Gleb Shtengel

ORCID: 0000-0001-6830-640X
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About
Contact & Profiles
Research Areas
  • Semiconductor Lasers and Optical Devices
  • Semiconductor Quantum Structures and Devices
  • Photonic and Optical Devices
  • Advanced Fluorescence Microscopy Techniques
  • Advanced Electron Microscopy Techniques and Applications
  • Optical Network Technologies
  • Cellular transport and secretion
  • Photosynthetic Processes and Mechanisms
  • Advanced Photonic Communication Systems
  • Cellular Mechanics and Interactions
  • Spectroscopy and Laser Applications
  • Cancer Immunotherapy and Biomarkers
  • Force Microscopy Techniques and Applications
  • Endoplasmic Reticulum Stress and Disease
  • CAR-T cell therapy research
  • Immune Cell Function and Interaction
  • Solid State Laser Technologies
  • Cell Image Analysis Techniques
  • Lipid Membrane Structure and Behavior
  • Laser Design and Applications
  • Mitochondrial Function and Pathology
  • Skin and Cellular Biology Research
  • Electron and X-Ray Spectroscopy Techniques
  • Photonic Crystal and Fiber Optics
  • Near-Field Optical Microscopy

Janelia Research Campus
2013-2025

Howard Hughes Medical Institute
2013-2025

Helix (United States)
2015

Nokia (United States)
1995-2002

Ioffe Institute
1990-2002

Alcatel Lucent (Germany)
2002

Physico-Technical Institute
2002

Hanover College
2001

Stony Brook University
1998

AT&T (United States)
1995-1996

Understanding molecular-scale architecture of cells requires determination 3D locations specific proteins with accuracy matching their nanometer-length scale. Existing electron and light microscopy techniques are limited either in molecular specificity or resolution. Here, we introduce interferometric photoactivated localization (iPALM), the combination single-photon, simultaneous multiphase interferometry that provides sub-20-nm protein optimal specificity. We demonstrate measurement 25-nm...

10.1073/pnas.0813131106 article EN Proceedings of the National Academy of Sciences 2009-02-07

Within cells, the spatial compartmentalization of thousands distinct proteins serves a multitude diverse biochemical needs. Correlative super-resolution (SR) fluorescence and electron microscopy (EM) can elucidate protein relationships to global ultrastructure, but has suffered from tradeoffs structure preservation, retention, resolution, field view. We developed platform for three-dimensional cryogenic SR focused ion beam-milled block-face EM across entire vitreously frozen cells. The...

10.1126/science.aaz5357 article EN Science 2020-01-17

Far-field optical microscopy using focused light is an important tool in a number of scientific disciplines including chemical, (bio)physical and biomedical research, particularly with respect to the study living cells organisms. Unfortunately, applicability microscope limited, since diffraction imposes limitations on spatial resolution image. Consequently details of, for example, cellular protein distributions, can be visualized only certain extent. Fortunately, recent years have witnessed...

10.1088/0022-3727/48/44/443001 article EN cc-by Journal of Physics D Applied Physics 2015-10-15

A fundamental objective in molecular biology is to understand how DNA organized concert with various proteins, RNA, and biological membranes. Mitochondria maintain express their own (mtDNA), which arranged within structures called nucleoids. Their functions, dimensions, composition, precise locations relative other mitochondrial are poorly defined. Superresolution fluorescence microscopy techniques that exceed the previous limits of imaging small highly compartmentalized mitochondria have...

10.1128/mcb.05694-11 article EN Molecular and Cellular Biology 2011-10-18

Microscopic images of specific proteins in their cellular context yield important insights into biological processes and architecture. The advent superresolution optical microscopy techniques provides the possibility to augment EM with nanometer-resolution fluorescence access precise location ultrastructure. Unfortunately, efforts combine have been stymied by divergent incompatible sample preparation protocols two methods. Here, we describe a protocol that preserves both delicate...

10.1073/pnas.1121558109 article EN Proceedings of the National Academy of Sciences 2012-04-02

Lipid droplets (LDs) are neutral lipid storage organelles that transfer lipids to various including peroxisomes. Here, we show the hereditary spastic paraplegia protein M1 Spastin, a membrane-bound AAA ATPase found on LDs, coordinates fatty acid (FA) trafficking from LDs peroxisomes through two interrelated mechanisms. First, Spastin forms tethering complex with peroxisomal ABCD1 promote LD–peroxisome contact formation. Second, recruits membrane-shaping ESCRT-III proteins IST1 and CHMP1B via...

10.1083/jcb.201902061 article EN cc-by-nc-sa The Journal of Cell Biology 2019-06-21

Cytotoxic T lymphocytes (CTLs) and natural killer cells kill virus-infected tumor through the polarized release of perforin granzymes. Perforin is a pore-forming toxin that creates lesion in plasma membrane target cell which granzymes enter cytosol initiate apoptosis. Endosomal sorting complexes required for transport (ESCRT) proteins are involved repair small wounds. We found ESCRT were precisely recruited to sites CTL engagement immediately after release. Inhibition machinery...

10.1126/science.abl3855 article EN Science 2022-04-21

Abstract To coordinate cellular physiology, eukaryotic cells rely on the rapid exchange of molecules at specialized organelle–organelle contact sites 1,2 . Endoplasmic reticulum–mitochondrial (ERMCSs) are particularly vital communication hubs, playing key roles in signalling molecules, lipids and metabolites 3,4 ERMCSs maintained by interactions between complementary tethering surface each organelle 5,6 However, due to extreme sensitivity these membrane interfaces experimental perturbation...

10.1038/s41586-023-06956-y article EN cc-by Nature 2024-01-24

Viral ESCRT The (Endosomal Sorting Complex Required for Transport) protein complex plays a role in budding into multivesicular bodies, cytokinesis, and HIV budding, but the details of how ESCRTs facilitate viral are unclear. Now, using high-resolution light electron microscopical imaging techniques, Van Engelenburg et al. (p. 653 , published online 16 January) dissect proteins budding. findings suggest that machinery required scission particles from infected cells is located within core...

10.1126/science.1247786 article EN Science 2014-01-17

Abstract The rhodamine system is a flexible framework for building small‐molecule fluorescent probes. Changing N ‐substitution patterns and replacing the xanthene oxygen with dimethylsilicon moiety can shift absorption fluorescence emission maxima of dyes to longer wavelengths. Acylation nitrogen atoms forces molecule adopt nonfluorescent lactone form, providing convenient method make fluorogenic compounds. Herein, we take advantage all these structural manipulations describe novel...

10.1002/anie.201509649 article EN cc-by-nc Angewandte Chemie International Edition 2015-12-11

The prokaryotic tubulin homolog, FtsZ, forms a ring-like structure (FtsZ-ring) at midcell. FtsZ-ring establishes the division plane and enables assembly of macromolecular machinery (divisome). Although many molecular components divisome have been identified their interactions extensively characterized, spatial organization these proteins within is unclear. Consequently, physical mechanisms that drive assembly, maintenance, constriction remain elusive. Here we applied single-molecule based...

10.1371/journal.pgen.1005128 article EN cc-by PLoS Genetics 2015-04-07

Vimentin intermediate filaments (VIFs) form complex, tightly packed networks; due to this density, traditional imaging approaches cannot discern single-filament behavior. To address this, we developed and validated a sparse vimentin-SunTag labeling strategy, enabling single-particle tracking of individual VIFs providing sensitive, unbiased, quantitative method for measuring global VIF motility. Using approach, define the steady-state motility rate, showing constant ∼8% undergo directed...

10.1083/jcb.202406054 article EN The Journal of Cell Biology 2025-03-10

The ability to localize proteins precisely within subcellular space is crucial understanding the functioning of biological systems. Recently, we described a protocol that correlates precise map fluorescent fusion localized using three-dimensional super-resolution optical microscopy with fine ultrastructural context electron micrographs. While it achieved difficult simultaneous objectives high photoactivated fluorophore preservation and ultrastructure preservation, required specialized...

10.1371/journal.pone.0077209 article EN cc-by PLoS ONE 2013-10-25

Endoplasmic reticulum exit sites (ERESs) are tubular outgrowths of endoplasmic that serve as the earliest station for protein sorting and export into secretory pathway. How these structures respond to different cellular conditions remains unclear. Here, we report ERESs undergo lysosome-dependent microautophagy when Ca2+ is released by lysosomes in response nutrient stressors such mTOR inhibition or amino acid starvation mammalian cells. Targeting uptake were observed super-resolution...

10.1016/j.devcel.2024.03.027 article EN cc-by Developmental Cell 2024-04-08

Rapid decrease of differential gain has been determined to dominate the temperature dependence threshold current in 1.3-/spl mu/m multiquantum well and bulk active lasers giving rise low values T/sub 0/. Extensive experimental characterization each type device is described. Results are presented for on chemical potential carrier density as a function temperature. The data indicate important role temperature-insensitive, dependent determining gain. Modeling MQW based detailed band theory...

10.1109/2944.401204 article EN IEEE Journal of Selected Topics in Quantum Electronics 1995-06-01

Abstract The rhodamine system is a flexible framework for building small‐molecule fluorescent probes. Changing N ‐substitution patterns and replacing the xanthene oxygen with dimethylsilicon moiety can shift absorption fluorescence emission maxima of dyes to longer wavelengths. Acylation nitrogen atoms forces molecule adopt nonfluorescent lactone form, providing convenient method make fluorogenic compounds. Herein, we take advantage all these structural manipulations describe novel...

10.1002/ange.201509649 article EN cc-by-nc Angewandte Chemie 2015-12-11
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