Bruce J. Schnapp

John Brown University

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Trends

Author Order

Document Type

Co-Authors

Thomas S. Reese

Drexel University

Michael P. Sheetz

National University of Singapore

Ronald D. Vale

Howard Hughes Medical Institute

Tatiana Abramson

Harvard University

Jeff Gelles

Brandeis University

Virgil Mureşan

Rutgers, The State University of New Jersey

E. Steuer

University of Minnesota System

Enrico Mugnaini

Northwestern University

Sunjong Kwon

Oregon Health & Science University

James O. Deshler

U.S. National Science Foundation

Cooperative Institutions

Harvard University

National Institutes of Health

Harvard University Press

Boston University

Karolinska Institutet

Princeton University

Massachusetts Institute of Technology

Stockholm University

Howard Hughes Medical Institute

The Ohio State University

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Field

Nanometer Measurements Of Motor Protein And Membrane Glycoprotein Movements

Proceedings of SPIE, the International Society for Optical Engineering/Proceedings of SPIE (1989)

Michael P. Sheetz Jeff Gelles E. Steuer Bruce J. Schnapp J. Dubinska

The recent application of digital imaging technologies to the analysis of video images from a DIC (differential interference contrast) light microscope has given 1-2 nm precision for the measurement of movements of submicron particles at 30 Hz. [Gelles et al., Nature 331(1988)450]. This technique has been applied to the study of the movements of 1) motor proteins (kinesin and cytoplasmic dynein) on microtubules (MTs) and 2) membrane glycoproteins in cellular plasma membranes. In both cases the nanometer measurements have provided important new insights into the molecular mechanisms which govern those biological movements.

Kinesin

Nanometre

Molecular biophysics

Molecular motor

10.1117/12.962707

Cite

Citations (0)

Nanometer-scale motion analysis of microtubule-based motor enzymes

Proceedings annual meeting Electron Microscopy Society of America (1988)

Jeff Gelles Bruce J. Schnapp E. Steuer Michael P. Sheetz

Kinesin and cytoplasmic dynein are mechanochemical ATPases thought to transport vesicular organelles within cells by moving them along microtubules. Molecules from purified enzyme preparations will bind to plastic microspheres (beads) and move them along microtubules in vitro at rates of ∽0.5 μm s -1 . Bead movement can be directly observed by light microscopy in an assay that provides an opportunity to study motions driven by small numbers of enzyme molecules. Measurement of such motions with nanometer-scale precision yields information about the molecular events which drive bead movement. We devised a method to measure the relative position o£ an enzyme-driven 150nm bead with a precision better than 1 nm at 30 Hz 2 . This method is based on digital processing of bead images in differential interference contrast microscopy using a cross-correlation/centroid algorithm.

Kinesin

Bead

Organelle

Molecular motor

10.1017/s0424820100102420

Cite

Citations (2)

Erratum: “Improved nm displacement detector for microscopic beads at frequencies below 10 Hz” [Rev. Sci. Instrum. 68, 2195 (1997)]

Review of Scientific Instruments (1997)

Daqun Li Bruce J. Schnapp

First Page

10.1063/1.1148455

Cite

Citations (0)

A Change in the Selective Translocation of the Kinesin-1 Motor Domain Marks the Initial Specification of the Axon

Neuron (2006)

Catherine Jacobson Bruce J. Schnapp Gary Banker

Kinesin

Neurite

Growth cone

Molecular motor

10.1016/j.neuron.2006.02.005

Cite

Citations (264)

Optimized Filter Set and Viewing Conditions for the S65T Mutant of GFP in Living Cells

BioTechniques (1996)

Mark J. Zylka Bruce J. Schnapp

Opsin

10.2144/96212bm11

Cite

Citations (14)

The paranodal axo-glial junction in the central nervous system studied with thin sections and freeze-fracture

Neuroscience (1976)

Bruce J. Schnapp Camillo Peracchia Enrico Mugnaini

Axolemma

10.1016/0306-4522(76)90075-0

Cite

Citations (76)

Vesicle Movements And Microtubule-Based Motors

Journal of Cell Science (1986)

Michael P. Sheetz Ronald D. Vale Bruce J. Schnapp Trina A. Schroer Thomas S. Reese

ABSTRACT The movements of many cytoplasmic vesicles follow the paths of microtubules, some moving in one direction and others moving in the opposite direction on the same microtubule. Recently we have isolated one cytoplasmic motor, kinesin, and defined another, the axoplasmic retrograde factor, both of which are capable of powering anionic latex beads in both directions along polar microtubule arrays. Evidence summarized here supports but does not prove the hypothesis that kinesin and the retrograde motors are indeed responsible for powering vesicle movements.

Kinesin

Molecular motor

Axoplasmic transport

10.1242/jcs.1986.supplement_5.11

Cite

Citations (33)

Single microtubules from squid axoplasm support bidirectional movement of organelles

Cell (1985)

Bruce J. Schnapp Ronald D. Vale Michael P. Sheetz Thomas S. Reese

Axoplasm

Organelle

10.1016/0092-8674(85)90160-6