Search Results - "CAPLOW, Michael"

Glutathionylation at Cys-111 Induces Dissociation of Wild Type and FALS Mutant SOD1 Dimers by Redler, Rachel L, Wilcox, Kyle C, Proctor, Elizabeth A, Fee, Lanette, Caplow, Michael, Dokholyan, Nikolay V

“…Mutation of the ubiquitous cytosolic enzyme Cu/Zn superoxide dismutase (SOD1) is hypothesized to cause familial amyotrophic lateral sclerosis (FALS) through…”
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Ubiquitin editing enzyme UCH L1 and microtubule dynamics: Implication in mitosis by Bheda, Anjali, Gullapalli, Anuradha, Caplow, Michael, Pagano, Joseph S., Shackelford, Julia

“…Microtubules are essential components of the cytoskeleton and are involved in many aspects of cell responses including cell division, migration, and…”
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The Rate and Equilibrium Constants for a Multistep Reaction Sequence for the Aggregation of Superoxide Dismutase in Amyotrophic Lateral Sclerosis by Khare, Sagar D., Caplow, Michael, Dokholyan, Nikolay V., Wolfenden, Richard V.

“…Mutation-induced aggregation of the dimeric enzyme Cu, Zn superoxide dismutase 1 (SOD1) has been implicated in the familial form of the disease amyotrophic…”
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Conservation of Structure and Protein-Protein Interactions Mediated by the Secreted Mycobacterial Proteins EsxA, EsxB, and EspA by CALLAHAN, Brian, NGUYEN, Kiet, COLLINS, Alissa, VALDES, Kayla, CAPLOW, Michael, CROSSMAN, David K, STEYN, Adrie J. C, EISELE, Leslie, DERBYSHIRE, Keith M

“…Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley…”
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Modifications of Superoxide Dismutase (SOD1) in Human Erythrocytes by Wilcox, Kyle C., Zhou, Li, Jordon, Joshua K., Huang, Yi, Yu, Yanbao, Redler, Rachel L., Chen, Xian, Caplow, Michael, Dokholyan, Nikolay V.

“…Over 100 mutations in Cu/Zn-superoxide dismutase (SOD1) result in familial amyotrophic lateral sclerosis. Dimer dissociation is the first step in SOD1…”
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Jan Hermans (1933‐2018): Red‐blooded biophysicists study hemoglobin by Carter, Charlie, Wolfenden, Richard, Caplow, Michael, Lentz, Barry, Pielak, Gary, Watenpaugh, Keith, Hu, Hao, Puett, David

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Induction of microtubule catastrophe by formation of tubulin-GDP and apotubulin subunits at microtubule ends by Caplow, Michael, Shanks, John

“…The recent discovery that GTP linked to latex beads binds to microtubule ends suggested that nucleotide interactions at this site may play a role in regulating…”
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Post­translational Modifications Promote Formation of SOD1 Oligomers With Potential Toxicity in ALS by Dokholyan, Nikolay, Redler, Rachel, Proctor, Elizabeth, Ding, Feng, Caplow, Michael

“…Abstract only Mutation of the ubiquitous cytosolic enzyme Cu/Zn superoxide dismutase (SOD1) causes a subset of cases of familial amyotrophic lateral sclerosis…”
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Non-native Soluble Oligomers of Cu/Zn Superoxide Dismutase (SOD1) Contain a Conformational Epitope Linked to Cytotoxicity in Amyotrophic Lateral Sclerosis (ALS) by Redler, Rachel L, Fee, Lanette, Fay, James M, Caplow, Michael, Dokholyan, Nikolay V

“…Soluble misfolded Cu/Zn superoxide dismutase (SOD1) is implicated in motor neuron death in amyotrophic lateral sclerosis (ALS); however, the relative…”
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Modifications of superoxide dismutase (SOD1) in human erythrocytes: a possible role in amyotrophic lateral sclerosis by Wilcox, Kyle C, Zhou, Li, Jordon, Joshua K, Huang, Yi, Yu, Yanbao, Redler, Rachel L, Chen, Xian, Caplow, Michael, Dokholyan, Nikolay V

“…Over 100 mutations in Cu/Zn-superoxide dismutase (SOD1) result in familial amyotrophic lateral sclerosis. Dimer dissociation is the first step in SOD1…”
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Kinetics of carbamate formation and breakdown by Caplow, Michael

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Post-Translational Modifications Promote Formation of SOD1 Oligomers with Potential Toxicity in ALS by Dokholyan, Nikolay V., Redler, Rachel L., Proctor, Elizabeth A., Ding, Feng V., Wilcox, Kyle, Caplow, Michael

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The Kinesin-Related Protein MCAK Is a Microtubule Depolymerase that Forms an ATP-Hydrolyzing Complex at Microtubule Ends by Hunter, Andrew W., Caplow, Michael, Coy, David L., Hancock, William O., Diez, Stefan, Wordeman, Linda, Howard, Jonathon

“…MCAK belongs to the Kin I subfamily of kinesin-related proteins, a unique group of motor proteins that are not motile but instead destabilize microtubules. We…”
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Inhibition of microtubule assembly by phosphorylation of microtubule-associated proteins by Jameson, Larry, Frey, Tom, Zeeberg, Barry, Dalldorf, Fred, Caplow, Michael

“…32P labeling of microtubular protein by endogenous protein kinase activity is shown to result from a net increase in protein-bound phosphate and is not the…”
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FALS mutations in Cu, Zn superoxide dismutase destabilize the dimer and increase dimer dissociation propensity: A large-scale thermodynamic analysis by Khare, Sagar D., Caplow, Michael, Dokholyan, Nikolay V.

“…Mutations in the dimeric enzyme Cu, Zn superoxide dismutase (SOD1) leading to its aggregation are implicated in the toxicity in familial amyotrophic lateral…”
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Dissociation of the tubulin dimer is extremely slow, thermodynamically very unfavorable, and reversible in the absence of an energy source by Caplow, Michael, Fee, Lanette

“…The finding that exchange of tubulin subunits between tubulin dimers (alpha-beta + alpha'beta' <--> alpha'beta + alphabeta') does not occur in the absence of…”
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Evidence that a single monolayer tubulin-GTP cap is both necessary and sufficient to stabilize microtubules by Caplow, M, Shanks, J

“…Evidence that 13 or 14 contiguous tubulin-GTP subunits are sufficient to cap and stabilize a microtubule end and that loss of only one of these subunits…”
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Chymotrypsin catalysis. Evidence for a new intermediate by Caplow, Michael

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Microtubule dynamics by Caplow, M

“…Although compelling evidence has been obtained for heterogeneity in the structure of subunits in microtubules, it has not been possible to prove that this…”
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Concerning the Chemical Nature of Tubulin Subunits That Cap and Stabilize Microtubules by Caplow, Michael, Fee, Lanette

“…There is no definitive evidence on the nature of the cap at microtubule ends that is responsible for dynamic instability behavior. It was, therefore, of…”
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