about
Structure of fully liganded Hb ζ2β2strapped in a tense conformationIdentification of a Small Molecule that Increases Hemoglobin Oxygen Affinity and Reduces SS Erythrocyte SicklingDesign, Synthesis, and Investigation of Novel Nitric Oxide (NO)-Releasing Prodrugs as Drug Candidates for the Treatment of Ischemic Disorders: Insights into NO-Releasing Prodrug Biotransformation and Hemoglobin-NO BiochemistryAryloxyalkanoic Acids as Non-Covalent Modifiers of the Allosteric Properties of HemoglobinErythrocytic pyruvate kinase mutations causing hemolytic anemia, osteosclerosis, and seconday hemochromatosis in dogsPyridyl derivatives of benzaldehyde as potential antisickling agents.Investigating the magnetic susceptibility properties of fresh human blood for noninvasive oxygen saturation quantificationA reverse time-course method for transcriptional chase analyses of mRNA half-lives in cultured cells.Identification of a novel class of covalent modifiers of hemoglobin as potential antisickling agentsAn erythroid chaperone that facilitates folding of alpha-globin subunits for hemoglobin synthesisCorrection of murine hemoglobinopathies by prenatal tolerance induction and postnatal nonmyeloablative allogeneic BM transplants.A hemoglobin variant associated with neonatal cyanosis and anemiaNew developments in anti-sickling agents: can drugs directly prevent the polymerization of sickle haemoglobin in vivo?Hb Baden: structural and functional characterization.Forced chromatin looping raises fetal hemoglobin in adult sickle cells to higher levels than pharmacologic inducers.Crystal structure of carbonmonoxy sickle hemoglobin in R-state conformation.Clinical Implications of the Association of Fetal Hemoglobin with Peripheral Oxygen Saturation in Sickle Cell Disease.Mixed chimerism following in utero hematopoietic stem cell transplantation in murine models of hemoglobinopathy.Structural basis for the potent antisickling effect of a novel class of five-membered heterocyclic aldehydic compounds.Structures of R- and T-state hemoglobin Bassett: elucidating the structural basis for the low oxygen affinity of a mutant hemoglobin.Design, Synthesis, and Biological Evaluation of Ester and Ether Derivatives of Antisickling Agent 5-HMF for the Treatment of Sickle Cell Disease.Characterization of hemoglobin bassett (alpha94Asp-->Ala), a variant with very low oxygen affinity.Purification of diverse hemoglobins by metal salt precipitation.Glutaraldehyde cross-linking increases the stability of Lumbricus terrestris erythrocruorin.Prolonging the shelf life of Lumbricus terrestris erythrocruorin for use as a novel blood substitute.T2 -prepared balanced steady-state free precession (bSSFP) for quantifying whole-blood oxygen saturation at 1.5T.Rational design of pyridyl derivatives of vanillin for the treatment of sickle cell disease.A Triazole Disulfide Compound Increases the Affinity of Hemoglobin for Oxygen and Reduces the Sickling of Human Sickle Cells.Direct comparison of oligochaete erythrocruorins as potential blood substitutes.Rational modification of vanillin derivatives to stereospecifically destabilize sickle hemoglobin polymer formationDomain-focused CRISPR screen identifies HRI as a fetal hemoglobin regulator in human erythroid cellsRapid and reproducible characterization of sickling during automated deoxygenation in sickle cell disease patientsThe E3 ligase adaptor molecule SPOP regulates fetal hemoglobin levels in adult erythroid cellsIncreasing the stability of Lumbricus terrestris erythrocruorin via poly(acrylic acid) conjugationHereditary methemoglobinemia in a cyanotic cat presented for ovariohysterectomy
P50
Q27680169-ECEFF119-CD1F-4EC3-B07A-35A69F7BFA22Q27684817-F4DE8672-A211-417A-9EF2-7DC09C132DC8Q27702646-3B94CC5C-1BA7-459F-97F6-055AA640840EQ27727697-50C2E4FF-8550-481A-B761-D518F8076C5CQ30419292-DE343A62-9371-42C7-9486-C2B3F65383AFQ30446978-E612B9D7-F588-4FEE-B75B-6125705790B1Q34097379-86B4AAE4-510B-4892-8323-37C45A3F72DDQ34342433-2FA39448-CC00-4247-8F15-63071BE7D4D3Q35661138-0460ECB9-120A-4E2D-B774-8CE61C394EA6Q35865381-AA3A2772-850E-499C-879E-E00058305A60Q36027459-4614EEB4-D2E7-4AE5-98CA-9571C5C59134Q36784035-6AE2F0E8-F9A9-4E99-A3E9-8E7B49D14B74Q38948912-87B5A2B7-66B0-4DA6-B336-351E5FDCBA25Q39658277-DCC9FA5F-4DC2-4723-BDDA-D67ADA909A15Q40953481-0212CA2E-0FF4-4BD2-B0DF-E1EF83965012Q41131938-748C9FAB-93AC-4852-B894-20DD15703548Q42651980-957FED6D-FE3E-421C-9A1C-A1276309B5D6Q44319089-FF0DD418-A343-4FC3-A617-3A291A69F11BQ44904614-0FE7CF67-6C67-4599-A07F-5DFC906C0A65Q44908064-D7227BF3-FA71-4CD1-8B94-A766875D59D5Q45066332-697AC11E-3202-4A79-804E-0E990EF51186Q45115834-7C94D321-BED3-441A-962D-B138DD814C55Q46670768-FB746B6F-130C-496F-8A72-CA82A5D94356Q47196244-05DC37EC-9EAA-4D80-A63D-83A5903529D3Q47358316-427FD42C-1698-4A25-94AF-7A03E2E01CB1Q47761178-6954F1A7-970E-49E0-BE4A-D9619950AB8FQ52321402-4133F06F-B351-4055-95EA-E67EF0CDFB8DQ52596367-4E7E7D94-C277-45DD-8364-B1AECD83B9A4Q53712321-11FEF9B8-5856-4B4D-93E8-268B77A2BE75Q57050917-879E92D8-6A68-417A-925B-D83EC271BC45Q63433323-C722E69C-52B0-48DD-A4BA-011C89FF3A0FQ64112591-7DB0121C-04AF-4D92-86AD-707B01ED43C9Q64290214-4B1F0DFA-6A3F-44EB-A4C4-35E2A53A6AF4Q89148152-FAA6E9D0-DF50-4F0E-90E3-7A803A5158D8Q91960445-18AD3476-BFE0-4818-8701-9615A684ECC7
P50
description
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Osheiza Abdulmalik
@ast
Osheiza Abdulmalik
@en
Osheiza Abdulmalik
@es
Osheiza Abdulmalik
@nl
type
label
Osheiza Abdulmalik
@ast
Osheiza Abdulmalik
@en
Osheiza Abdulmalik
@es
Osheiza Abdulmalik
@nl
altLabel
Abdulmalik O
@en
Abdulmalik OY
@en
prefLabel
Osheiza Abdulmalik
@ast
Osheiza Abdulmalik
@en
Osheiza Abdulmalik
@es
Osheiza Abdulmalik
@nl
P106
P31
P4012
P496
0000-0003-2497-4291