Education, Training, and Experience (key aspects)


B.A.    Rice University, 1973
Environmental Science and Engineering


Ph.D. from The University of Texas Medical Branch, 1978
Department of Human Biological Chemistry and Genetics
Human Genetics and Cell Biology

Mentor: Barbara H. Bowman, Ph.D.

Research focus: proteins of human blood


Post-doctoral Training at Yale University School of Medicine 1978-1982
Department of Molecular Biophysics and Biochemistry

Mentor: William H. Konigsberg, Ph.D.

Research focus: tissue factor and the initiation and control of blood coagulation


Assistant Professor, 1982-1988
University of Colorado School of Medicine
Department of Pathology
Department of Biochemistry, Biophysics and Genetics (secondary)
Research focus: tissue factor, blood coagulation, and their regulation by

blood proteins


Associate Professor, 1988-1993
Professor, 1993-2022

Professor Emeritus, 2022- present
University of Nebraska Medical Center
Department of Pathology, Microbiology, and Immunology
Research focus: tissue factor and blood coagulation regulation and disease
                          Coxsackievirus receptor(s), Coxsackievirus stability and virulence



Research Productivity:


Carson, Steven D., August 29, 1995.  Storage cabinet with active dehumidifier.

U.S. Pat. No. 5, 444, 984. (available for commercialization through

IRBF Development, LLC)


Commercialized Reagents:
Monoclonal Antibody HTF1 against human tissue factor (available for

commercialization through IRBF Development, LLC )

Monoclonal Antibody E(mh)1 against human and mouse coxsackievirus and

adenovirus receptor (available for commercialization

through IRBF Development, LLC )

Monoclonal Antibody RIg9 against rabbit IgG (available for commercialization
            through IRBF Development, LLC )


Most significant publications:
Carson, S.D., and W.H. Konigsberg.  1980.  Cadmium increases tissue factor
(coagulation factor III) activity by facilitating its reassociation with lipids. 
Science 208:307-309.

Enabled efficient reconstitution of active tissue factor-lipid
complexes from preparative fractions, facilitating efforts to isolate the
protein; explained the increased specific activity after chromatography on
concanavalin A.

Carson, S.D.  1981.  Plasma high density lipoproteins inhibit the activation of
factor X by factor VIIa and tissue factor (factor III). FEBS Letts. 132:37-40.

Stimulated efforts to isolate the factor X-dependent inhibitor of the
extrinsic pathway of coagulation, initially called LACI (lipoprotein
associated coagulation inhibitor) or EPI (extrinsic pathway inhibitor) and
now known as TFPI (tissue factor pathway inhibitor).

Carson, S.D.  1985.  Computerized analysis of enzyme cascade reactions using
continuous rate data obtained with an ELISA reader.  Computer Programs in
Biomedicine 19:151-157.

Carson, S.D., and P.G. Archer.  1986.  Tissue factor activity in HeLa cells measured with a
continuous chromogenic assay and ELISA reader.  Thrombos. Res.  41:185-195.

Carson, S.D.  1987.  Continuous chromogenic tissue factor assay: Comparison to clot-based
assays and sensitivity established using pure tissue factor.  Thrombos. Res. 47:379-387.

Enabled quantitative high-throughput assay for tissue factor activity. The
software employed a novel algorithm developed specifically for this
application. The assay was applied to intact and disrupted cells. And, the
assay was calibrated with respect to established clot-based assays.  Later
versions of the software have been used at major pharmaceutical companies.

Carson, S.D., R. Bach, and S.M. Carson.  1985.  Monoclonal antibodies against
bovine tissue factor which block interaction with factor VIIa. Blood 66:152-156.

Carson, S.D., S.E. Ross, R. Bach, and A. Guha.  1987.  An inhibitory monoclonal
antibody against human tissue factor. Blood 70:490-493.

The first of these papers enabled immunoaffinity-purification of sufficient
tissue factor protein for chemical characterization and functional studies.
The antibody reported in the second paper has been used by investigators
around the world to inhibit, purify, and detect human tissue factor.

Carson, S.D., W.M. Henry, and T.B. Shows.  1985.  Tissue factor gene localized
to human chromosome 1 (1pter-1p21). Science 229:991-993.

The only protein of the coagulation cascade with no known genetic
deficiency (at the time) and the last to be mapped to a human chromosome.

Carson, S.D., and D.R. Johnson.  1990.  Consecutive enzyme cascades:
Complement activation at the cell surface triggers increased tissue factor
expression. Blood 76:361-367.

Demonstrated a direct link between the antibody-mediated immune
response and activation of coagulation.

Carson, S.D., N.M. Chapman, and S.M. Tracy.  1997.  Purification of the putative
coxsackievirus B receptor from HeLa cells. Biochem. Biophys. Res. Commun.

One of three papers reporting the receptor in early 1997, ours correctly
identified the amino terminal residue, identified corresponding cDNA
clones in public repositories, and confirmed the previous inferential
mapping of the gene to chromosome 21.

Carson, S.D.  2004.  Coxsackievirus and adenovirus receptor (CAR) is modified
and shed in membrane vesicles. Biochemistry 43:8136-8142.

Revealed that membrane vesicles (also called microparticles) shed from
cell surfaces can contain CAR from which a portion of the intracellular
sequence has been removed by a calpain-like protease.

Carson, S.D., K.-S. Kim, S. J. Pirruccello, S. Tracy, and N.M. Chapman.
2007. Endogenous low-level expression of the coxsackievirus and
adenovirus receptor (CAR) enables coxsackievirus B3 infection of RD cells. J.
Gen Virol. 88:3031-3038.

Carson, S.D., N. M. Chapman, S. Hafenstein, and S. Tracy. 2011. Variation of
coxsackievirus B3 capsid primary structure, ligands, and stability are selected in a
coxsackievirus and adenovirus receptor-limited environment.
J. Virol. 85:3306-3314.

RD cells had been considered to be normally devoid of CAR. The 2007
paper provided a mechanism for CAR-dependent coxsackievirus
infection of RD cells, and an explanation for the development of chronically
infected RD cell cultures. The 2011 paper showed that additional cell-
binding capabilities can evolve in viruses cultured on RD cells when they
are allowed to compete for the rare CAR that gets expressed by the cells.
This provided a plausible hypothesis for why these viruses evolve to
bind cell surface molecules that do not directly support infection in addition
to the receptor that does support infection.

Organtini, L.J., A.M. Makhov, J.F. Conway, S. Hafenstein, and S.D. Carson.
2014. Kinetic and structural analysis of coxsackievirus B3 receptor interactions
and formation of the A-particle. J. Virol. 88:5755-5765.

Carson, S.D. 2014. Kinetic models for receptor-catalyzed conversion of
coxsackievirus B3 to A-particles. J. Virol. 88:11568-11575.

Carson,S.D., S. Tracy, Z. G. Kaczmarek, A. Alhazmi, N. M. Chapman. 2015. Three
capsid amino acids notably influence coxsackie B3 virus stability. J. Gen. Virol. 97:60-68.

Carson, S. D., and A. J. Cole. 2020. Albumin enhances the rate at which
coxsackievirus B3 strain 28 converts to A-particle. J. Virol. 94:1-17. J Virol 94:e01962-19

The first of the two 2014 papers obtained high-resolution structure
for soluble CAR bound to CVB3 and for the CAR-catalyzed A-particle
which no longer bound soluble CAR. Testing a range of CAR
concentrations revealed kinetics for the CAR-catalyzed inactivation
of CVB3. The first-order rate constant increased (almost)
hyperbolically as CAR concentration increased, enabling an empirical
mathematical description of the kinetics. The second paper continued
the analysis of the kinetic data with accommodation of  two capsid
“breathing” conformations, and concluded that the best models for
kapp vs CAR include allostery. The 2015 paper characterized CVB3 strains
differing by single capsid amino acids with half-lives at 37C ranging
from 7 to 17 hours. These CVB3 strains will be useful for validating the
proposed allosteric models. In 2020, we showed that CVB3/28, a commonly
used laboratory strain, was converted to the A-particle more quickly in the presence of
serum albumin. The albumin enhanced the CAR-catalyzed inactivation of
CVB3/28, and was functioning kinetically as a non-essential activating cofactor.


A detailed Curriculum Vitae can be opened here.



Management Skills:

Running a research laboratory in an academic setting requires a unique

operations and management skillset. As principal investigator, I am

responsible for:

--Managing personnel, trainees, and students;
--Managing budgets;
--Securing research funding by preparing proposals to private and government

--Understanding and complying with requirements for use of radioactive materials,

use of infectious agents, protection of human volunteers and donors, use

of human-derived materials, appropriate and humane use of animals, and

disposal of regulated waste;

--Regular reporting of progress as well as publication of studies in appropriate peer-

reviewed journals.

--Conceiving hypotheses and experimental tests to confirm or refute those hypotheses.

--Conducting and interpreting the experiments.

The professional setting requires that laboratory oversight and experimental bench

work are integrated with teaching, committee and administrative assignments, and

other academic responsibilities.


Perhaps my greatest accomplishment has been the ability to structure my time and

responsibilities so that I could spend most of my career in the laboratory doing

research, not telling others how to do it for me.