas phase derivatization in peptide analysis I: the utility of trimethyl borate in identifying phosphorylation sites

2004 ◽  
Vol 231 (2-3) ◽  
pp. 179-187 ◽  
Author(s):  
Scott Gronert ◽  
Renee Huang ◽  
Kathy H. Li
Keyword(s):  
Gas Phase ◽  
Phosphorylation Sites ◽  
Peptide Analysis ◽  
Trimethyl Borate

Characterization of Phosphorylation Sites in Bovine Rhodopsin Using Modified Gas Phase Sequencing Programs

1994 ◽  
pp. 159-167 ◽  
Author(s):  
Benne F. Parten ◽  
J. Hugh McDowell ◽  
Joseph P. Nawrocki ◽  
Paul A. Hargrave
Keyword(s):  
Gas Phase ◽  
Phosphorylation Sites ◽  
Bovine Rhodopsin

Identification of phosphorylation sites in peptides using a gas-phase sequencer

1988 ◽  
Vol 174 (2) ◽  
pp. 537-547 ◽  
Author(s):  
Yuhuan Wang ◽  
Carol J. Fiol ◽  
Anna A. DePaoli-Roach ◽  
Alexander W. Bell ◽  
Mark A. Hermodson ◽  
...  
Keyword(s):  
Gas Phase ◽  
Phosphorylation Sites

Behaviour of arylalkylamines toward trimethyl borate as a gas-phase reagent

2000 ◽  
Vol 203 (1-3) ◽  
pp. 101-110 ◽  
Author(s):  
Luis E Ramos ◽  
Ana M Cardoso ◽  
A.J.Ferrer Correia ◽  
Nico M.M Nibbering
Keyword(s):  
Gas Phase ◽  
Trimethyl Borate

Residual Gas Reactions in the Electron Microscope: I. Qualitative Observations on the Water Gas Reaction

1968 ◽  
Vol 26 ◽  
pp. 292-293
Author(s):  
Richard E. Hartman ◽  
Roberta S. Hartman ◽  
Peter L. Ramos
Keyword(s):  
Electron Beam ◽  
Electron Microscope ◽  
Gas Phase ◽  
Absolute Temperature ◽  
Residual Gas ◽  
Gas Reactions ◽  
Image Position ◽  
The Right ◽  
Water Gas ◽  
Thinning Rate

The action of water and the electron beam on organic specimens in the electron microscope results in the removal of oxidizable material (primarily hydrogen and carbon) by reactions similar to the water gas reaction .which has the form:The energy required to force the reaction to the right is supplied by the interaction of the electron beam with the specimen.The mass of water striking the specimen is given by:where u = gH2O/cm2 sec, PH2O = partial pressure of water in Torr, & T = absolute temperature of the gas phase. If it is assumed that mass is removed from the specimen by a reaction approximated by (1) and that the specimen is uniformly thinned by the reaction, then the thinning rate in A/ min iswhere x = thickness of the specimen in A, t = time in minutes, & E = efficiency (the fraction of the water striking the specimen which reacts with it).

Integration of Core-Edge Spectroscopy Methods for the Study of Polymers

1996 ◽  
Vol 54 ◽  
pp. 154-155
Author(s):  
E. G. Rightor
Keyword(s):  
Excited State ◽  
Polymer Blends ◽  
Gas Phase ◽  
Spatial Resolution ◽  
High Spatial Resolution ◽  
Electronic States ◽  
Core Electron ◽  
Bulk Solids ◽  
Development Application

Core edge spectroscopy methods are versatile tools for investigating a wide variety of materials. They can be used to probe the electronic states of materials in bulk solids, on surfaces, or in the gas phase. This family of methods involves promoting an inner shell (core) electron to an excited state and recording either the primary excitation or secondary decay of the excited state. The techniques are complimentary and have different strengths and limitations for studying challenging aspects of materials. The need to identify components in polymers or polymer blends at high spatial resolution has driven development, application, and integration of results from several of these methods.

Specificity determinants of phosphoprotein phosphatases controlling kinetochore functions

2020 ◽  
Vol 64 (2) ◽  
pp. 325-336 ◽  
Author(s):  
Dimitriya H. Garvanska ◽  
Jakob Nilsson
Keyword(s):  
Spindle Assembly Checkpoint ◽  
Activity Level ◽  
Phosphorylation Sites ◽  
Binding Affinities ◽  
Mitotic Kinases ◽  
Anaphase Onset ◽  
Phosphoprotein Phosphatases ◽  
Linear Motifs ◽  
Temporal And Spatial ◽  
Kinetochore Function

Abstract Kinetochores are instrumental for accurate chromosome segregation by binding to microtubules in order to move chromosomes and by delaying anaphase onset through the spindle assembly checkpoint (SAC). Dynamic phosphorylation of kinetochore components is key to control these activities and is tightly regulated by temporal and spatial recruitment of kinases and phosphoprotein phosphatases (PPPs). Here we focus on PP1, PP2A-B56 and PP2A-B55, three PPPs that are important regulators of mitosis. Despite the fact that these PPPs share a very similar active site, they target unique ser/thr phosphorylation sites to control kinetochore function. Specificity is in part achieved by PPPs binding to short linear motifs (SLiMs) that guide their substrate specificity. SLiMs bind to conserved pockets on PPPs and are degenerate in nature, giving rise to a range of binding affinities. These SLiMs control the assembly of numerous substrate specifying complexes and their position and binding strength allow PPPs to target specific phosphorylation sites. In addition, the activity of PPPs is regulated by mitotic kinases and inhibitors, either directly at the activity level or through affecting PPP–SLiM interactions. Here, we discuss recent progress in understanding the regulation of PPP specificity and activity and how this controls kinetochore biology.

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