ArticleProceedings of the National Academy of Sciences of the United States of America1996
Imaging ROMK1 inwardly rectifying ATP-sensitive K+ channel protein using atomic force microscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 60 citations in OpenAlex.
- Article
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- Specific transfection of inflamed brain by macrophages: a new therapeutic strategy for neurodegenerative diseases.PloS one · 2013Article
- Using DNA as a fiducial marker to study SMC complex interactions with the atomic force microscope.Biophysical journal · 2012Article
- Polyelectrolyte complex optimization for macrophage delivery of redox enzyme nanoparticles.Nanomedicine (London, England) · 2011Article
- Single protein molecule mapping with magnetic atomic force microscopy.Biophysical journal · 2010Article
- Single-molecule dynamics of the DNA-EcoRII protein complexes revealed with high-speed atomic force microscopy.Biochemistry · 2009Article
- Molecular mechanism underlying RAG1/RAG2 synaptic complex formation.The Journal of biological chemistry · 2009Article
- Probing cellular microenvironments and tissue remodeling by atomic force microscopy.Pflugers Archiv : European journal of physiology · 2008Review
- Aldosterone and amiloride alter ENaC abundance in vascular endothelium.Pflugers Archiv : European journal of physiology · 2008Article
- Is the vascular endothelium under the control of aldosterone? Facts and hypothesis.Pflugers Archiv : European journal of physiology · 2007Review
- Route of glucocorticoid-induced macromolecules across the nuclear envelope as viewed by atomic force microscopy.Pflugers Archiv : European journal of physiology · 2006Review
- DNA strand arrangement within the SfiI-DNA complex: atomic force microscopy analysis.Biochemistry · 2006Article
- Nuclear envelope: nanoarray responsive to aldosterone.The Journal of membrane biology · 2004Review
- Aldosterone signaling pathway across the nuclear envelope.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Aquaporin 1 regulates GTP-induced rapid gating of water in secretory vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Three-dimensional reconstruction of the recombinant type 3 ryanodine receptor and localization of its amino terminus.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- The polypeptide backbone of recombinant human zona pellucida glycoprotein-3 initiates acrosomal exocytosis in human spermatozoa in vitro.The Biochemical journal · 1998Article
- Structural activity of a cloned potassium channel (ROMK1) monitored with the atomic force microscope: the "molecular-sandwich" technique.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The inwardly rectifying K+ channel ROMK1 has been implicated as being significant in K+ secretion in the distal nephron. ROMK1 has been shown by immunocytochemistry to be expressed in relevant nephron segments. The development of the atomic force microscope has made possible the production of high resolution images of small particles, including a variety of biological macromolecules. Recently, a fusion protein of glutathione S-transferase (GST) and ROMK1 (ROMK1-GST) has been used to produce a polyclonal antibody for immunolocalization of ROMK1. We have used atomic force microscopy to examine ROMK1-GST and the native ROMK1 polypeptide cleaved from GST. Imaging was conducted with the proteins in physiological solutions attached to mica. ROMK1-GST appears in images as a particle composed of two units of similar size. Analyses of images indicate that the two units have volumes of approximately 118 nm3, which is close to the theoretical volume of a globular protein of approximately 65 kDa (the molecular mass of ROMK1-GST). Native GST exists as a dimer, and the images obtained here are consistent with the ROMK1-GST fusion protein's existence as a heterodimer. In experiments on ROMK1 in aqueous solution, single molecules appear to aggregate, but contact to the mica was maintained. Addition of ATP to the solution produced a change in height of the aggregates. This change (which was reversible) suggests that ATP induces a structural change in the ROMK1 protein. The data show that atomic force microscopy is a useful tool for examination of purified protein molecules under near-physiological conditions, and furthermore, that structural alterations in the proteins may be continuously investigated.
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