Kenneth G. Mann

ORCID: 0000-0003-1878-263X
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About
Contact & Profiles
Research Areas
  • Blood Coagulation and Thrombosis Mechanisms
  • Hemophilia Treatment and Research
  • Coagulation, Bradykinin, Polyphosphates, and Angioedema
  • Platelet Disorders and Treatments
  • Blood properties and coagulation
  • Venous Thromboembolism Diagnosis and Management
  • Protease and Inhibitor Mechanisms
  • Vitamin K Research Studies
  • Enzyme Production and Characterization
  • Hemostasis and retained surgical items
  • Atrial Fibrillation Management and Outcomes
  • Trauma, Hemostasis, Coagulopathy, Resuscitation
  • Venomous Animal Envenomation and Studies
  • Peptidase Inhibition and Analysis
  • Antiplatelet Therapy and Cardiovascular Diseases
  • Cell Adhesion Molecules Research
  • Erythrocyte Function and Pathophysiology
  • Bone and Dental Protein Studies
  • Hemoglobin structure and function
  • Cancer-related gene regulation
  • Heparin-Induced Thrombocytopenia and Thrombosis
  • Trauma and Emergency Care Studies
  • Monoclonal and Polyclonal Antibodies Research
  • Acute Myocardial Infarction Research
  • Lipid Membrane Structure and Behavior

Haematologic Technologies (United States)
2016-2022

University of Vermont
2012-2022

MedStar Washington Hospital Center
2021

Iowa City Public Library
2018

International Society of Nephrology
2017

University of Pisa
2014

Texas Biomedical Research Institute
2013

Brigham and Women's Hospital
1999-2012

VA Boston Healthcare System
2012

Boston Children's Hospital
2012

In seven strains of cultured normal human osteoblast-like cells, a mean 1615 molecules tritium-labeled 17β-estradiol per cell nucleus could be bound to specific nuclear sites. The binding the labeled steroid was temperature-dependent, steroid-specific, saturable, and type-specific. These are characteristics biologically active estrogen receptors. Pretreatment with 10 nanomolar estradiol in vitro increased progesterone four six strains, indicating an induction functional RNA blot analysis...

10.1126/science.3388021 article EN Science 1988-07-01

Abstract Gel filtration of reduced protein polypeptide chains in 6 m guanidine hydrochloride has been evaluated as a means estimating or subunit molecular weights suggested by Davison (Science, 161, 906 (1968)). As gel medium, 6% agarose permits useful weight estimates between the extreme limits 80,000 and 1,000. Provided rather than volume is used to measure elution position, excellent precision accuracy can be obtained. A plot log versus position yields sigmoidal curve from which estimated...

10.1016/s0021-9258(18)94300-0 article EN cc-by Journal of Biological Chemistry 1969-09-01

The rates of prothrombin activation under initial conditions invariant concentrations and Factor Xa were studied in the presence various combinations Ca2+, homogeneous bovine V, Va, phosphatidylcholine-phosphatidylserine vesicles, activated platelets. Reactions monitored continuously through enhanced fluorescence accompanying interaction newly formed thrombin with dansylarginine-N-(3-ethyl-1,5-pentanediyl) amide. complete prothrombinase (Factor Xa, phospholipid, Va) behaved as a typical...

10.1016/s0021-9258(19)86616-4 article EN cc-by Journal of Biological Chemistry 1979-11-01

Introduction The biochemical investigation of a biological process can be divided into three segments. first is the development an inventory components involved in process, second establishment connectivity between components, and third dynamics processes as they occur living organism.

10.1055/s-0037-1615780 article EN Thrombosis and Haemostasis 1999-01-01

We have developed a model of the extrinsic blood coagulation system that includes stoichiometric anticoagulants. The accounts for formation, expression, and propagation vitamin K-dependent procoagulant complexes extends our previous by including: (<i>a</i>) tissue factor pathway inhibitor (TFPI)-mediated inactivation (TF)·VIIa its product complexes; (<i>b</i>) antithrombin-III (AT-III)-mediated IIa, mIIa, VIIa, IXa, Xa; (<i>c</i>) initial activation V VIII thrombin generated Xa-membrane;...

10.1074/jbc.m201173200 article EN cc-by Journal of Biological Chemistry 2002-05-01

Because it is unclear whether age-related bone loss results from increased resorption, decreased formation or both, we measured the serum level of Gla-protein (BGP), a specific marker for turnover, in 174 women, ages 30 to 94 yr. Serum BGP linearly with aging (r = 0.44, P less than 0.001) 4.4 +/- 0.4 (mean SE) 4th decade 8.9 0.9 ng/ml 10th decade. This increase correlated inversely (P concomitant decreases mineral density at lumbar spine, midradius, and distal radius. Using partial...

10.1172/jci110882 article EN Journal of Clinical Investigation 1983-05-01

Objectives: To investigate the hemostatic status of critically ill, nonbleeding trauma patients. We hypothesized that a hypercoagulable state exists in patients early after severe injury and pattern clotting fibrinolysis are similar between burned nonburn Materials: Patients admitted to surgical or burn intensive care unit within 24 hours were enrolled. Blood samples drawn on days 0 through 7. Laboratory tests included prothrombin time (PT), activated partial thromboplastin (aPTT), levels...

10.1097/ta.0b013e3181ae6f1c article EN Journal of Trauma and Acute Care Surgery 2009-08-01

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTInhibition of hydroxyapatite-crystal growth by bone-specific and other calcium-binding proteinsRobert W. Romberg, Peter G. Werness, B. Lawrence Riggs, Kenneth MannCite this: Biochemistry 1986, 25, 5, 1176–1180Publication Date (Print):March 11, 1986Publication History Published online1 May 2002Published inissue 11 March 1986https://doi.org/10.1021/bi00353a035RIGHTS & PERMISSIONSArticle Views821Altmetric-Citations225LEARN ABOUT THESE METRICSArticle...

10.1021/bi00353a035 article EN Biochemistry 1986-03-11

The kinetics of the activation human prothrombin catalyzed by prothrombinase was studied using fluorescent alpha-thrombin inhibitor dansylarginine-N-(3-ethyl-1,5-pentanediyl)amide (DAPA). Prothrombinase proteolytically activates to cleavages at Arg273-Thr274 (bond A) and Arg322-Ile323 B). differential fluorescence properties DAPA complexed with intermediates products were exploited study individual bond in zymogen. When catalyst composed (human factor Xa, Va, synthetic phospholipid vesicles,...

10.1016/s0021-9258(18)61503-0 article EN cc-by Journal of Biological Chemistry 1987-03-01

Background —The mechanism of the antithrombotic action statins is unclear. The aim this study was to evaluate effects simvastatin on coagulation process at sites microvascular injury. Methods and Results —Tissue factor–initiated assessed in blood samples collected every 30 seconds from bleeding-time wounds 17 patients who had advanced coronary artery disease total cholesterol levels 224.6±11.8 mg/dL (mean±SEM). Quantitative Western blotting for time courses fibrinogen depletion activation...

10.1161/01.cir.103.18.2248 article EN Circulation 2001-05-08

The activation of prothrombin, factor V, VIII, IX, and X by the tissue factor-factor VIIa complex, in vitro, a system which each precursor protein was present at plasma concentration, evaluated using combination activity assays, immunoblots, active-site blots, autoradiography. thrombin generation curves observed were distinctly nonlinear typically displayed time lag little or no observed. This followed an almost linear propagation phase formation. function factor/factor concentration...

10.1016/s0021-9258(17)31661-7 article EN cc-by Journal of Biological Chemistry 1994-09-01

The intrinsic fluorescence of human and bovine prothrombin fragment 1 is quenched (approximately -35%) when calcium ions are bound. also by the binding Ca2+ but to a lesser extent (total change approximately -6%). transition effected Mg2+, Mn2+, Gd3+, Tb3+. With all quenching readily reversed titration with EDTA. Titration any above results in sigmoidal curve. midpoints (expressed as Tm) occur at following concentrations ions: Ca2+, 0.22 (0.35) mM; (0.45) 12.6 (12.6) muM; 3.6 (5.3) muM (the...

10.1016/s0021-9258(19)75174-6 article EN cc-by Journal of Biological Chemistry 1977-02-01
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