NIH VideoCast - Ins and outs of the lysosomal chloride conductance: biophysics to biology for an organellar anion transporter

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Ins and outs of the lysosomal chloride conductance: biophysics to biology for an organellar anion transporter

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Air date:	Friday, January 14, 2011, 12:00:00 PM Time displayed is Eastern Time, Washington DC Local
Views:	Total views: 155 * This only includes stats from October 2011 and forward.
Category:	NIH Director's Seminars
Runtime:	00:56:12
Closed captioning:	Check box to display CC outside of the video Note: You can drag the captioning window around and resize it
Description:	Director's Seminar Series Dr. Mindell received his B.S. degree in Molecular Biophysics and Biochemistry from Yale University in 1986. In 1994 he received his M.D. and Ph.D. degrees from the Albert Einstein College of Medicine, where he worked with Alan Finkelstein studying the structure and function of ion channels formed by diphtheria toxin. After a residency in internal medicine at Brigham and Women's Hospital, Dr. Mindell did post-doctoral work with Chris Miller at Brandeis University; there he focused on structural and functional characterization of ClC-type chloride channels using cryoelectron microscopy and other approaches. Dr. Mindell joined NINDS as an investigator in 2002. His laboratory is using a combination of structural and functional approaches to answer mechanistic questions regarding ClC channels and other anion transport proteins. The Membrane Transport Biophysics Unit focuses on understanding the physical principles governing membrane-protein function. Our major model proteins are members of the ClC family of anion-transport proteins. Use a combination of biochemical and physiological approaches, we seek to understand the protein elements mediating chloride selectivity as well as those involved in regulating the passage of ions across the membrane. Recent developments, including the determination of a high-resolution structure of a bacterial ClC, have allowed us to focus our attention on particular regions of these proteins, which we explore with combinations of biochemistry, genetic mutation, and electrical recordings.

NLM Title:	Ins and outs of the lysosomal chloride conductance : biophysics to biology for an organellar anion transporter / Joseph Mindell.
Author:	Mindell, Joseph. National Institutes of Health (U.S.)
Publisher:
Abstract:	(CIT): Director's Seminar Series Dr. Mindell received his B.S. degree in Molecular Biophysics and Biochemistry from Yale University in 1986. In 1994 he received his M.D. and Ph.D. degrees from the Albert Einstein College of Medicine, where he worked with Alan Finkelstein studying the structure and function of ion channels formed by diphtheria toxin. After a residency in internal medicine at Brigham and Women's Hospital, Dr. Mindell did post-doctoral work with Chris Miller at Brandeis University; there he focused on structural and functional characterization of ClC-type chloride channels using cryoelectron microscopy and other approaches. Dr. Mindell joined NINDS as an investigator in 2002. His laboratory is using a combination of structural and functional approaches to answer mechanistic questions regarding ClC channels and other anion transport proteins. The Membrane Transport Biophysics Unit focuses on understanding the physical principles governing membrane-protein function. Our major model proteins are members of the ClC family of anion-transport proteins. Use a combination of biochemical and physiological approaches, we seek to understand the protein elements mediating chloride selectivity as well as those involved in regulating the passage of ions across the membrane. Recent developments, including the determination of a high-resolution structure of a bacterial ClC, have allowed us to focus our attention on particular regions of these proteins, which we explore with combinations of biochemistry, genetic mutation, and electrical recordings.
Subjects:	Anions Chlorides Lysosomal Storage Diseases Lysosomes--physiology Organelles
Publication Types:	Lecture Webcast
NLM Classification:	QU 350
NLM ID:	101556024
CIT Live ID:	9904
Permanent link:	https://videocast.nih.gov/watch=9904

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