sameAs
Acylphosphatase 1Acylphosphatase 2Acylphosphatase 2, muscle typeAcylphosphatase 1, erythrocyte (common) typeAcylphosphatase TTHA0567acylphosphatase Rv2922AAcylphosphatase LBA1522Acylphosphatase TDE0797Acylphosphatase lpg1886Acylphosphatase PA0954Acylphosphatase LA_3975Acylphosphatase AHA_2230Acylphosphatase VC1355Acylphosphatase VF_1502Acylphosphatase VP1627Acylphosphatase CBU_1995Acylphosphatase DVU1192Acylphosphatase Rru_A2654Acylphosphatase CT0126Acylphosphatase Caur_3593Acylphosphatase SAOUHSC_01406Acylphosphatase DR_0929Acylphosphatase SSUBM407_1598Acylphosphatase SMU_1725Acylphosphatase SAG1607Acylphosphatase spr1789Putative acylphosphatase SPy_0352Acylphosphatase EF2401Acylphosphatase HMPREF0351_11911Acylphosphatase L196178Acylphosphatase BSU_07640Acylphosphatase CA_C2830Acylphosphatase Moth_1216Acylphosphatase lp_1554Acylphosphatase BMAA1957Acylphosphatase THEYE_A0841Acylphosphatase BPSS2164Acylphosphatase gsr3993Acylphosphatase AMED_1902Acylphosphatase GSU0889
P361
A new acylphosphatase isoenzyme from human erythrocytes: purification, characterization, and primary structureChemical synthesis and expression of a gene coding for human muscle acylphosphataseDifferential modulation of expression of the two acylphosphatase isoenzymes by thyroid hormoneThe Diamond STING serverCrystal structure of the Atx1 metallochaperone protein at 1.02 A resolutionCrystal structure and anion binding in the prokaryotic hydrogenase maturation factor HypF acylphosphatase-like domainThree-dimensional structure of acylphosphatase. Refinement and structure analysisStructure–function analysis of the 3′ phosphatase component of T4 polynucleotide kinase/phosphataseThe Structure of Fcp1, an Essential RNA Polymerase II CTD PhosphataseRational stabilization of enzymes by computational redesign of surface charge-charge interactionsSolution structure and conformational heterogeneity of acylphosphatase from Bacillus subtilisA Rigidifying Salt-Bridge Favors the Activity of Thermophilic Enzyme at High Temperatures at the Expense of Low-Temperature ActivityStructure of the [NiFe]-hydrogenase maturation protein HypF fromThermococcus kodakarensisKOD1Structure of hydrogenase maturation protein HypF with reaction intermediates shows two active sitesEdge strand engineering prevents native-like aggregation in Sulfolobus solfataricus acylphosphataseCrystal structure of common type acylphosphatase from bovine testisCloning and expression of the cDNA coding for the erythrocyte isoenzyme of human acylphosphataseA nucleophilic catalysis step is involved in the hydrolysis of aryl phosphate monoesters by human CT acylphosphataseInsights into acylphosphatase structure and catalytic mechanismImmunoaffinity purification and immunoassay determination of human erythrocyte acylphosphataseModeling by homology of RNA binding domain in A1 hnRNP proteinACYP1 gene possesses two alternative splicing forms that induce apoptosisPhosphoglycerate kinase 2 (PGK2) is essential for sperm function and male fertility in miceAssignment of the human erythrocyte acylphosphatase gene (ACYP1) to chromosome band 14q24.3Effects of acylphosphatase on the activity of erythrocyte membrane Ca2+ pumpInhibition of horse muscle acylphosphatase by pyridoxal 5'-phosphateShortening a loop can increase protein native state entropy.Importance of hydrophobic cluster formation through long-range contacts in the folding transition state of two-state proteins.Understanding protein hydrogen bond formation with kinetic H/D amide isotope effects.Three-dimensional structural characterization of a novel Drosophila melanogaster acylphosphatase.Identifying specific protein residues that guide surface interactions and orientation on silica nanoparticles.Topological mirror images in protein structure computation: an underestimated problem.Development and application of serine/threonine ligation for synthetic protein chemistry.Application of maximum-entropy maps in the accurate refinement of a putative acylphosphatase using 1.3 A X-ray diffraction data.A molecular dynamics study of acylphosphatase in aggregation-promoting conditions: the influence of trifluoroethanol/water solvent.Slow folding of muscle acylphosphatase in the absence of intermediates.Determination of a transition state at atomic resolution from protein engineering data.Selection of antibody fragments specific for an alpha-helix region of acylphosphatase.A 25-signal proteomic signature and outcome for patients with resected non-small-cell lung cancer.Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding.
P921
Q21113795-F904966C-9574-491C-A831-C788531A4453Q21113800-75DE031E-5CA9-46EE-92CE-59C5A60AB819Q21498826-277FFCCC-7A60-4317-8A81-B6A793BB744EQ21498827-8D205CE5-544C-4E77-B0D2-3821684A354DQ21756482-C4818D39-27F1-4E33-8449-01C173B08F71Q22232803-8108F0EF-DA34-495B-B01C-840E464B85A3Q22257968-32F2123B-3B03-43B0-B32D-2C77F63F1BC2Q22291807-4A172B97-3BC9-482C-BC6D-8E49B0747D44Q22335966-37C8832E-EA5E-407B-BB54-D12856ADFF08Q22990443-89127420-144C-4EFA-9791-32F922A65E04Q23063504-F8E7387C-BF32-4BBE-A79D-470771DF91B0Q23429977-0AD057BB-7DE7-434B-A93C-83F867EF42CBQ23435974-BA627608-EABB-4C31-8B17-3CCE94981B79Q23436425-C753E970-3557-45EF-B3AE-0CDF077A55E9Q23443399-B3940823-2039-4765-9C06-A61A7926943BQ23448158-5E69677D-E3E1-40AC-9A53-FB6EA3F85A02Q23461666-B1546CD6-7294-45FE-AA3C-7F59E09525BCQ23467784-3F279878-5114-4CAC-BA3A-6835F1086D31Q23470542-E37C14D9-3D21-449B-AA64-48E705470F4EQ23474823-EC4EB056-6B99-4938-B5AB-651EF4FDC3DDQ23478402-36F28C9E-50DD-46EC-9F9B-CC9841F4C1D8Q23484399-4293C9B4-FE92-41CA-91F8-DE702215AE63Q23489857-48F6564C-7530-47A7-B4FF-DFAE4882E6E2Q23491454-D61FEE65-B36B-4FD4-BC82-3D63BB2F671EQ23493122-DD71B6B1-431D-4180-9E2A-EA9CFD1A4E6DQ23495937-733A8BF5-524C-43A4-93D0-CA1A64815061Q23497580-FAF27090-62A0-472E-890F-4F41FD4EBEAAQ23502229-B30821D1-714E-44BF-AE50-919619102A7BQ23504535-08B3A3F1-010D-449B-8E1C-6F30127C3360Q23506974-56166B68-2556-43E2-9FFF-1A63EEDAB557Q23518173-CA8259AE-7DD2-461C-A8B2-8A69AC172CAEQ23525121-4FD55BE0-62FD-4E2D-91C5-37F6EF770ADCQ23538149-6ABA5805-36CD-49EC-A2AB-D65D86950861Q23538599-C80A303E-E650-4889-96AF-FDB136F013CFQ23546051-2A8E1F3C-13DD-43B3-A5DA-080B53EE7670Q23551154-4767620D-D47B-4324-80C7-A2AD47F63336Q23555606-B5449125-9DD0-4B8E-AD31-FC35E2D17252Q23570591-98F5081A-6C66-45F5-9BEC-E99A8E1B49E8Q23573075-AF7F38E9-A08D-4F37-9875-CCB4AF5B4E6CQ23585903-5CFEAB4E-23D6-4640-92B4-ABAE68ABA1DD
P361
Q24295381-FF1AE538-CF0E-4665-BB51-89825298989CQ24323387-CF3748F4-F250-43E6-8BEE-91480C15694FQ24528213-D7AA1E54-C1A4-4C51-B9F8-6DDF6B79FF7FQ24812433-2AFBD7E7-7F5B-48BC-B33F-37F6699BDD89Q27619033-231514B3-F1FC-4F55-AF72-0148C08C7FE5Q27639566-D1AAA1FB-4D3B-480F-8628-CE2F105B0CB0Q27642071-64765011-1F6A-42EE-BB87-C559C7F653F4Q27644742-04B4E7FD-40E4-4626-9F15-E7E72B627A68Q27652973-5A614A15-2EF3-4A5C-8FD7-3158C24C942CQ27653671-B6620F1A-68E7-4786-A396-71739B8A873EQ27661385-2922BE5B-0C36-4883-8119-FAD73F2C75BAQ27667310-41951109-4FC6-4368-B305-ED05375F3518Q27673788-AEBE6A7A-438D-4B64-9DEA-FB308C7F8B12Q27676035-BD224D74-4E6B-4715-9A98-286201A6A6B0Q27690644-CC231CAB-9911-4F2B-909E-7AE3CE9A62CFQ27734684-3C8A8216-7F4F-4CD8-9A0B-84A6B401A176Q28115485-E38D79DB-BF51-4B6A-9C85-0F034FA59222Q28212599-12910C2B-FE91-46FA-AABA-0DDBC367A80DQ28235991-FAA03CC2-D4A5-446A-804D-33808FEF9518Q28241311-100F2CEB-8BD3-4F67-A0AE-720A303179F0Q28243471-1EE47542-941A-4CF5-8CDF-0DF975E7068FQ28247576-5DCFDD09-CC18-4CC2-A2C4-52CF72112706Q28258839-21B439B0-BF79-4FC5-BBC0-84B85B60BBCBQ28281584-550FFA13-31D3-4AFF-82C8-95E078949583Q28295457-A460F691-0A1B-4E9E-84C0-47CCFF721FE7Q28323299-AEAD893F-2474-4F4C-96D6-2CDB3F9D1148Q30009100-EA42F82A-948B-4320-BA33-BDC57B876FB6Q30164075-4904A795-3EF6-4ACD-9C3B-FB42445FC110Q30165459-0804A5FD-8C90-45FE-8C2A-E72D729E3D40Q30341624-E12EF81A-9720-4A4F-A83E-680F3CD2D484Q30352514-DF7E23C9-E0B7-4AF1-93DC-816F008D78BDQ30352985-6AD3571C-8B8B-4C7E-BBF8-3038F5FE4143Q30362103-4CFE3A57-4571-459A-8B75-D8DB280C1BCAQ30368116-D57B89A6-B70C-4EC5-9A65-411E4798B128Q30975440-F5EA3373-BB86-4D42-829B-C5E3F625278AQ31990320-43472E5A-1E70-4E46-ACE3-11D65DDFD892Q33185120-60D3AD2B-F48A-4703-98B1-5A0DC65A5740Q33197925-AB07997E-4176-416A-BE50-FD163073079EQ33286794-D3CD178C-3FDF-458F-B96F-CF9A4FBF80F1Q33878446-41BF3B0B-FA7D-4E40-8B63-F60A060AFD07
P921
description
InterPro Family
@en
Proteinfamilie
@de
eiwitfamilie
@nl
famille InterPro
@fr
name
Acilfosfataza
@sh
Acilfosfataza
@sr
Acylphosphatase
@en
type
label
Acilfosfataza
@sh
Acilfosfataza
@sr
Acylphosphatase
@en
altLabel
1,3-diphosphoglycerate phosphatase
@en
Acylphosphatase
@en
IPR020456
@en
acetic phosphatase
@en
acetylphosphatase
@en
acylphosphate phosphohydrolase
@en
prefLabel
Acilfosfataza
@sh
Acilfosfataza
@sr
Acylphosphatase
@en