Videos

The Role of Transthyretin (TTR) in Normal Human Physiology
The first video in the 9-part “Interview with the Innovators” series is titled “The Role of Transthyretin (TTR) in Normal Human Physiology.” In this video clip, Joel N. Buxbaum, MD, Professor Emeritus, Molecular Medicine, The Scripps Research Institute, and Chief Medical Officer (consulting), Protego Biopharma, discusses the principal, as well as, less defined mechanisms underlying the physiologic functions of TTR in healthy individuals. These learnings are key for the optimal understanding of disease states associated with abnormalities in TTR structure and function.

Transthyretin (TTR) Amyloidosis: Disease Definition and Key Clinical Features
Ola Akinboboye, MD, MPH, MBA, Clinical Professor, Cardiology, Donald and Barbara Zucker School of Medicine at Hofstra University/Northwell Health and Medical Director, Laurelton Heart Specialists PC (Rosedale, NY) describes the clinical manifestations of wild-type and hereditary or variant transthyretin amyloidosis (ATTR) and some common mutational drivers of pathogenic phenotypes.

Transthyretin (TTR) Amyloidosis: Main Types and Disease Trajectory Over Time
Ola Akinboboye, MD, MPH, MBA, Clinical Professor, Cardiology, Donald and Barbara Zucker School of Medicine at Hofstra University/Northwell Health and Medical Director, Laurelton Heart Specialists PC (Rosedale, NY) discusses the pathophysiologic features of TTR amyloidosis (ATTR) as a disease entity and introduces the two types of ATTR, wild-type and hereditary or variant.

Complexities of Transthyretin Amyloid Disposition
Joel N. Buxbaum, MD, Professor Emeritus, Molecular Medicine, The Scripps Research Institute, and Chief Medical Officer (consulting), Protego Biopharma, explores the mechanisms of organ damage in TTR amyloidosis (ATTR). This important information focuses on the biophysical and biochemical underpinnings of misfolded transthyretin (TTR) leading to tissue dysfunction in this disease.

Transthyretin (TTR) Amyloidosis: Current Diagnostic Approaches in the Clinic
Justin L. Grodin, MD, MPH, Assistant Professor of Medicine, UT Southwestern Medical Center (Dallas, TX), presents a diagnostic algorithmic approach for the establishment of a firm diagnosis of ATTR, with a focus on ATTR patients with heart manifestations (cardiomyopathy).

Recognizing Clinical Clues of ATTR-CM
Clement C. Eiswirth, Jr., MD, FACC, Medical Director, Cardiomyopathy and Heart Failure Program, Ochsner Health, New Orleans, LA, examines clinical hints for consideration in the diagnosis of ATTR-CM.

Evoking Suspicion of ATTR-CM: Warning Signs
Clement C. Eiswirth, Jr., MD, FACC, Medical Director, Cardiomyopathy and Heart Failure Program, Ochsner Health, New Orleans, LA, offers warning signs of ATTR-CM to consider for patients with heart failure.

Setting Realistic Treatment Goals and Expectations for Patients with Transthyretin Amyloidosis
Ola Akinboboye, MD, MPH, MBA, Clinical Professor, Cardiology, Donald and Barbara Zucker School of Medicine at Hofstra University/Northwell Health and Medical Director, Laurelton Heart Specialists PC (Rosedale, NY) and Clement C. Eiswirth, Jr., MD, FACC, Medical Director, Cardiomyopathy and Heart Failure Program, Ochsner Health, New Orleans, LA, highlight the importance of early diagnosis and realistic expectations for patients being treated for transthyretin amyloidosis.

Serum Transthyretin in the Management of TTR Amyloidosis
Justin L. Grodin, MD, MPH, Assistant Professor of Medicine, UT Southwestern Medical Center, Dallas, TX, explains the current and potentially future utilities of serum transthyretin (sTTR) as a biomarker in the management of transthyretin amyloidosis.

Transthyretin (TTR) Protein in Humans: Stabilization vs Destabilization
In this first video clip, Sarah C. Paciulli, MS, RN, CHFN, NP-C, VCU Health, Richmond, VA; Amy Brownell, MSN, FNP-C, AACC, System Director of Heart Failure, AMITA Health, Chicago, IL; and Lori Roth, MS, PA-C, Advanced Heart Failure Clinic, UT Southwestern Medical Center, Dallas, TX, describe the functions of transthyretin (TTR) in its naturally occurring tetrameric form and resulting damage from TTR destabilization.

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