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Article ; Online: You can't keep a bad idea down: Dark history, death, and potential rebirth of eugenics.

Liscum, Mannie / Garcia, Michael L

Anatomical record (Hoboken, N.J. : 2007)

2021 Volume 305, Issue 4, Page(s) 902–937

Abstract: Be careful what you wish for": This adage guides both how this project came to life, and how the topic covered in this review continues to unfold. What began as talks between two friends on shared interests in military history led to a 4-year discussion ...

Abstract	"Be careful what you wish for": This adage guides both how this project came to life, and how the topic covered in this review continues to unfold. What began as talks between two friends on shared interests in military history led to a 4-year discussion about how our science curriculum does little to introduce our students to societal and ethical impacts of the science they are taught. What emerged was a curricular idea centered on how "good intentions" of some were developed and twisted by others to result in disastrous consequences of state-sanctioned eugenics. In this article, we take the reader (as we did our students) through the long and soiled history of eugenic thought, from its genesis to the present. Though our focus is on European and American eugenics, we will show how the interfaces and interactions between science and society have evolved over time but have remained ever constant. Four critical 'case studies' will also be employed here for deep, thoughtful exploration on a particular eugenic issue. The goal of the review, as it is with our course, is not to paint humanity with a single evil brush. Instead, our ambition is to introduce our students/readers to the potential for harm through the misapplication and misappropriation of science and scientific technology, and to provide them with the tools to ask the appropriate questions of their scientists, physicians, and politicians.
MeSH term(s)	Eugenics ; History, 20th Century ; Humans ; United States
Language	English
Publishing date	2021-12-17
Publishing country	United States
Document type	Historical Article ; Journal Article ; Review
ZDB-ID	2269667-2
ISSN	1932-8494 ; 1932-8486
ISSN (online)	1932-8494
ISSN	1932-8486
DOI	10.1002/ar.24849
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Article ; Online: A Method for Investigating the Pseudomonas syringae-Arabidopsis thaliana Pathosystem Under Various Light Environments.

Leuchtman, Daniel L / Shumate, Anthony D / Gassmann, Walter / Liscum, Emmanuel

Methods in molecular biology (Clifton, N.J.)

2019 Volume 1991, Page(s) 107–113

Abstract: Arabidopsis thaliana and Pseudomonas syringae pv. tomato DC3000 (Pst DC3000) comprise an effective model pathosystem for resolving mechanisms behind numerous aspects of plant innate immunity. Following the characterization of key molecular components ... ...

Abstract	Arabidopsis thaliana and Pseudomonas syringae pv. tomato DC3000 (Pst DC3000) comprise an effective model pathosystem for resolving mechanisms behind numerous aspects of plant innate immunity. Following the characterization of key molecular components over the past decades, we may begin investigating defense signaling under various environmental conditions to gain a more holistic understanding of the underlying processes. As a critical regulator of growth and development, exploration into the influence of light on pathogenesis is a logical step toward a systems-level understanding of innate immunity. Based on methods described previously, here we describe a method for investigating plant immune responses under various light environments.
MeSH term(s)	Arabidopsis/immunology ; Arabidopsis/microbiology ; Arabidopsis/radiation effects ; Immunity, Innate/immunology ; Immunity, Innate/radiation effects ; Light ; Plant Diseases/immunology ; Plant Diseases/microbiology ; Plant Leaves/immunology ; Plant Leaves/microbiology ; Plant Leaves/radiation effects ; Pseudomonas syringae/pathogenicity ; Pseudomonas syringae/radiation effects
Language	English
Publishing date	2019-04-30
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-9458-8_12
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Article ; Online: A role for NPC1 and NPC2 in intestinal cholesterol absorption--the hypothesis gutted.

Liscum, Laura

The Biochemical journal

2007 Volume 408, Issue 1, Page(s) e1–3

Abstract: Dietary and biliary cholesterol are taken up by intestinal epithelial cells and transported to the endoplasmic reticulum. At the endoplasmic reticulum, cholesterol is esterified, packaged into chylomicrons and secreted into the lymph for delivery to the ... ...

Abstract	Dietary and biliary cholesterol are taken up by intestinal epithelial cells and transported to the endoplasmic reticulum. At the endoplasmic reticulum, cholesterol is esterified, packaged into chylomicrons and secreted into the lymph for delivery to the bloodstream. NPC1L1 (Niemann-Pick C1-like 1) is a protein on the enterocyte brush-border membrane that facilitates cholesterol absorption. Cholesterol's itinerary as it moves to the endoplasmic reticulum is unknown, as is the identity of any cellular proteins that facilitate the movement. Two proteins that play an important role in intracellular cholesterol transport and could potentially influence NPC1L1-mediated cholesterol uptake are NPC1 and NPC2 (Niemann-Pick type C disease proteins 1 and 2). In this issue of the Biochemical Journal, Dixit and colleagues show that the absence or presence of NPC1 and NPC2 has no effect on intestinal cholesterol absorption in the mouse. Thus neither protein fills the gap in our knowledge of intra-enterocyte cholesterol transport. Furthermore, the NPC1/NPC2 pathway would not be a good target for limiting the uptake of dietary cholesterol.
MeSH term(s)	Animals ; Biomarkers ; Carrier Proteins/metabolism ; Cholesterol/metabolism ; Intestinal Absorption ; Membrane Glycoproteins/metabolism ; Niemann-Pick Diseases/metabolism
Chemical Substances	Biomarkers ; Carrier Proteins ; Membrane Glycoproteins ; Cholesterol (97C5T2UQ7J)
Language	English
Publishing date	2007-10-23
Publishing country	England
Document type	Comment ; Journal Article
ZDB-ID	2969-5
ISSN	1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
ISSN (online)	1470-8728
ISSN	0006-2936 ; 0306-3275 ; 0264-6021
DOI	10.1042/BJ20071340
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Article: Niemann-Pick type C mutations cause lipid traffic jam.

Liscum, L

Traffic (Copenhagen, Denmark)

2001 Volume 1, Issue 3, Page(s) 218–225

Abstract: The Niemann-Pick C protein (NPC1) is required for cholesterol transport from late endosomes and lysosomes to other cellular membranes. Mutations in NPC1 cause lysosomal lipid storage and progressive neurological degeneration. Cloning of the NPC1 gene has ...

Abstract	The Niemann-Pick C protein (NPC1) is required for cholesterol transport from late endosomes and lysosomes to other cellular membranes. Mutations in NPC1 cause lysosomal lipid storage and progressive neurological degeneration. Cloning of the NPC1 gene has given us tools with which to investigate the function of this putative cholesterol transporter. Here, we discuss recent studies indicating that NPC1 is not a cholesterol-specific transport molecule. Instead, NPC1 appears to be required for the vesicular shuttling of both lipids and fluid-phase constituents from multivesicular late endosomes to destinations such as the trans-Golgi network.
MeSH term(s)	Animals ; Biological Transport/genetics ; CHO Cells/metabolism ; Carrier Proteins/chemistry ; Carrier Proteins/genetics ; Carrier Proteins/physiology ; Cholesterol/metabolism ; Cholesterol, LDL/metabolism ; Cricetinae ; Cricetulus ; Endoplasmic Reticulum/metabolism ; Endosomes/metabolism ; Fibroblasts/metabolism ; Glycoproteins/chemistry ; Glycoproteins/genetics ; Glycoproteins/physiology ; Humans ; Intracellular Membranes/metabolism ; Lysosomes/metabolism ; Membrane Glycoproteins/chemistry ; Membrane Glycoproteins/genetics ; Membrane Glycoproteins/physiology ; Membrane Lipids/metabolism ; Models, Biological ; Models, Molecular ; Niemann-Pick Diseases/genetics ; Niemann-Pick Diseases/metabolism ; Protein Conformation ; Protein Structure, Tertiary ; Sphingolipids/metabolism ; Transport Vesicles/metabolism
Chemical Substances	Carrier Proteins ; Cholesterol, LDL ; Glycoproteins ; Membrane Glycoproteins ; Membrane Lipids ; NPC1 protein, human ; Sphingolipids ; Cholesterol (97C5T2UQ7J)
Language	English
Publishing date	2001-01-31
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	1483852-7
ISSN	1600-0854 ; 1398-9219
ISSN (online)	1600-0854
ISSN	1398-9219
DOI	10.1034/j.1600-0854.2000.010304.x
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Article ; Online: LDL receptor related protein 1 requires the I

Mills, Joslyn / Hanada, Toshihiko / Hase, Yoichi / Liscum, Laura / Chishti, Athar H

Biochimica et biophysica acta. Molecular cell research

2019 Volume 1866, Issue 12, Page(s) 118552

Abstract: KIF13B, a kinesin-3 family motor, was originally identified as GAKIN due to its biochemical interaction with human homolog of Drosophila discs-large tumor suppressor (hDLG1). Unlike its homolog KIF13A, KIF13B contains a carboxyl-terminal CAP-Gly domain. ... ...

Abstract	KIF13B, a kinesin-3 family motor, was originally identified as GAKIN due to its biochemical interaction with human homolog of Drosophila discs-large tumor suppressor (hDLG1). Unlike its homolog KIF13A, KIF13B contains a carboxyl-terminal CAP-Gly domain. To investigate the function of the CAP-Gly domain, we developed a mouse model that expresses a truncated form of KIF13B protein lacking its CAP-Gly domain (KIF13BΔCG), whereas a second mouse model lacks the full-length KIF13A. Here we show that the KIF13BΔCG mice exhibit relatively higher serum cholesterol consistent with the reduced uptake of [
MeSH term(s)	Animals ; Cells, Cultured ; Discs Large Homolog 1 Protein/metabolism ; Kinesin/metabolism ; Low Density Lipoprotein Receptor-Related Protein-1/metabolism ; Membrane Proteins/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout
Chemical Substances	Discs Large Homolog 1 Protein ; Dlg1 protein, mouse ; Low Density Lipoprotein Receptor-Related Protein-1 ; Membrane Proteins ; KIF13b protein, mouse (EC 3.6.1.-) ; Kinesin (EC 3.6.4.4)
Language	English
Publishing date	2019-09-02
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamcr.2019.118552
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Article ; Online: Peer Review Practices for Evaluating Biomedical Research Grants: A Scientific Statement From the American Heart Association.

Liaw, Lucy / Freedman, Jane E / Becker, Lance B / Mehta, Nehal N / Liscum, Laura

Circulation research

2017 Volume 121, Issue 4, Page(s) e9–e19

Abstract: The biomedical research enterprise depends on the fair and objective peer review of research grants, leading to the distribution of resources through efficient and robust competitive methods. In the United States, federal funding agencies and foundations ...

Abstract	The biomedical research enterprise depends on the fair and objective peer review of research grants, leading to the distribution of resources through efficient and robust competitive methods. In the United States, federal funding agencies and foundations collectively distribute billions of dollars annually to support biomedical research. For the American Heart Association, a Peer Review Subcommittee is charged with establishing the highest standards for peer review. This scientific statement reviews the current literature on peer review practices, describes the current American Heart Association peer review process and those of other agencies, analyzes the strengths and weaknesses of American Heart Association peer review practices, and recommends best practices for the future.
MeSH term(s)	American Heart Association ; Biomedical Research/economics ; Biomedical Research/methods ; Biomedical Research/standards ; Humans ; Peer Review/methods ; Peer Review/standards ; Research Support as Topic/economics ; Research Support as Topic/methods ; Research Support as Topic/standards ; United States
Language	English
Publishing date	2017-08-04
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	80100-8
ISSN	1524-4571 ; 0009-7330 ; 0931-6876
ISSN (online)	1524-4571
ISSN	0009-7330 ; 0931-6876
DOI	10.1161/RES.0000000000000158
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Article: Pharmacological inhibition of the intracellular transport of low-density lipoprotein-derived cholesterol in Chinese hamster ovary cells.

Liscum, L

Biochimica et biophysica acta

1990 Volume 1045, Issue 1, Page(s) 40–48

Abstract: Mammalian cells, cultured in the presence of serum lipoproteins, acquire cholesterol necessary for growth from the uptake and lysosomal hydrolysis of low-density lipoproteins (LDL). The mechanism(s) of intracellular transport of LDL-derived cholesterol ... ...

Abstract	Mammalian cells, cultured in the presence of serum lipoproteins, acquire cholesterol necessary for growth from the uptake and lysosomal hydrolysis of low-density lipoproteins (LDL). The mechanism(s) of intracellular transport of LDL-derived cholesterol from lysosomes to other cellular sites is unknown. In this study, various pharmacological agents were assessed for their ability to inhibit the movement of LDL-cholesterol from lysosomes to the plasma membrane. The only pharmacological agent tested in these experiments that specifically inhibited LDL-cholesterol movement was U18666A. Ketoconazole impaired the intracellular transport of LDL-cholesterol; however, ketoconazole also had a general effect on cholesterol movement, since it impeded the desorption of endogenously synthesized cholesterol into the medium. Other drugs that affected cholesterol movement appeared to be nonspecific. Cholesterol transport from lysosomes to plasma membranes was not significantly altered by agents that affect lysosomal function or cytoskeletal organization, as well as energy poisons and cycloheximide.
MeSH term(s)	Androstenes/pharmacology ; Animals ; Anticholesteremic Agents/pharmacology ; Cattle ; Cell Line ; Cholesterol/metabolism ; Cholesterol, LDL/blood ; Cholesterol, LDL/isolation & purification ; Cholesterol, LDL/metabolism ; Cricetinae ; Cricetulus ; Female ; Ketoconazole/pharmacology ; Kinetics ; Monensin/pharmacology ; Ovary
Chemical Substances	Androstenes ; Anticholesteremic Agents ; Cholesterol, LDL ; 3-beta-(2-(diethylamino)ethoxy)androst-5-en-17-one (3039-71-2) ; Monensin (906O0YJ6ZP) ; Cholesterol (97C5T2UQ7J) ; Ketoconazole (R9400W927I)
Language	English
Publishing date	1990-06-28
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/0005-2760(90)90201-8
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Article: Intracellular trafficking of Niemann-Pick C proteins 1 and 2: obligate components of subcellular lipid transport.

Liscum, Laura / Sturley, Stephen L

Biochimica et biophysica acta

2004 Volume 1685, Issue 1-3, Page(s) 22–27

Abstract: Niemann-Pick C 1 (NPC1) is a large integral membrane glycoprotein that resides in late endosomes, whereas NPC2 is a small soluble protein found in the lumen of lysosomes. Mutations in either NPC1 or NPC2 result in aberrant lipid transport from endocytic ... ...

Abstract	Niemann-Pick C 1 (NPC1) is a large integral membrane glycoprotein that resides in late endosomes, whereas NPC2 is a small soluble protein found in the lumen of lysosomes. Mutations in either NPC1 or NPC2 result in aberrant lipid transport from endocytic compartments, which results in lysosomal storage of a complex mixture of lipids, primarily cholesterol and glycosphingolipids. What are the biological functions of the NPC1 and NPC2 proteins? Here we review what is known about the intracellular itinerary of these two proteins as they facilitate lipid transport. We propose that the intracellular trafficking patterns of these proteins will provide clues about their function.
MeSH term(s)	Animals ; Carrier Proteins/metabolism ; Endosomes/metabolism ; Glycoproteins/metabolism ; Humans ; Lipid Metabolism ; Lysosomes/metabolism ; Membrane Glycoproteins/metabolism ; Models, Biological ; Niemann-Pick Diseases/metabolism ; Protein Transport
Chemical Substances	Carrier Proteins ; Glycoproteins ; Membrane Glycoproteins ; NPC1 protein, human ; NPC2 protein, human
Language	English
Publishing date	2004-10-11
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbalip.2004.08.008
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Article ; Online: Phototropism: growing towards an understanding of plant movement.

Liscum, Emmanuel / Askinosie, Scott K / Leuchtman, Daniel L / Morrow, Johanna / Willenburg, Kyle T / Coats, Diana Roberts

The Plant cell

2014 Volume 26, Issue 1, Page(s) 38–55

Abstract: Phototropism, or the differential cell elongation exhibited by a plant organ in response to directional blue light, provides the plant with a means to optimize photosynthetic light capture in the aerial portion and water and nutrient acquisition in the ... ...

Abstract	Phototropism, or the differential cell elongation exhibited by a plant organ in response to directional blue light, provides the plant with a means to optimize photosynthetic light capture in the aerial portion and water and nutrient acquisition in the roots. Tremendous advances have been made in our understanding of the molecular, biochemical, and cellular bases of phototropism in recent years. Six photoreceptors and their associated signaling pathways have been linked to phototropic responses under various conditions. Primary detection of directional light occurs at the plasma membrane, whereas secondary modulatory photoreception occurs in the cytoplasm and nucleus. Intracellular responses to light cues are processed to regulate cell-to-cell movement of auxin to allow establishment of a trans-organ gradient of the hormone. Photosignaling also impinges on the transcriptional regulation response established as a result of changes in local auxin concentrations. Three additional phytohormone signaling pathways have also been shown to influence phototropic responsiveness, and these pathways are influenced by the photoreceptor signaling as well. Here, we will discuss this complex dance of intra- and intercellular responses that are regulated by these many systems to give rise to a rapid and robust adaptation response observed as organ bending.
MeSH term(s)	Biological Transport ; Gene Expression Regulation, Plant ; Indoleacetic Acids/metabolism ; Models, Genetic ; Photosynthesis ; Phototropins/metabolism ; Phototropins/physiology ; Phototropism/physiology ; Phytochrome/metabolism ; Phytochrome/physiology ; Plant Physiological Phenomena ; Plant Proteins/genetics ; Plant Proteins/metabolism ; Plant Proteins/physiology ; Signal Transduction
Chemical Substances	Indoleacetic Acids ; Phototropins ; Plant Proteins ; Phytochrome (11121-56-5)
Language	English
Publishing date	2014-01-30
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	623171-8
ISSN	1532-298X ; 1040-4651
ISSN (online)	1532-298X
ISSN	1040-4651
DOI	10.1105/tpc.113.119727
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Article: Flux of fatty acids through NPC1 lysosomes.

Passeggio, Jessica / Liscum, Laura

The Journal of biological chemistry

2005 Volume 280, Issue 11, Page(s) 10333–10339

Abstract: Niemann-Pick type C (NPC) is an autosomal recessive lipid storage disorder characterized by lysosomal accumulation of cholesterol and gangliosides resulting from a defect in intracellular lipid trafficking. The NPC1 gene encodes a 1278-amino acid ... ...

Abstract	Niemann-Pick type C (NPC) is an autosomal recessive lipid storage disorder characterized by lysosomal accumulation of cholesterol and gangliosides resulting from a defect in intracellular lipid trafficking. The NPC1 gene encodes a 1278-amino acid integral membrane protein involved in the sub-cellular trafficking of lipids. The exact biological function of NPC1 remains unclear. Recent evidence suggests that NPC1 is a eukaryotic member of the RND permease family of transport proteins, which when expressed in bacteria is capable of transporting fatty acids. The goal of this project was to assess the role of NPC1 in the transport of fatty acids in primary human fibroblasts using normal fibroblasts and fibroblasts from patients with three lysosomal storage diseases: NPC, mucolipidosis IV, and Sandhoff disease. If NPC1 is a fatty acid transporter, we expect to find fatty acid accumulation only in NPC fibroblasts. We used three experimental approaches to assess the role of NPC1 as a fatty acid transporter. First, we evaluated the accumulation versus metabolism of low density lipoprotein-derived oleic acid. Second, we assessed the amount of free fatty acid present after growth in lipoprotein-containing media. Third, we assessed the cellular accumulation of acriflavine, a fluorescent substrate for a number of resistance-nodulation-cell division permease transporters. Our results indicate that fatty acid flux through NPC1-deficient lysosomes is normal.
MeSH term(s)	Acriflavine/metabolism ; Acriflavine/pharmacology ; Carrier Proteins/metabolism ; Cells, Cultured ; Cholesterol/metabolism ; Chromatography, Gas ; Dextrans/chemistry ; Fatty Acids/metabolism ; Fibroblasts/metabolism ; Humans ; Intracellular Signaling Peptides and Proteins ; Lipid Metabolism ; Lipoproteins, LDL/chemistry ; Lipoproteins, LDL/metabolism ; Lysosomes/metabolism ; Membrane Glycoproteins/metabolism ; Niemann-Pick Diseases/metabolism ; Oleic Acid/metabolism ; Protein Transport
Chemical Substances	Carrier Proteins ; Dextrans ; Fatty Acids ; Intracellular Signaling Peptides and Proteins ; Lipoproteins, LDL ; Membrane Glycoproteins ; NPC1 protein, human ; Acriflavine (1T3A50395T) ; Oleic Acid (2UMI9U37CP) ; Cholesterol (97C5T2UQ7J)
Language	English
Publishing date	2005-01-04
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M413657200
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