C.S. Raman

ORCID: 0000-0002-1036-3193
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About
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Research Areas
  • Nitric Oxide and Endothelin Effects
  • Heme Oxygenase-1 and Carbon Monoxide
  • Hemoglobin structure and function
  • Metal-Catalyzed Oxygenation Mechanisms
  • Porphyrin Metabolism and Disorders
  • Eicosanoids and Hypertension Pharmacology
  • Connective tissue disorders research
  • Plant biochemistry and biosynthesis
  • Neonatal Health and Biochemistry
  • Monoclonal and Polyclonal Antibodies Research
  • Aortic Disease and Treatment Approaches
  • Industrial Gas Emission Control
  • X-ray Diffraction in Crystallography
  • Odor and Emission Control Technologies
  • Metalloenzymes and iron-sulfur proteins
  • Computational Drug Discovery Methods
  • Photosynthetic Processes and Mechanisms
  • Mitochondrial Function and Pathology
  • Glycosylation and Glycoproteins Research
  • Analytical Chemistry and Sensors
  • Metabolism and Genetic Disorders
  • Photoreceptor and optogenetics research
  • ATP Synthase and ATPases Research
  • Gas Sensing Nanomaterials and Sensors
  • Neutrophil, Myeloperoxidase and Oxidative Mechanisms

University of Maryland, Baltimore
2010-2023

Dr. C. V. Raman University
2019-2023

University of Maryland, Baltimore County
2022

The University of Texas Health Science Center at Houston
2001-2009

The University of Texas at Austin
2004-2006

The University of Texas Health Science Center at San Antonio
1992-2005

The University of Texas MD Anderson Cancer Center
2005

Marshfield Clinic
2005

The Ohio State University
2005

University of Iowa
2005

The vascular smooth muscle cell (SMC)-specific isoform of alpha-actin (ACTA2) is a major component the contractile apparatus in SMCs located throughout arterial system. Heterozygous ACTA2 mutations cause familial thoracic aortic aneurysms and dissections (TAAD), but only half mutation carriers have disease. Linkage analysis association studies individuals 20 families with indicate that can diversity diseases, including premature onset coronary artery disease (CAD) ischemic strokes (including...

10.1016/j.ajhg.2009.04.007 article EN publisher-specific-oa The American Journal of Human Genetics 2009-05-01

Background— A genetic predisposition for progressive enlargement of thoracic aortic aneurysms leading to type dissection (TAAD) is inherited in an autosomal-dominant manner up 19% patients, and a number chromosomal loci have been identified the condition. Having mapped TAAD locus 3p24–25, we sequenced gene transforming growth factor-β receptor II ( TGFBR2 ) determine whether mutations this resulted familial TAAD. Methods Results— We all 8 coding exons by using genomic DNA from 80 unrelated...

10.1161/circulationaha.105.537340 article EN Circulation 2005-07-19

Tyrosine nitration is a covalent posttranslational protein modification derived from the reaction of proteins with nitrating agents. Protein appears to be selective process since not all tyrosine residues in or are nitrated vivo. To investigate factors that may determine biological selectivity nitration, we developed an vitro model consisting three similar size but different three-dimensional structure and content. Exposure ribonuclease A putative vivo agents revealed preferential residue...

10.1006/abbi.1999.1480 article EN cc-by-nc-nd Archives of Biochemistry and Biophysics 1999-11-01

Non-syndromic thoracic aortic aneurysms and dissections (TAADs) are inherited in an autosomal dominant manner ∼20% of cases. Familial TAAD is genetically heterogeneous four loci have been mapped for this disease to date, including a locus at 16p associated with patent ductus arteriosus (PDA). The defective gene the has recently identified as smooth muscle cell (SMC)-specific myosin heavy chain (MYH11). On sequencing MYH11 93 families alone three TAAD/PDA, we novel mutations two but none...

10.1093/hmg/ddm201 article EN Human Molecular Genetics 2007-04-05

The crystal structures of the heme domain human inducible nitric-oxide synthase (NOS-2) in zinc-free and -bound states have been solved. In structure, two symmetry-related cysteine residues form a disulfide bond. zinc-bound state, these same part zinc-tetrathiolate (ZnS(4)) center indistinguishable from that observed endothelial isoform (NOS-3). As NOS-3, ZnS(4) plays key role stabilizing intersubunit contacts maintaining integrity cofactor (tetrahydrobiopterin) binding site NOS-2. A...

10.1074/jbc.274.30.21276 article EN cc-by Journal of Biological Chemistry 1999-07-01

Nitric oxide (NO) is extremely toxic to Clostridium botulinum , but its molecular targets are unknown. Here, we identify a heme protein sensor (SONO) that displays femtomolar affinity for NO. The crystal structure of the SONO domain reveals previously undescribed fold and strategically placed tyrosine residue modulates heme-nitrosyl coordination. Furthermore, architecture ortholog cloned from Chlamydomonas reinhardtii indicates NO signaling through cyclic guanosine monophosphate arose before...

10.1126/science.1103596 article EN Science 2004-10-08

Abstract Access to experimental X-ray diffraction image data is fundamental for validation and reproduction of macromolecular models indispensable development structural biology processing methods. Here, we established a publication dissemination system, Structural Biology Data Grid (SBDG; data.sbgrid.org), preserve primary sets that support scientific publications. are accessible researchers through community driven grid, which facilitates global access. Our analysis pilot collection...

10.1038/ncomms10882 article EN cc-by Nature Communications 2016-03-07

PAS domains, which have been identified in over 1100 proteins from all three kingdoms of life, convert various input stimuli into signals that propagate to downstream components by modifying protein-protein interactions. One such protein is the Escherichia coli redox sensor, Ec DOS, a phosphodiesterase degrades cyclic adenosine monophosphate redox-dependent manner. Here we report crystal structures heme domain DOS both inactive Fe(3+) and active Fe(2+) forms at 1.32 1.9 A resolution,...

10.1074/jbc.m314199200 article EN cc-by Journal of Biological Chemistry 2004-04-30

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTDiffusion-limited rates for monoclonal antibody binding to cytochrome cC. S. Raman, Ronald Jemmerson, Barry T. Nall, and Michael J. AllenCite this: Biochemistry 1992, 31, 42, 10370–10379Publication Date (Print):October 1, 1992Publication History Published online1 May 2002Published inissue 1 October 1992https://pubs.acs.org/doi/10.1021/bi00157a027https://doi.org/10.1021/bi00157a027research-articleACS PublicationsRequest reuse permissionsArticle...

10.1021/bi00157a027 article EN Biochemistry 1992-10-01

Restricted usage of VH genes is observed in rabbit B lymphocytes and human murine CD5 lymphocytes. This observation raised the possibility that most were CD5+. To investigate this we cloned gene from a cosmid library, using probe derived cDNA. The was transfected into T cell line then used transfectants to develop anti-rabbit mAb. By Western blot analysis, mAb reacted with 67-kDa protein lysates prepared mesenteric lymph node spleen cells. We determined frequency CD5+ peripheral lymphoid...

10.4049/jimmunol.149.12.3858 article EN The Journal of Immunology 1992-12-15

Hereditary coproporphyria is an autosomal dominant disorder resulting from the half-normal activity of coproporphyrinogen oxidase (CPO), a mitochondrial enzyme catalyzing antepenultimate step in heme biosynthesis. The mechanism by which CPO catalyzes oxidative decarboxylation, extraordinary metal- and cofactor-independent manner, poorly understood. Here, we report crystal structure human at 1.58-Å resolution. reveals previously uncharacterized tertiary topology comprising unusually flat...

10.1073/pnas.0506557102 article EN Proceedings of the National Academy of Sciences 2005-09-21

Nitric oxide is generated under normal and pathophysiological conditions by three distinct isoforms of nitric synthase (NOS). A small-molecule inhibitor NOS (3-Br-7-nitroindazole, 7-NIBr) profoundly neuroprotective in mouse models stroke Parkinson's disease. We report the crystal structure catalytic heme domain endothelial complexed with 7-NIBr at 1.65 resolution. Critical to binding substrate site adoption eNOS an altered conformation, which a key glutamate residue swings out toward one...

10.1021/bi010957u article EN Biochemistry 2001-10-20

The crystal structure of the endothelial nitric oxide synthase (NOS) heme domain complexed with NO reveals close hydrogen bonding interactions between and terminal guanidino nitrogen substrate, l-arginine. Dioxygen is expected to bind in a similar mode which will facilitate proton abstraction from l-Arg dioxygen, required step for O−O bond cleavage. Structures mechanism-based NOS inhibitors, N5-(1-iminoethyl)-l-ornithine N-(3-(aminomethyl)benzyl)acetamidine, provide clues on how this class...

10.1021/bi002658v article EN Biochemistry 2001-04-12

It has been proposed that Cys99 of human endothelial nitric oxide synthase (eNOS) is responsible for tetrahydrobiopterin (BH4) binding. To examine this possibility rigorously, we expressed rat neuronal NOS (nNOS) in Escherichia coli, with the homologous Cys331 to Ala mutation, and characterized structural functional attributes purified, mutated enzyme. C331A-nNOS, as isolated, was catalytically incompetent. Upon prolonged incubation L-arginine (L-Arg), not only BH4 binding but also catalytic...

10.1074/jbc.273.52.34799 article EN cc-by Journal of Biological Chemistry 1998-12-01

Hydrostatic pressures up to 2 kbar have been used form monomers from the 14-subunit oligomer of chaperonin, Cpn60. The fluorescence 1,1'-bi(4-anilino) naphthalene-5,5'-disulfonic acid (bisANS), followed at high pressure, demonstrated an increase in hydrophobic exposure on dissociation. Cpn60 dissociated with first order kinetics. transition occurred between 1.3 and (P50 = 1.75 kbar), it was facilitated by MgATP 1.1 kbar). With MgATP, showed a rapid phase (t1/2 3.7 min) addition that similar...

10.1074/jbc.270.5.2061 article EN cc-by Journal of Biological Chemistry 1995-02-01

The reversible two-electron interconversion of formate and CO2 is catalyzed by both nonmetallo- metallo-formate dehydrogenases (FDHs). latter group comprises molybdenum- or tungsten-containing enzymes with the metal coordinated two equivalents a pyranopterin cofactor, cysteinyl selenocysteinyl (Sec) ligand supplied polypeptide, catalytically essential terminal sulfido ligand. In addition, these biocatalysts incorporate one more [4Fe–4S] clusters for facilitating long-distance electron...

10.1021/acscatal.2c00316 article EN ACS Catalysis 2022-08-10

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTEnthalpy of Antibody-Cytochrome c BindingC. S. Raman, Michael J. Allen, and Barry T. NallCite this: Biochemistry 1995, 34, 17, 5831–5838Publication Date (Print):May 2, 1995Publication History Published online1 May 2002Published inissue 2 1995https://pubs.acs.org/doi/10.1021/bi00017a015https://doi.org/10.1021/bi00017a015research-articleACS PublicationsRequest reuse permissionsArticle Views344Altmetric-Citations38LEARN ABOUT THESE METRICSArticle...

10.1021/bi00017a015 article EN Biochemistry 1995-05-02
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