Howard Schulman

Affiliations: 
Stanford University, Palo Alto, CA 
Area:
calcium signaling
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"Howard Schulman"
Mean distance: 13.13 (cluster 11)
 
SNBCP

Children

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Leslie C. Griffith grad student Stanford
Phillis Hanson grad student Stanford
E Kevin Heist grad student Stanford
Mollie K. Meffert grad student 1990-1997 Stanford
Mark C. Bieda grad student 2000 Stanford
David N. Lieberman grad student 2000 Stanford
Vikas Duvvuri grad student 2001 Stanford
Jennifer Tsui grad student 2000-2005 Stanford
Paul De Koninck post-doc Rockefeller
K Ulrich Ulli Bayer post-doc 1996-2002 Stanford
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Publications

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Chen X, Cai Q, Zhou J, et al. (2023) CaMKII autophosphorylation but not downstream kinase activity is required for synaptic memory. Biorxiv : the Preprint Server For Biology
Tullis JE, Larsen ME, Rumian NL, et al. (2023) LTP induction by structural rather than enzymatic functions of CaMKII. Nature
Bhattacharyya M, Lee YK, Muratcioglu S, et al. (2020) Flexible linkers in CaMKII control the balance between activating and inhibitory autophosphorylation. Elife. 9
Bayer KU, Schulman H. (2019) CaM Kinase: Still Inspiring at 40. Neuron. 103: 380-394
Pandini A, Schulman H, Khan S. (2019) Conformational coupling by trans-phosphorylation in calcium calmodulin dependent kinase II. Plos Computational Biology. 15: e1006796
Neef S, Steffens A, Pellicena P, et al. (2017) Improvement of cardiomyocyte function by a novel pyrimidine-based CaMKII-inhibitor. Journal of Molecular and Cellular Cardiology
Bhattacharyya M, Stratton MM, Going CC, et al. (2016) Molecular mechanism of activation-triggered subunit exchange in Ca(2+)/calmodulin-dependent protein kinase II. Elife. 5
Bhattacharyya M, Stratton MM, Going CC, et al. (2016) Author response: Molecular mechanism of activation-triggered subunit exchange in Ca2+/calmodulin-dependent protein kinase II Elife
Pellicena P, Schulman H. (2014) CaMKII inhibitors: from research tools to therapeutic agents. Frontiers in Pharmacology. 5: 21
Stratton M, Lee IH, Bhattacharyya M, et al. (2014) Correction: Activation-triggered subunit exchange between CaMKII holoenzymes facilitates the spread of kinase activity. Elife. 3: e02490
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