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Institution

Johns Hopkins University School of Medicine

HealthcareBaltimore, Maryland, United States
About: Johns Hopkins University School of Medicine is a healthcare organization based out in Baltimore, Maryland, United States. It is known for research contribution in the topics: Population & Cancer. The organization has 44277 authors who have published 79222 publications receiving 4788882 citations.


Papers
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Journal ArticleDOI
TL;DR: The molecular characterization of a human homolog of trp, TRPC1, was described, which was 40% identical to Drosophila TRP over most of the protein and lacked the charged residues in the S4 transmembrane region proposed to be required for the voltage sensor in many voltage-gated ion channels.
Abstract: In many vertebrate and invertebrate cells, inositol 1,4,5-trisphospate production induces a biphasic Ca2+ signal. Mobilization of Ca2+ from internal stores drives the initial burst. The second phase, referred to as store-operated Ca2+ entry (formerly capacitative Ca2+ entry), occurs when depletion of intracellular Ca2+ pools activates a non-voltage-sensitive plasma membrane Ca2+ conductance. Despite the prevalence of store-operated Ca2+ entry, no vertebrate channel responsible for store-operated Ca2+ entry has been reported. trp (transient receptor potential), a Drosophila gene required in phototransduction, encodes the only known candidate for such a channel throughout phylogeny. In this report, we describe the molecular characterization of a human homolog of trp, TRPC1. TRPC1 (transient receptor potential channel-related protein 1) was 40% identical to Drosophila TRP over most of the protein and lacked the charged residues in the S4 transmembrane region proposed to be required for the voltage sensor in many voltage-gated ion channels. TRPC1 was expressed at the highest levels in the fetal brain and in the adult heart, brain, testis, and ovaries. Evidence is also presented that TRPC1 represents the archetype of a family of related human proteins.

605 citations

Journal ArticleDOI
TL;DR: Findings suggest that NQO1 may exercise a selective "gatekeeping" role in regulating the proteasomal degradation of specific proteins, thereby broadening the cytoprotective role of N QO1 far beyond its highly effective antioxidant functions.

605 citations

Journal ArticleDOI
TL;DR: It is reported that NOS is stoichiometrically phosphorylated by cAMP dependent protein kinase, protein kinasing C, and calcium/calmodulin-dependent protein kinases, with each kinase phosphorylating a different serine site on NOS.

605 citations

Journal ArticleDOI
01 Nov 1980-Cell
TL;DR: It is shown that after depleting interphase nuclei of histones and other nuclear proteins by treatment with nonionic detergent and high salt, intact loops of DNA can be visualized as a halo surrounding a nuclear skeleton or matrix, suggesting that the replicating DNA loops are motile with respect to their nuclear matrix anchorage sites.

605 citations


Authors

Showing all 44754 results

NameH-indexPapersCitations
Robert Langer2812324326306
Bert Vogelstein247757332094
Solomon H. Snyder2321222200444
Steven A. Rosenberg2181204199262
Kenneth W. Kinzler215640243944
Hagop M. Kantarjian2043708210208
Mark P. Mattson200980138033
Stuart H. Orkin186715112182
Paul G. Richardson1831533155912
Aaron R. Folsom1811118134044
Gonçalo R. Abecasis179595230323
Jie Zhang1784857221720
Daniel R. Weinberger177879128450
David Baker1731226109377
Eliezer Masliah170982127818
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
2023149
2022622
20216,078
20205,107
20194,444
20183,848